Recombined cells in the creation of the Dr. Brzostowski Hector Damian enzyme First to understand the basics to move to the understanding of how this enzyme. Defense mechanisms against aggression in immunity: According to WIKIPEDIA saving me write the whole rationale for the reader involved in the issue all are based on many books as WIKIPEDIA and finally presents the CRE "recombined cells Enzyme" .. . Microorganisms or toxins that get into an organism will encounter the cells and mechanisms of the innate immune system. The innate immune response is often triggered when microbes are identified by pattern recognition receptors that recognize components that are present in large groups of organisms, or when damaged cells, injured or stressed send alarm signals, many of which (but not all) are recognized by the same receptors that recognize pathogens. The germs that achieve penetrate a body will encounter the cells and mechanisms of the innate immune system. The innate immune defenses are non-specific, meaning these systems to recognize and respond to pathogens in a generic way. This system does not confer lasting immunity against the pathogen. The innate immune system is the dominant system of protection in the vast majority of organisms. Immunity: The innate immune system comprises the cells and mechanisms that defend the host from infection by other organisms, non-specifically. This means that the cells of the innate system recognize, and respond to pathogens in a generic way, unlike the adaptive immune system, it does not confer long-term immunity or protecting the host. The main functions of innate immune system in vertebrates include: Recruitment of immune cells to sites of infection and inflammation by producing chemical factors, specialized chemical mediators, called cytokines. Cascade activation of the complement system to identify bacteria, activate cells, and promote the clearance of dead cells or antibody complexes. The identification and removal of foreign substances present in organs, tissues, blood and lymph, by leukocytes. The activation of the adaptive immune system through a process known as antigen presentation. The major histocompatibility complex (MHC or MHC, English acronym for the major histocompatibility complex), or major histocompatibility complex, is a family of genes located on the short arm of chromosome 6 whose products are involved in antigen presentation to lymphocytes T. In humans, MHC genes constitute the so-called HLA (for human leukocyte antigen), because these proteins as antigens found on leukocytes, which could be detected with antibodies. The MHC genes are essential in the body's immune defense against pathogens, and on the other hand, constitute the main barrier to organ transplantation and stem cell. The region of the short arm of chromosome 6 containing MHC genes has information: • certain plasma membrane glycoproteins involved in the mechanisms of antigen processing and presentation to T cells: are grouped into the class II genes ( encoding proteins MHC-II) and the class I genes (encoding proteins MHC-I) • and cytokines and complement system proteins, which are important in the immune response, but have nothing to do with genes MHC, these genes are grouped in class III. Both types of molecules involved in the immune response, which allows the identification of the molecules themselves and odd (invasive), to eliminate the latter through different mechanisms. Location comparative genomic analysis of the organization of the MHC region between very distant species has revealed the presence of rearrangements within the region specific storyline and changes in the complexity of genes. The structure of the MHC region is known at least seven species of mammals Euterios (placental), two birds five teleost fish and sharks. There are great differences in the organization of the MHC region between eutherian mammals and non-mammals. In eutherians, the region is arranged along the chromosome in regions I-II-class III genes is very dense and occupies a large area. In non-mammalian MHC region generally contains less genes and Class I and II regions are adjacent, except teleosts, where the two regions are linked. MHC regions sequenced completely, the less complex the chicken, which contains only 19 genes in 92 kb. [1] In humans, 3.6 Mbp (3.6 million base pairs) in the MHC region of chromosome 6 contains 140 genes flanked by the genetic markers MOG and COL11A2. [2] The MHC region is the most dense and most polymorphic genes in the mammalian genome, critical for immunity and reproductive success. The MHC region in marsupials Monodelphis domestica (gray short-tailed Didelphimorphia) is flanked by the same markers, comprising 3.95 Mb and contains 114 genes, 87 shared with humans. [1] The comparison between the human MHC region and marsupials has possible to analyze the evolution of this set of genes, and that marsupials are among the eutherian and non-mammalian vertebrates, separated by 200 million years. Thus it has been identified that exhibit marsupials MHC region similar to mammals in size and complexity, but also has characteristics similar organization to the region of non-mammalian MHC, which reveals a likely ancestral organization of this region. MHC region is divided into 3 subgroups of genes: Structure of an MHC Class-I. MHC class-I In eutherian Class-I region contains a set of genes whose presence and order metópicos is conserved between species. These molecules are expressed in every human cell except red blood cells, germ cells, cells from pre-implantation embryos and syncytiotrophoblast (embryonic tissue, not present in postnatal life: details ...). [ 3] Some cells, such as neurons, monocytes and hepatocytes, have low levels of MHC-I molecules (less than 103 per cell: see data). [4] Genes-MHC Class I (MHC-I) encoded glycoproteins with immunoglobulin structure: feature type α heavy chain which is subdivided into three regions: α1, α2 and α3. These three regions are exposed to the extracellular space and are joined to the cell membrane by a transmembrane region. Α chain is always associated with β2 microglobulin molecule that is encoded by a separate region on chromosome 15. The main function of the gene products of the type-I is the intracellular presentation of antigenic peptides to cytotoxic T lymphocytes (CD8 +). The antigenic peptide is accommodated in a recess formed between the regions α1 and α2 of the heavy chain, while the MHC-I recognition by cytotoxic T lymphocyte is the α3 chain. In this cleft formed by the α1 and α2 regions are presented peptides 8 to 11 amino acids, which is why antigenic peptide presentation must go through a process of fragmentation within the cell that expresses itself. In humans, there are many isotypes (different genes) of the Class-I molecules, which can be grouped into: • "Classic", whose function is antigen presentation to CD8 + T lymphocytes: in this group have HLA-A , HLA-B and HLA-C. • "nonclassical" (also called MHC class IB), with specialized functions not present antigens to T cells, but which bind to inhibitory receptors of NK cells, within this group are HLA-E, HLA-F , HLA-G. Therefore HLA-G proteins are known immunosuppressive and are expressed in the fetal cytotrophoblast. This expression is thought to prevent the fetus is rejected as a transplant [1]. Structure of an MHC Class-II. MHC Class-II These genes encode glycoproteins with immunoglobulin structure, but in this case the functional complex is formed by two strings, one α and β (each with two domains, α1 and α2, β1 and β2). Each of the chains is linked to the membrane by a transmembrane region, and both strands are facing each other, with domains 1 and 2 adjacent to the cell exterior. [5] These molecules are expressed mainly in antigen presenting cells ( phagocytic dendritic and B cells) where they present processed antigen peptides extracellular helper T lymphocytes (CD4 +). The antigenic peptide is accommodated in a recess formed by the α1 and β1 domains, while the MHC-II Reconco by the T helper cell in the chain is β2. In this cleft formed by the regions α1 and β1, peptides are between 12 and 16 amino acids. MHC-II molecules present 5-6 isotypes in humans, and can be grouped into: • "classical" presenting peptides to CD4 T cells, within this group have HLA-DP, HLA-DQ, HLA-DR; • "nonclassical" accessory with intracellular functions (not exposed on the cell membrane, but in internal membranes of lysosomes) normally loaded antigenic peptides on MHC-II molecules classical ones in this group include HLA- HLA-DM and DO. In addition to the MHC-II molecules, the Class-II region are genes encoding antigen processing molecules, such as TAP (transporter by Associated with antigen processing) and Tapasin. MHC Class-III This class contains genes that encode secreted proteins that play several immune functions: complement system components (such as C2, C4, and factor B) and inflammation-related molecules (cytokines such as TNF-α, LTA, LTB) or heat shock proteins (hsp). Class-III has a completely different function-classes I and II, but is between the other two in the short arm of human chromosome 6, so they are often described together. Polymorphism of genes I and II MHC-codominant expression of the HLA / MHC. The MHC genes are expressed in a codominant. This means that the alleles (variants) inherited from both parents are expressed equivalently: • As there are three genes Class-I in humans called HLA-A, HLA-B and HLA-C, and each individual inherits a set of each parent, any cell of an individual may express 6 different types of MHC-I molecules. • In the locus of class-II, each individual inherits a pair of HLA-DP (DPA1 and DPA2, encoding the α and β chains), a pair of HLA-DQ (DQA1 and DQA2 to α chains and β), an HLA-DRα (DRA1) and one or two HLA-DRβ genes (DRB1 and DRB3, -4 or -5). Thus, an individual can inherit heterozygous 6 or 8 Class-II alleles, three or four from each parent. Game alleles present in each chromosome is called MHC haplotype. In humans, each HLA allele receives a number. For example, for a given individual, the haplotype HLA-A2 can be, HLA-B5, HLA-DR3, etc ... Each individual heterozygous MHC haplotypes have two, one on each chromosome (one paternal and one of maternal origin). MHC genes are highly polymorphic, which means that there are many different alleles in different individuals of the population. Polymorphism is so great that in a mixed population (not inbred) no two individuals have exactly the same set of genes and MHC molecules, except for identical twins. Polymorphic regions of each allele are in the zone of contact with the peptide to be presented to the lymphocyte. For this reason, the contact area of ​​each MHC allele is highly variable, since MHC polymorphic residues are specific slots in which it can be introduced only certain types of residue of the peptide, which imposes a binding mode very precise between the peptide and the MHC molecule. This implies that each variant of MHC molecule can bind specifically only those peptides that fit properly into the groove of the MHC molecule, which is variable for each allele. Thus, MHC molecules have a broad specificity for peptide binding, since each MHC molecule can bind many, but not all types of possible peptides. This is an essential feature of MHC molecules: a specific individual, a few molecules are enough different to be able to present a wide variety of peptides. On the other hand, within a population, the existence of multiple alleles ensures that there will always be some individual who possesses an MHC molecule capable of loading the appropriate peptide to recognize a microbe concreto.La MHC polymorphism evolution ensures that a population will be able to defend against the huge diversity of existing microbes and do not succumb to the presence of a new pathogen or pathogen mutated, because at least some individuals will be able to develop an adequate immune response to beat the pathogen. Variations in MHC sequences (polymorphism responsible) result from the inheritance of different MHC molecules, and are not induced by recombination, as with antigen receptors. Functions MHC-I and II molecules have two types of antigenic peptides to the T lymphocytes, responsible for the specific immune response to eliminate the pathogen responsible for the production of such antigens. However, MHC class-I and II correspond to two different pathways of antigen processing and are associated with two different immune defense systems: [5] Table 1. Characteristics of the antigen processing pathways Feature Milky Way MHC-II MHC-I Composition of stable peptide-MHC complex polymorphic α and β chains, peptide bound to both polymorphic α chain and β2 microglobulin, α chain bound peptide presenting cells Types antigen (APC) dendritic cells, mononuclear phagocytes, B lymphocytes, some endothelial cells, thymus epithelium Almost all nucleated cells T lymphocytes capable of responding T helper (CD4 +) cytotoxic T lymphocytes (CD8 +) Origin of antigenic proteins Proteins present in endosomes or lysosomes (mostly internalized the extracellular environment) cytosolic proteins (predominantly synthesized by the cell, can also enter through the outside phagosomes) enzymes responsible for the generation of peptides Proteases endosomes and lysosomes (as cathepsin ) The proteasome cytosolic site peptide loading onto the MHC molecule vesicular compartment specialized endoplasmic reticulum molecules involved in the transport and loading of peptides on MHC invariant chain, DM TAP (transporter Associated with antigen processing) T lymphocytes from an individual Specifically exhibit a property called MHC restriction: only detect an antigen if it is presented by an MHC molecule from the same individual. This is because each T cell has a dual specificity: the T cell receptor (called T cell receptor TCR) recognizes some residues of the peptide and simultaneously some residues of the MHC molecule which presents it. This property is very important in the transplantation of organs, and means that, during development, T cells must "learn" to recognize the individual's own MHC molecules, by the complex process of maturation and selection which takes place in the thymus. MHC molecules can only present peptides, implying that T cells, since they can only recognize antigen whether is associated to a MHC molecule can only react to antigens of protein origin (from microbes) and to no other chemical compound (or lipids, or nucleic acids or sugars). Each MHC molecule may have a single peptide at a time, since the cleavage of the molecule only has space to accommodate a peptide. However, a given MHC molecule has a broad specificity, because many different peptides can have (but not all). Peptide processing associated with MHC-I molecules: proteins present in the cytosol are degraded by the proteasome, and the resulting peptides are internalized by the TAP channel in the endoplasmic reticulum, where they associate with newly synthesized molecules of MHC-I. The peptide-MHC-I pass the Golgi apparatus, where they are glycosylated, and then to secretory vesicles that fuse with the cell membrane, so that the complexes are exposed to the outside, allowing contact with T cells circulating. MHC peptide presenting acquired outside of the cell membrane during its own biosynthesis, within the cell. Therefore, the peptides presented by MHC molecules are derived from microbes inside the cell, and this is the reason why the T lymphocytes, identified only when associated peptides to MHC molecules, only detect microbes and cell associated trigger an immune response against intracellular microbes. It is noteworthy that MHC-I molecules acquire peptides derived cytosolic proteins, whereas MHC-II molecules acquire peptides of proteins in intracellular vesicles. Therefore, MHC-I molecules present self peptides, viral peptides (synthesized by the cell itself) or peptides derived from ingested microbes in phagosomes. MHC-II molecules, in turn, present peptides derived from ingested microbes in vesicles (such molecules are only expressed in phagocytic cells). MHC molecules are only expressed stably in the cell membrane if they have a charged peptide, the presence of peptide stabilizes the structure of MHC molecules, the "empty" molecules are degraded within the cell. MHC molecules loaded with a peptide may remain in the membrane for days, long enough to ensure that an appropriate T cell recognizes the complex and initiate the immune response. In each individual MHC molecules can present both foreign peptides (from pathogens) and peptides derived from the individual's own proteins. This implies that, at any given time, only a small proportion of MHC molecules from a cell present a foreign peptide: the majority of peptides that will present themselves, since they are more abundant. However, T lymphocytes are capable of detecting a peptide presented by only 0.1% -1% of MHC molecules for triggering an immune response. The peptides themselves, moreover, can not initiate an immune response (except in cases of autoimmune diseases), because the T cells specific for self-antigens are destroyed or inactivated in the thymus. However, the presence of self peptides associated with the MHC molecules is essential for the supervisory function of T cells: These cells are constantly patrol the body, verifying the presence of self peptides associated with MHC molecules and triggering an immune response in the rare cases that detect a foreign peptide. MHC molecules in transplant rejection MHC molecules were identified and named specifically for their role in transplant rejection among different strains of inbred mice. In humans, MHC molecules are leukocyte antigens (HLA). It took more than 20 years to understand the physiologic function of MHC molecules in the presentation of peptides to T cells [6] As described above, each human cell expressing MHC class alleles 6-I (allele HLA-A, -B and-C of each parent) and 6-8 alleles MHC class-2 (one-DP and HLA-DQ, and one or two of HLA-DR from each parent, and some combinations of these). The polymorphism of MHC genes is very high: it is estimated that the population there are at least 350 alleles of HLA-A, 620 HLA-B, DR alleles yy 400 90 DQ alleles. As these alleles can be inherited and expressed in many different combinations, each individual likely express some molecules will differ from the other individual molecules, except identical twins. All MHC molecules can be targets of transplant rejection, but HLA-DP and HLA-C have a low polymorphism, and probably are of minor importance in rejections. In the case of a transplant (organ or stem cells), HLA molecules serve as antigens: can trigger an immune response in the recipient, leading to graft rejection. Recognition of MHC antigens on cells from another individual is one of the strongest immune responses known. The reason that people react against another individual MHC molecules are fairly well understood. During maturation of T lymphocytes, they are chosen based on their ability to recognize TCR complexes weakly "self peptide: self MHC." Therefore, in principle, T cells should not react to a complex "foreign peptide: MHC strange", which is what will appear in the transplanted cells. However, it seems that what is happening is a kind of cross-reaction: the individual T cell receptor can be wrong, because the donor's MHC molecule is similar to that employed in the TCR binding region (variable region of the MHC is in the presenting peptide binding). For this reason, the receiving individual lymphocytes interpret the complex present in the cells of the transplanted organ as "foreign peptide: MHC self" and trigger an immune response against the body "invader", because it is perceived in the same way that a fabric itself infected or tumor, but with a much higher number of complexes capable of initiating a response. The recognition of foreign MHC molecule as self by T lymphocytes called allorecognition. There are two possible types of transplant rejection mediated by MHC molecules (HLA): • hyperacute rejection: occurs when the individual recipient has preformed anti-HLA antibodies before transplantation, which may be due to the prior blood transfusions ( including donor lymphocytes with HLA molecules), the generation of anti-HLA during pregnancy (the father against HLA present in the fetus) and the completion of a previous transplant; • acute humoral rejection and chronic organ dysfunction transplant: due to the formation of anti-HLA antibodies in the recipient against HLA molecules present on endothelial cells transplantation. In both cases, there is an immune reaction against the transplanted organ, can generate injuries in the same, leading to loss of function, the first case immediate and progressive in the second. For this reason, it is essential to perform a cross-reaction between donor cells and recipient's serum for the presence of anti-HLA antibodies in the recipient preformed against donor HLA molecules and prevent hyperacute rejection. Normally, it is checked the compatibility of the HLA-A,-B and-DR: as the number of inconsistencies, the 5-year survival decreases transplantation. Full compatibility exists only between identical twins, but now there are databases of donors worldwide to optimize HLA compatibility between a potential donor and recipient. Antibody From Wikipedia, the free encyclopedia Jump to: navigation, search good immunoglobulin molecule with typical Y-shaped In blue were observed four heavy chain Ig domains, whereas green light chains are shown. Between the stem (Fraction constant Fc) and branches (Fab) there is a thinner portion called "hinge region" (hinge). Antibody (also known as immunoglobulins, abbreviated Ig) are glycoproteins gamma globulin type. Can be found in soluble form in the blood or other bodily fluids of vertebrates, having an identical shape which acts as B cell receptor and are employed by the immune system to identify and neutralize foreign elements such as bacteria, viruses or parasites. [1] The typical antibody is comprised of basic structural units, each with two large heavy chains and two light chains of smaller size that formed, for example, monomers with a unit, two units dimers or pentamers with five units . Antibodies are synthesized by a type of white blood cell called B lymphocyte There are different types of antibody isotypes, based on how heavy chain held. Five different classes are known in mammals isotypes play different roles, helping to direct the appropriate immune response for each different type of foreign object they encounter. [2] Although the general structure of all antibodies is very similar, a small region of apex of the protein is extremely variable, allowing the existence of millions of antibodies, each with a slightly different end. This part of the protein is known as hypervariable region. Each of these variants can be attached to a "target" other, which is what is known as an antigen. [3] This huge diversity of antibodies enables the immune system to recognize a variety of antigens equally high. The only part of the antigen recognized by the antibody is called epitope. These epitopes bind with its antibody in a highly specific interaction is called induced adaptation that allows the antibodies to identify and bind only their unique antigen among the millions of different molecules that make up an organism. The recognition of an antigen by an antibody it for attack by other parts of the immune system. The antibodies may also neutralize targets directly by, for example, binding to a portion of a pathogen necessary for it to cause an infection. The large population of antibody diversity is generated by random combinations of a set of different gene segments encoding the antigen-binding sites (or paratopes), which subsequently undergo random mutations in this region of the antibody gene, which results in a even greater diversity. [2] [4] The antibody genes are also rearranged in a process known as immunoglobulin class switching that changes the base of the heavy chain to another, creating a different antibody isotype that holds the variable region specific to the target antigen. This allows a single antibody can be used for different parts of the immune system. The production of antibodies is the main function of the humoral immune system. [5] The antigen-antibody (Ag-Ab) is one of the cornerstones in the human body's immune response. The term refers to specific binding of an antibody with an antigen for inhibiting or slowing its toxicity. The structural connection between the macromolecules is performed through several weak forces which decrease with distance, such as hydrogen bonding, the Van Der Waals forces, electrostatic interactions and hydrophobic. Ag-Ab recognition is a complementary reaction therefore takes place through multiple noncovalent bonds between a portion of the amino acid antigen and antibody binding site. The reaction is characterized by its specificity, speed, spontaneity and reversibility. Contents [hide] 1 Features ◦ ◾ ◾ 1.2 Speed ​​1.1 Specificity ◾ ◾ 1.4 1.3 Spontaneity Reversibility Specificity Characteristics antibody capacity to bind antigen that stimulated through the epitope or antigenic determinant by weak intermolecular bonds. The binding specificity is given by very precise and to distinguish between chemical groups with minimal differences despite their similarity, and allows the arrest of a single antigen in question. The speed quickly happens the first stage of the Ag-Ab reaction is of the order of milliseconds, and is limited only by diffusion. The second stage, which is longer includes all manifestations that occur as a result of the interaction, such as precipitation, agglutination, neutralization, etc.. Spontaneity Ag-Ab reaction requires no additional energy to be made. Since the reaction reversibility is due to non-covalent forces, is reversible and, therefore, is affected by factors such as temperature, the ratio of Ag-Ac, pH and ionic strength. Symptoms substance or element causing said reaction is called an allergen, and are defined as symptoms caused allergic reactions. When an allergen enters the body of a subject who is allergic to it, their immune system responds by producing a large amount of antibodies called IgE. The subsequent exposure to the allergen causes the release of chemical mediators, including histamine, which produce the typical symptoms of the allergic reaction. Immune system From Wikipedia, the free encyclopedia Jump to: navigation, search good immune system Neutrophil Neutrophil with anthrax copy.jpg (yellow) ingested by phagocytosis of anthrax bacteria (Naraja). The image corresponds to a scanning electron microscope. The white line corresponds to 5 microns. Protection function of an organism to external agents. Basic structures Synonyms White blood leukocytes or immune system Immune System An immune system, immune system or immune system (from the Latin in-mūn (itātem) 'no obligation' cient. 'Immunity' and the Greek syn σύν 'with', 'union ',' system ',' set ') is the set of biological structures and processes within an organism that protects against disease by identifying and killing pathogens and cancerous cells. [1] detects a wide variety of agents, from viruses to intestinal parasites, [2] [3] and needs to distinguish them from their own cells and tissues of the body to function properly. The immune system is mainly composed of leukocytes (lymphocytes, [4] other leukocytes, [5] antibody [6] T cells [7], cytokines [7] macrophages [7], neutrophils [7] among other components that help your operation). [7] Detection is complicated as pathogens can evolve rapidly, producing adaptations that avoid the immune system and allow the pathogens to successfully infect their guests. [8] To overcome this challenge, multiple mechanisms evolved that recognize and neutralize pathogens. Even simple unicellular organisms such as bacteria possess enzyme systems that protect against viral infections. Other basic immune mechanisms evolved in ancient eukaryotes and remain in their modern descendants, such as plants, fish, reptiles and insects. These mechanisms include antimicrobial peptides called defensins, [9] the phagocytosis and the complement system. Vertebrates, including humans, have defense mechanisms even more sophisticated. [10] The vertebrate immune systems consist of many types of proteins, cells, organs and tissues, which interact in an elaborate and dynamic network. As part of this more complex immune response, the human immune system adapts over time to recognize specific pathogens more efficiently. In this adaptation process is called "adaptive immunity" or "acquired immunity" able to create an immunological memory. [11] Immunological memory created from a primary response to a specific pathogen, provides an enhanced response to secondary encounters with that same specific pathogen. This process of acquired immunity is based on vaccination. The immune system disorders can cause diseases. Immunodeficiency occurs when the immune system is less active than normal, [12] resulting in recurrent infections and life-threatening. Immunodeficiency can result from a genetic disease, such as severe combined immunodeficiency, [13] or be caused by drugs or infections, such as acquired immunodeficiency syndrome (AIDS) is caused by the retrovirus HIV. [14] contrast, autoimmune diseases result from an overactive immune system attacking normal tissues as if they were foreign organisms. Among the common autoimmune diseases include Hashimoto's thyroiditis, rheumatoid arthritis, diabetes mellitus type 1 and lupus erythematosus. Immunology covers the study of all aspects of the immune system that have significant relevance to human health and disease. It is expected that further research in this area plays a serious role in the promotion of health and treatment of diseases. Immunoassay From Wikipedia, the free encyclopedia Jump to: navigation, search Immunoassay is a set of analytical laboratory immunochemical techniques have in common using immune complexes, ie resulting from the conjugation of antibodies and antigens, as references of quantification of an analyte (the substance under analysis) determined, which can be the antibody (Ab) or antigen (Ag), using the measurement as a marker molecule that is part of the reaction with the immune complex in the test or chemical assay. The technique is based on the high specificity and affinity of antibodies for their specific antigens and used monoclonal antibodies (obtained in the laboratory) or polyclonal sera (obtained from animals), being more specific monoclonals. Its high sensitivity and specificity allows the quantification of organic compounds present in liquids in low concentration in the nanogram / ml or picogram / ml. The development of immunoassay has had great impact in the field of medical diagnosis by laboratory tests or clinical chemistry. For the measurement technique ◦ Competitive: the antigen (Ag) to be measured competes with labeled antigen for antibody (Ab). Is measured by the amount of labeled antigen which is considered unconjugated is inversely proportional to the analyte. ◦ not competitive (also called sandwich) the Ag in the sample reacts with two different Ac which bind to different parts of Ag. Ac one is generally solid support to facilitate separation of the bound fraction, and the other is marked Ac. Is measured by the amount of marker which is considered directly proportional to the amount of analyte. The medium where the measurement is made ◦ Homogeneous: In this type of test signal generated by the binding of antigen and antibody is measured directly in the same medium that is used to enhance the formation of the immune complex. Heterogeneous ◦: In this type of test signal generated by the binding of antigen and antibody is measured by a different means than that used for immune complex binding, generally involve an intermediate step of washing to remove interference. Is considered homogeneous immunoassays noncompetitive format are most sensitive and specific. ◦ marker by Radioimmunoassay (RIA): The label is a radioactive isotope. ◦ Enzimoinmunoanálsis (EIA): the label is an enzyme such as enzyme immunoassay technique known by the abbreviation ELISA. ◦ fluoroimmunoassay: the marker is a fluorescent molecule, such FPIA. ◦ Test Inmunoquimioluminiscente: the brand is generally an enzyme capable of catalyzing a chemiluminescent reaction. Are equally or more sensitive than radioimmunoassay, and no risk of handling radioactive substances. In contrast are underdeveloped and can not always be applied. ◦ Uses Measuring hormone levels: for example measuring levels of thyroid hormones or estrogen ◦ Measuring serum metabolites whose amount or presence is evidence of cell damage: eg measuring myocardial biomarkers such as troponins ◦ Detection viruses: for example, the cause of hepatitis and their identification ◦ detection of cancer or tumor cells: through its proteins and tumor markers released into the serum of patients. ◦ Detecting exposure to infectious agents: for example rubella or toxoplasmosis in pregnant or immunosuppressed people. Detection of metabolites ◦ indicators physiological problems, by its presence or excess amount in blood, for example in case of anemia measured ferritin levels. ◦ Measure levels of medications, drugs of abuse and blood toxins. CRE: Unable to disclose their production in vitro thus protecting the IP patentable applies and results from Dr. Brzostowski SA Laboratory, and used in the care of various rheumatic diseases, raising the natural defenses and health restructuring, starting the research into the functioning of the pancreas and cure of Diabetes, rejuvenating our body cells.

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Defense mechanisms against aggression in immunity: According to WIKIPEDIA saving me write the whole rationale for the reader involved in the issue all are based on many books as WIKIPEDIA and finally presents the CRE "recombined cells Enzyme" .. . Microorganisms or toxins that get into an organism will encounter the cells and mechanisms of the innate immune system. The innate immune response is often triggered when microbes are identified by pattern recognition receptors that recognize components that are present in large groups of organisms, or when damaged cells, injured or stressed send alarm signals, many of which (but not all) are recognized by the same receptors that recognize pathogens. The germs that achieve penetrate a body will encounter the cells and mechanisms of the innate immune system. The innate immune defenses are non-specific, meaning these systems to recognize and respond to pathogens in a generic way. This system does not confer lasting immunity against the pathogen. The innate immune system is the dominant system of protection in the vast majority of organisms. Immunity: The innate immune system comprises the cells and mechanisms that defend the host from infection by other organisms, non-specifically. This means that the cells of the innate system recognize, and respond to pathogens in a generic way, unlike the adaptive immune system, it does not confer long-term immunity or protecting the host. The main functions of innate immune system in vertebrates include: Recruitment of immune cells to sites of infection and inflammation by producing chemical factors, specialized chemical mediators, called cytokines. Cascade activation of the complement system to identify bacteria, activate cells, and promote the clearance of dead cells or antibody complexes. The identification and removal of foreign substances present in organs, tissues, blood and lymph, by leukocytes. The activation of the adaptive immune system through a process known as antigen presentation. The major histocompatibility complex (MHC or MHC, English acronym for the major histocompatibility complex), or major histocompatibility complex, is a family of genes located on the short arm of chromosome 6 whose products are involved in antigen presentation to lymphocytes T. In humans, MHC genes constitute the so-called HLA (for human leukocyte antigen), because these proteins as antigens found on leukocytes, which could be detected with antibodies. The MHC genes are essential in the body's immune defense against pathogens, and on the other hand, constitute the main barrier to organ transplantation and stem cell. The region of the short arm of chromosome 6 containing MHC genes has information: • certain plasma membrane glycoproteins involved in the mechanisms of antigen processing and presentation to T cells: are grouped into the class II genes ( encoding proteins MHC-II) and the class I genes (encoding proteins MHC-I) • and cytokines and complement system proteins, which are important in the immune response, but have nothing to do with genes MHC, these genes are grouped in class III. Both types of molecules involved in the immune response, which allows the identification of the molecules themselves and odd (invasive), to eliminate the latter through different mechanisms. Location comparative genomic analysis of the organization of the MHC region between very distant species has revealed the presence of rearrangements within the region specific storyline and changes in the complexity of genes. The structure of the MHC region is known at least seven species of mammals Euterios (placental), two birds five teleost fish and sharks. There are great differences in the organization of the MHC region between eutherian mammals and non-mammals. In eutherians, the region is arranged along the chromosome in regions I-II-class III genes is very dense and occupies a large area. In non-mammalian MHC region generally contains less genes and Class I and II regions are adjacent, except teleosts, where the two regions are linked. MHC regions sequenced completely, the less complex the chicken, which contains only 19 genes in 92 kb. [1] In humans, 3.6 Mbp (3.6 million base pairs) in the MHC region of chromosome 6 contains 140 genes flanked by the genetic markers MOG and COL11A2. [2] The MHC region is the most dense and most polymorphic genes in the mammalian genome, critical for immunity and reproductive success. The MHC region in marsupials Monodelphis domestica (gray short-tailed Didelphimorphia) is flanked by the same markers, comprising 3.95 Mb and contains 114 genes, 87 shared with humans. [1] The comparison between the human MHC region and marsupials has possible to analyze the evolution of this set of genes, and that marsupials are among the eutherian and non-mammalian vertebrates, separated by 200 million years. Thus it has been identified that exhibit marsupials MHC region similar to mammals in size and complexity, but also has characteristics similar organization to the region of non-mammalian MHC, which reveals a likely ancestral organization of this region. MHC region is divided into 3 subgroups of genes: Structure of an MHC Class-I. MHC class-I In eutherian Class-I region contains a set of genes whose presence and order metópicos is conserved between species. These molecules are expressed in every human cell except red blood cells, germ cells, cells from pre-implantation embryos and syncytiotrophoblast (embryonic tissue, not present in postnatal life: details ...). [ 3] Some cells, such as neurons, monocytes and hepatocytes, have low levels of MHC-I molecules (less than 103 per cell: see data). [4] Genes-MHC Class I (MHC-I) encoded glycoproteins with immunoglobulin structure: feature type α heavy chain which is subdivided into three regions: α1, α2 and α3. These three regions are exposed to the extracellular space and are joined to the cell membrane by a transmembrane region. Α chain is always associated with β2 microglobulin molecule that is encoded by a separate region on chromosome 15. The main function of the gene products of the type-I is the intracellular presentation of antigenic peptides to cytotoxic T lymphocytes (CD8 +). The antigenic peptide is accommodated in a recess formed between the regions α1 and α2 of the heavy chain, while the MHC-I recognition by cytotoxic T lymphocyte is the α3 chain. In this cleft formed by the α1 and α2 regions are presented peptides 8 to 11 amino acids, which is why antigenic peptide presentation must go through a process of fragmentation within the cell that expresses itself. In humans, there are many isotypes (different genes) of the Class-I molecules, which can be grouped into: • "Classic", whose function is antigen presentation to CD8 + T lymphocytes: in this group have HLA-A , HLA-B and HLA-C. • "nonclassical" (also called MHC class IB), with specialized functions not present antigens to T cells, but which bind to inhibitory receptors of NK cells, within this group are HLA-E, HLA-F , HLA-G. Therefore HLA-G proteins are known immunosuppressive and are expressed in the fetal cytotrophoblast. This expression is thought to prevent the fetus is rejected as a transplant [1]. Structure of an MHC Class-II. MHC Class-II These genes encode glycoproteins with immunoglobulin structure, but in this case the functional complex is formed by two strings, one α and β (each with two domains, α1 and α2, β1 and β2). Each of the chains is linked to the membrane by a transmembrane region, and both strands are facing each other, with domains 1 and 2 adjacent to the cell exterior. [5] These molecules are expressed mainly in antigen presenting cells ( phagocytic dendritic and B cells) where they present processed antigen peptides extracellular helper T lymphocytes (CD4 +). The antigenic peptide is accommodated in a recess formed by the α1 and β1 domains, while the MHC-II Reconco by the T helper cell in the chain is β2. In this cleft formed by the regions α1 and β1, peptides are between 12 and 16 amino acids. MHC-II molecules present 5-6 isotypes in humans, and can be grouped into: • "classical" presenting peptides to CD4 T cells, within this group have HLA-DP, HLA-DQ, HLA-DR; • "nonclassical" accessory with intracellular functions (not exposed on the cell membrane, but in internal membranes of lysosomes) normally loaded antigenic peptides on MHC-II molecules classical ones in this group include HLA- HLA-DM and DO. In addition to the MHC-II molecules, the Class-II region are genes encoding antigen processing molecules, such as TAP (transporter by Associated with antigen processing) and Tapasin. MHC Class-III This class contains genes that encode secreted proteins that play several immune functions: complement system components (such as C2, C4, and factor B) and inflammation-related molecules (cytokines such as TNF-α, LTA, LTB) or heat shock proteins (hsp). Class-III has a completely different function-classes I and II, but is between the other two in the short arm of human chromosome 6, so they are often described together. Polymorphism of genes I and II MHC-codominant expression of the HLA / MHC. The MHC genes are expressed in a codominant. This means that the alleles (variants) inherited from both parents are expressed equivalently: • As there are three genes Class-I in humans called HLA-A, HLA-B and HLA-C, and each individual inherits a set of each parent, any cell of an individual may express 6 different types of MHC-I molecules. • In the locus of class-II, each individual inherits a pair of HLA-DP (DPA1 and DPA2, encoding the α and β chains), a pair of HLA-DQ (DQA1 and DQA2 to α chains and β), an HLA-DRα (DRA1) and one or two HLA-DRβ genes (DRB1 and DRB3, -4 or -5). Thus, an individual can inherit heterozygous 6 or 8 Class-II alleles, three or four from each parent. Game alleles present in each chromosome is called MHC haplotype. In humans, each HLA allele receives a number. For example, for a given individual, the haplotype HLA-A2 can be, HLA-B5, HLA-DR3, etc ... Each individual heterozygous MHC haplotypes have two, one on each chromosome (one paternal and one of maternal origin). MHC genes are highly polymorphic, which means that there are many different alleles in different individuals of the population. Polymorphism is so great that in a mixed population (not inbred) no two individuals have exactly the same set of genes and MHC molecules, except for identical twins. Polymorphic regions of each allele are in the zone of contact with the peptide to be presented to the lymphocyte. For this reason, the contact area of ​​each MHC allele is highly variable, since MHC polymorphic residues are specific slots in which it can be introduced only certain types of residue of the peptide, which imposes a binding mode very precise between the peptide and the MHC molecule. This implies that each variant of MHC molecule can bind specifically only those peptides that fit properly into the groove of the MHC molecule, which is variable for each allele. Thus, MHC molecules have a broad specificity for peptide binding, since each MHC molecule can bind many, but not all types of possible peptides. This is an essential feature of MHC molecules: a specific individual, a few molecules are enough different to be able to present a wide variety of peptides. On the other hand, within a population, the existence of multiple alleles ensures that there will always be some individual who possesses an MHC molecule capable of loading the appropriate peptide to recognize a microbe concreto.La MHC polymorphism evolution ensures that a population will be able to defend against the huge diversity of existing microbes and do not succumb to the presence of a new pathogen or pathogen mutated, because at least some individuals will be able to develop an adequate immune response to beat the pathogen. Variations in MHC sequences (polymorphism responsible) result from the inheritance of different MHC molecules, and are not induced by recombination, as with antigen receptors. Functions MHC-I and II molecules have two types of antigenic peptides to the T lymphocytes, responsible for the specific immune response to eliminate the pathogen responsible for the production of such antigens. However, MHC class-I and II correspond to two different pathways of antigen processing and are associated with two different immune defense systems: [5] Table 1. Characteristics of the antigen processing pathways Feature Milky Way MHC-II MHC-I Composition of stable peptide-MHC complex polymorphic α and β chains, peptide bound to both polymorphic α chain and β2 microglobulin, α chain bound peptide presenting cells Types antigen (APC) dendritic cells, mononuclear phagocytes, B lymphocytes, some endothelial cells, thymus epithelium Almost all nucleated cells T lymphocytes capable of responding T helper (CD4 +) cytotoxic T lymphocytes (CD8 +) Origin of antigenic proteins Proteins present in endosomes or lysosomes (mostly internalized the extracellular environment) cytosolic proteins (predominantly synthesized by the cell, can also enter through the outside phagosomes) enzymes responsible for the generation of peptides Proteases endosomes and lysosomes (as cathepsin ) The proteasome cytosolic site peptide loading onto the MHC molecule vesicular compartment specialized endoplasmic reticulum molecules involved in the transport and loading of peptides on MHC invariant chain, DM TAP (transporter Associated with antigen processing) T lymphocytes from an individual Specifically exhibit a property called MHC restriction: only detect an antigen if it is presented by an MHC molecule from the same individual. This is because each T cell has a dual specificity: the T cell receptor (called T cell receptor TCR) recognizes some residues of the peptide and simultaneously some residues of the MHC molecule which presents it. This property is very important in the transplantation of organs, and means that, during development, T cells must "learn" to recognize the individual's own MHC molecules, by the complex process of maturation and selection which takes place in the thymus. MHC molecules can only present peptides, implying that T cells, since they can only recognize antigen whether is associated to a MHC molecule can only react to antigens of protein origin (from microbes) and to no other chemical compound (or lipids, or nucleic acids or sugars). Each MHC molecule may have a single peptide at a time, since the cleavage of the molecule only has space to accommodate a peptide. However, a given MHC molecule has a broad specificity, because many different peptides can have (but not all). Peptide processing associated with MHC-I molecules: proteins present in the cytosol are degraded by the proteasome, and the resulting peptides are internalized by the TAP channel in the endoplasmic reticulum, where they associate with newly synthesized molecules of MHC-I. The peptide-MHC-I pass the Golgi apparatus, where they are glycosylated, and then to secretory vesicles that fuse with the cell membrane, so that the complexes are exposed to the outside, allowing contact with T cells circulating. MHC peptide presenting acquired outside of the cell membrane during its own biosynthesis, within the cell. Therefore, the peptides presented by MHC molecules are derived from microbes inside the cell, and this is the reason why the T lymphocytes, identified only when associated peptides to MHC molecules, only detect microbes and cell associated trigger an immune response against intracellular microbes. It is noteworthy that MHC-I molecules acquire peptides derived cytosolic proteins, whereas MHC-II molecules acquire peptides of proteins in intracellular vesicles. Therefore, MHC-I molecules present self peptides, viral peptides (synthesized by the cell itself) or peptides derived from ingested microbes in phagosomes. MHC-II molecules, in turn, present peptides derived from ingested microbes in vesicles (such molecules are only expressed in phagocytic cells). MHC molecules are only expressed stably in the cell membrane if they have a charged peptide, the presence of peptide stabilizes the structure of MHC molecules, the "empty" molecules are degraded within the cell. MHC molecules loaded with a peptide may remain in the membrane for days, long enough to ensure that an appropriate T cell recognizes the complex and initiate the immune response. In each individual MHC molecules can present both foreign peptides (from pathogens) and peptides derived from the individual's own proteins. This implies that, at any given time, only a small proportion of MHC molecules from a cell present a foreign peptide: the majority of peptides that will present themselves, since they are more abundant. However, T lymphocytes are capable of detecting a peptide presented by only 0.1% -1% of MHC molecules for triggering an immune response. The peptides themselves, moreover, can not initiate an immune response (except in cases of autoimmune diseases), because the T cells specific for self-antigens are destroyed or inactivated in the thymus. However, the presence of self peptides associated with the MHC molecules is essential for the supervisory function of T cells: These cells are constantly patrol the body, verifying the presence of self peptides associated with MHC molecules and triggering an immune response in the rare cases that detect a foreign peptide. MHC molecules in transplant rejection MHC molecules were identified and named specifically for their role in transplant rejection among different strains of inbred mice. In humans, MHC molecules are leukocyte antigens (HLA). It took more than 20 years to understand the physiologic function of MHC molecules in the presentation of peptides to T cells [6] As described above, each human cell expressing MHC class alleles 6-I (allele HLA-A, -B and-C of each parent) and 6-8 alleles MHC class-2 (one-DP and HLA-DQ, and one or two of HLA-DR from each parent, and some combinations of these). The polymorphism of MHC genes is very high: it is estimated that the population there are at least 350 alleles of HLA-A, 620 HLA-B, DR alleles yy 400 90 DQ alleles. As these alleles can be inherited and expressed in many different combinations, each individual likely express some molecules will differ from the other individual molecules, except identical twins. All MHC molecules can be targets of transplant rejection, but HLA-DP and HLA-C have a low polymorphism, and probably are of minor importance in rejections. In the case of a transplant (organ or stem cells), HLA molecules serve as antigens: can trigger an immune response in the recipient, leading to graft rejection. Recognition of MHC antigens on cells from another individual is one of the strongest immune responses known. The reason that people react against another individual MHC molecules are fairly well understood. During maturation of T lymphocytes, they are chosen based on their ability to recognize TCR complexes weakly "self peptide: self MHC." Therefore, in principle, T cells should not react to a complex "foreign peptide: MHC strange", which is what will appear in the transplanted cells. However, it seems that what is happening is a kind of cross-reaction: the individual T cell receptor can be wrong, because the donor's MHC molecule is similar to that employed in the TCR binding region (variable region of the MHC is in the presenting peptide binding). For this reason, the receiving individual lymphocytes interpret the complex present in the cells of the transplanted organ as "foreign peptide: MHC self" and trigger an immune response against the body "invader", because it is perceived in the same way that a fabric itself infected or tumor, but with a much higher number of complexes capable of initiating a response. The recognition of foreign MHC molecule as self by T lymphocytes called allorecognition. There are two possible types of transplant rejection mediated by MHC molecules (HLA): • hyperacute rejection: occurs when the individual recipient has preformed anti-HLA antibodies before transplantation, which may be due to the prior blood transfusions ( including donor lymphocytes with HLA molecules), the generation of anti-HLA during pregnancy (the father against HLA present in the fetus) and the completion of a previous transplant; • acute humoral rejection and chronic organ dysfunction transplant: due to the formation of anti-HLA antibodies in the recipient against HLA molecules present on endothelial cells transplantation. In both cases, there is an immune reaction against the transplanted organ, can generate injuries in the same, leading to loss of function, the first case immediate and progressive in the second. For this reason, it is essential to perform a cross-reaction between donor cells and recipient's serum for the presence of anti-HLA antibodies in the recipient preformed against donor HLA molecules and prevent hyperacute rejection. Normally, it is checked the compatibility of the HLA-A,-B and-DR: as the number of inconsistencies, the 5-year survival decreases transplantation. Full compatibility exists only between identical twins, but now there are databases of donors worldwide to optimize HLA compatibility between a potential donor and recipient. Antibody From Wikipedia, the free encyclopedia Jump to: navigation, search good immunoglobulin molecule with typical Y-shaped In blue were observed four heavy chain Ig domains, whereas green light chains are shown. Between the stem (Fraction constant Fc) and branches (Fab) there is a thinner portion called "hinge region" (hinge). Antibody (also known as immunoglobulins, abbreviated Ig) are glycoproteins gamma globulin type. Can be found in soluble form in the blood or other bodily fluids of vertebrates, having an identical shape which acts as B cell receptor and are employed by the immune system to identify and neutralize foreign elements such as bacteria, viruses or parasites. [1] The typical antibody is comprised of basic structural units, each with two large heavy chains and two light chains of smaller size that formed, for example, monomers with a unit, two units dimers or pentamers with five units . Antibodies are synthesized by a type of white blood cell called B lymphocyte There are different types of antibody isotypes, based on how heavy chain held. Five different classes are known in mammals isotypes play different roles, helping to direct the appropriate immune response for each different type of foreign object they encounter. [2] Although the general structure of all antibodies is very similar, a small region of apex of the protein is extremely variable, allowing the existence of millions of antibodies, each with a slightly different end. This part of the protein is known as hypervariable region. Each of these variants can be attached to a "target" other, which is what is known as an antigen. [3] This huge diversity of antibodies enables the immune system to recognize a variety of antigens equally high. The only part of the antigen recognized by the antibody is called epitope. These epitopes bind with its antibody in a highly specific interaction is called induced adaptation that allows the antibodies to identify and bind only their unique antigen among the millions of different molecules that make up an organism. The recognition of an antigen by an antibody it for attack by other parts of the immune system. The antibodies may also neutralize targets directly by, for example, binding to a portion of a pathogen necessary for it to cause an infection. The large population of antibody diversity is generated by random combinations of a set of different gene segments encoding the antigen-binding sites (or paratopes), which subsequently undergo random mutations in this region of the antibody gene, which results in a even greater diversity. [2] [4] The antibody genes are also rearranged in a process known as immunoglobulin class switching that changes the base of the heavy chain to another, creating a different antibody isotype that holds the variable region specific to the target antigen. This allows a single antibody can be used for different parts of the immune system. The production of antibodies is the main function of the humoral immune system. [5] The antigen-antibody (Ag-Ab) is one of the cornerstones in the human body's immune response. The term refers to specific binding of an antibody with an antigen for inhibiting or slowing its toxicity. The structural connection between the macromolecules is performed through several weak forces which decrease with distance, such as hydrogen bonding, the Van Der Waals forces, electrostatic interactions and hydrophobic. Ag-Ab recognition is a complementary reaction therefore takes place through multiple noncovalent bonds between a portion of the amino acid antigen and antibody binding site. The reaction is characterized by its specificity, speed, spontaneity and reversibility. Contents [hide] 1 Features ◦ ◾ ◾ 1.2 Speed ​​1.1 Specificity ◾ ◾ 1.4 1.3 Spontaneity Reversibility Specificity Characteristics antibody capacity to bind antigen that stimulated through the epitope or antigenic determinant by weak intermolecular bonds. The binding specificity is given by very precise and to distinguish between chemical groups with minimal differences despite their similarity, and allows the arrest of a single antigen in question. The speed quickly happens the first stage of the Ag-Ab reaction is of the order of milliseconds, and is limited only by diffusion. The second stage, which is longer includes all manifestations that occur as a result of the interaction, such as precipitation, agglutination, neutralization, etc.. Spontaneity Ag-Ab reaction requires no additional energy to be made. Since the reaction reversibility is due to non-covalent forces, is reversible and, therefore, is affected by factors such as temperature, the ratio of Ag-Ac, pH and ionic strength. Symptoms substance or element causing said reaction is called an allergen, and are defined as symptoms caused allergic reactions. When an allergen enters the body of a subject who is allergic to it, their immune system responds by producing a large amount of antibodies called IgE. The subsequent exposure to the allergen causes the release of chemical mediators, including histamine, which produce the typical symptoms of the allergic reaction. Immune system From Wikipedia, the free encyclopedia Jump to: navigation, search good immune system Neutrophil Neutrophil with anthrax copy.jpg (yellow) ingested by phagocytosis of anthrax bacteria (Naraja). The image corresponds to a scanning electron microscope. The white line corresponds to 5 microns. Protection function of an organism to external agents. Basic structures Synonyms White blood leukocytes or immune system Immune System An immune system, immune system or immune system (from the Latin in-mūn (itātem) 'no obligation' cient. 'Immunity' and the Greek syn σύν 'with', 'union ',' system ',' set ') is the set of biological structures and processes within an organism that protects against disease by identifying and killing pathogens and cancerous cells. [1] detects a wide variety of agents, from viruses to intestinal parasites, [2] [3] and needs to distinguish them from their own cells and tissues of the body to function properly. The immune system is mainly composed of leukocytes (lymphocytes, [4] other leukocytes, [5] antibody [6] T cells [7], cytokines [7] macrophages [7], neutrophils [7] among other components that help your operation). [7] Detection is complicated as pathogens can evolve rapidly, producing adaptations that avoid the immune system and allow the pathogens to successfully infect their guests. [8] To overcome this challenge, multiple mechanisms evolved that recognize and neutralize pathogens. Even simple unicellular organisms such as bacteria possess enzyme systems that protect against viral infections. Other basic immune mechanisms evolved in ancient eukaryotes and remain in their modern descendants, such as plants, fish, reptiles and insects. These mechanisms include antimicrobial peptides called defensins, [9] the phagocytosis and the complement system. Vertebrates, including humans, have defense mechanisms even more sophisticated. [10] The vertebrate immune systems consist of many types of proteins, cells, organs and tissues, which interact in an elaborate and dynamic network. As part of this more complex immune response, the human immune system adapts over time to recognize specific pathogens more efficiently. In this adaptation process is called "adaptive immunity" or "acquired immunity" able to create an immunological memory. [11] Immunological memory created from a primary response to a specific pathogen, provides an enhanced response to secondary encounters with that same specific pathogen. This process of acquired immunity is based on vaccination. The immune system disorders can cause diseases. Immunodeficiency occurs when the immune system is less active than normal, [12] resulting in recurrent infections and life-threatening. Immunodeficiency can result from a genetic disease, such as severe combined immunodeficiency, [13] or be caused by drugs or infections, such as acquired immunodeficiency syndrome (AIDS) is caused by the retrovirus HIV. [14] contrast, autoimmune diseases result from an overactive immune system attacking normal tissues as if they were foreign organisms. Among the common autoimmune diseases include Hashimoto's thyroiditis, rheumatoid arthritis, diabetes mellitus type 1 and lupus erythematosus. Immunology covers the study of all aspects of the immune system that have significant relevance to human health and disease. It is expected that further research in this area plays a serious role in the promotion of health and treatment of diseases. Immunoassay From Wikipedia, the free encyclopedia Jump to: navigation, search Immunoassay is a set of analytical laboratory immunochemical techniques have in common using immune complexes, ie resulting from the conjugation of antibodies and antigens, as references of quantification of an analyte (the substance under analysis) determined, which can be the antibody (Ab) or antigen (Ag), using the measurement as a marker molecule that is part of the reaction with the immune complex in the test or chemical assay. The technique is based on the high specificity and affinity of antibodies for their specific antigens and used monoclonal antibodies (obtained in the laboratory) or polyclonal sera (obtained from animals), being more specific monoclonals. Its high sensitivity and specificity allows the quantification of organic compounds present in liquids in low concentration in the nanogram / ml or picogram / ml. The development of immunoassay has had great impact in the field of medical diagnosis by laboratory tests or clinical chemistry. For the measurement technique ◦ Competitive: the antigen (Ag) to be measured competes with labeled antigen for antibody (Ab). Is measured by the amount of labeled antigen which is considered unconjugated is inversely proportional to the analyte. ◦ not competitive (also called sandwich) the Ag in the sample reacts with two different Ac which bind to different parts of Ag. Ac one is generally solid support to facilitate separation of the bound fraction, and the other is marked Ac. Is measured by the amount of marker which is considered directly proportional to the amount of analyte. The medium where the measurement is made ◦ Homogeneous: In this type of test signal generated by the binding of antigen and antibody is measured directly in the same medium that is used to enhance the formation of the immune complex. Heterogeneous ◦: In this type of test signal generated by the binding of antigen and antibody is measured by a different means than that used for immune complex binding, generally involve an intermediate step of washing to remove interference. Is considered homogeneous immunoassays noncompetitive format are most sensitive and specific. ◦ marker by Radioimmunoassay (RIA): The label is a radioactive isotope. ◦ Enzimoinmunoanálsis (EIA): the label is an enzyme such as enzyme immunoassay technique known by the abbreviation ELISA. ◦ fluoroimmunoassay: the marker is a fluorescent molecule, such FPIA. ◦ Test Inmunoquimioluminiscente: the brand is generally an enzyme capable of catalyzing a chemiluminescent reaction. Are equally or more sensitive than radioimmunoassay, and no risk of handling radioactive substances. In contrast are underdeveloped and can not always be applied. ◦ Uses Measuring hormone levels: for example measuring levels of thyroid hormones or estrogen ◦ Measuring serum metabolites whose amount or presence is evidence of cell damage: eg measuring myocardial biomarkers such as troponins ◦ Detection viruses: for example, the cause of hepatitis and their identification ◦ detection of cancer or tumor cells: through its proteins and tumor markers released into the serum of patients. ◦ Detecting exposure to infectious agents: for example rubella or toxoplasmosis in pregnant or immunosuppressed people. Detection of metabolites ◦ indicators physiological problems, by its presence or excess amount in blood, for example in case of anemia measured ferritin levels. ◦ Measure levels of medications, drugs of abuse and blood toxins. CRE: Unable to disclose their production in vitro thus protecting the IP patentable applies and results from Dr. Brzostowski SA Laboratory, and used in the care of various rheumatic diseases, raising the natural defenses and health restructuring, starting the research into the functioning of the pancreas and cure of Diabetes, rejuvenating our body cells.