Apolipoprotein A1
Apo A1 is primarily found in high density lipoprotein (HDL) particles. It serves to prevent the accumulation of cholesterol loaded macrophages which deposit on the arterial wall as foam cells. This is the prominent early feature of atherosclerotic lesion formation ultimately resulting in atherosclerosis. Its primary function is to activate LCAT within the HDL complex, which catalyzes the esterification of cholesterol. This results in a more soluble cholesterol-HDL complex which increases the cholesterol transport capacity of the HDL particle for subsequent removal by the liver. Apo AI is therefore a convenient marker for assessing the cholesterol clearing capacity of the blood, and studies have clearly indicated that it is a better discriminator of angiographically documented coronary artery disease than HDL cholesterol. Swiss-Prot Accession Number Q00623.
C-Reactive Protein
CRP is an acute phase reactant, which can be used as a general screening aid for inflammatory diseases, infections, and neoplastic diseases. In addition to its usual value as an acute phase reactant, CRP in large concentration (>5 mg/dL) predicts progression of erosions in rheumatoid arthritis. Elevated serum CRP is characteristic of bacterial, but not viral, meningitis or meningoencephalitis. Swiss-Prot Accession Number P48199 (rat); P14847 (mouse).
CD40
CD40 is a type I transmembrane glycoprotein belonging to the TNF receptor superfamily. The mature mCD40 consists of a 172 amino acid extracellular domain, a 22 amino acid transmembrane region and a 90 amino acid cytoplasmic domain. CD40 is expressed on B cells, follicular dendritic cells, dendritic cells, activated monocytes, macrophages, endothelial cells, vascular smooth muscle cells and several tumor cell lines. Interaction of CD40 with its ligand, CD40L, leads to the aggregation of CD40 molecules, which in turn interact with cytoplasmic components to initiate signaling pathways. Interaction between CD40L on T cells and CD40 on B cells stimulates B cell proliferation and provides the signal for immunoglobulin isotype switching. Mutations in the CD40L gene, which result in a CD40L molecule unable to interact with CD40, and is responsible for the hyper-IgM syndrome. Cross-linking of CD40 with antibodies or by binding to CD40L produces cell type-specific responses which include co-stimulation and induction of proliferation, induction of cytokine production, rescue from apoptosis, and up-regulation of adhesion molecules. Swiss-Prot Accession Number P27512.
CD40 Ligand
CD40 Ligand is a 260 amino acid type II transmembrane glycoprotein belonging to the TNF family. Murine CD40L consists of a 22 amino acid cytoplasmic domain, a 24 amino acid transmembrane domain, and 214 amino acid extracellular domain bearing a single glycosylation site. CD40L is expressed predominantly on activated CD4+ T lymphocytes. Murine CD40L shares 78% amino acid sequence identity with human CD40L. Native bioactive soluble CD40L exists. The receptor of CD40L is CD40, a type I transmembrane glycoprotein belonging to the TNF receptor family. Although all monomeric, dimeric and trimeric forms of soluble CD40L can bind to CD40, the soluble trimeric form of CD40L has the most potent biological activity through oligomerization of cell surface CD40. CD40L mediates a range of activities on B cells including induction of activation-associated surface antigen, entry into cell cycle, isotype switching, Ig secretion, and memory generation. CD40-CD40L interaction also plays important roles in monocyte activation and dendritic cell maturation. Swiss-Prot Accession Number P27548.
Endothelin-1
CD40 is a type I transmembrane glycoprotein belonging to the TNF receptor superfamily. The mature mCD40 consists of a 172 amino acid extracellular domain, a 22 amino acid transmembrane region and a 90 amino acid cytoplasmic domain. CD40 is expressed on B cells, follicular dendritic cells, dendritic cells, activated monocytes, macrophages, endothelial cells, vascular smooth muscle cells and several tumor cell lines. Interaction of CD40 with its ligand, CD40L, leads to the aggregation of CD40 molecules, which in turn interact with cytoplasmic components to initiate signaling pathways. Interaction between CD40L on T cells and CD40 on B cells stimulates B cell proliferation and provides the signal for immunoglobulin isotype switching. Mutations in the CD40L gene, which result in a CD40L molecule unable to interact with CD40, and is responsible for the hyper-IgM syndrome. Cross-linking of CD40 with antibodies or by binding to CD40L produces cell type-specific responses which include co-stimulation and induction of proliferation, induction of cytokine production, rescue from apoptosis, and up-regulation of adhesion molecules. Swiss-Prot Accession Number P27512.
Eotaxin
CD40 ligand is a 260 amino acid type II transmembrane glycoprotein belonging to the TNF family. Murine CD40L consists of a 22 amino acid cytoplasmic domain, a 24 amino acid transmembrane domain, and 214 amino acid extracellular domain bearing a single glycosylation site. CD40L is expressed predominantly on activated CD4+ T lymphocytes. Murine CD40L shares 78% amino acid sequence identity with human CD40L. Native bioactive soluble CD40L exists. The receptor of CD40L is CD40, a type I transmembrane glycoprotein belonging to the TNF receptor family. Although all monomeric, dimeric and trimeric forms of soluble CD40L can bind to CD40, the soluble trimeric form of CD40L has the most potent biological activity through oligomerization of cell surface CD40. CD40L mediates a range of activities on B cells including induction of activation-associated surface antigen, entry into cell cycle, isotype switching, Ig secretion, and memory generation. CD40-CD40L interaction also plays important roles in monocyte activation and dendritic cell maturation. Swiss-Prot Accession Number P27548.
EGF
Epidermal growth factor is a small protein that is a powerful mitogen. EGF promotes cell growth and differentiation, is essential in embryogenesis, and is important in wound healing. It is produced by many normal cell types and is made in large amounts by some tumors. Swiss-Prot Accession Number P07522.
Factor VII
Factor VII plays a role in the coagulation cascade, the chain reaction that is set in motion when there is an injury to a blood vessel. There are two types of Factor VII Deficiency: Inherited Factor VII Deficiency and Acquired Factor VII Deficiency (which is the result of other physical disorders, and may last only a short time). The inherited type of Factor VII Deficiency affects only 1 in 1 million people. However, one in 500 people may be a carrier of the defective gene. The acquired form of Factor VII Deficiency is more common and can result from severe liver disease which reduces the function of the liver (Factor VII is produced in the liver) or they have low vitamin K levels as a result of taking certain kinds of medication. In addition, acquired Factor VII deficiency is associated with certain forms of cancer and autoimmune response to Factor VII. Swiss-Prot Accession Number P70375.
Fibrinogen
Cleavage of soluble fibrinogen by thrombin to form fibrin is the final common reaction of the coagulation cascade. Low levels of fibrinogen are seen in association with fibrinolysis and liver disease. A high level of fibrinogen is a risk factor for thrombosis and is a strong predictor of cardiovascular risk and stroke, particularly in young adults. Low-dose heparin and ACE-inhibitors reduce fibrinogen and the risk of adverse cardiovascular events. Swiss-Prot Accession Number Q8K0E8 (beta chain); Q8VCM7 (gamma chain).
FGF-basic
Cleavage of soluble fibrinogen by thrombin to form fibrin is the final common reaction of the coagulation cascade. Low levels of fibrinogen are seen in association with fibrinolysis and liver disease. A high level of fibrinogen is a risk factor for thrombosis and is a strong predictor of cardiovascular risk and stroke, particularly in young adults. Low-dose heparin and ACE-inhibitors reduce fibrinogen and the risk of adverse cardiovascular events. Swiss-Prot Accession Number Q8K0E8 (beta chain); Q8VCM7 (gamma chain).
FGF-9
Human FGF-9 is a protein of 208 amino acids with sequence similarity of approximately 30 percent to other members of the family of fibroblast growth factors. A sequence comparison between the Xenopus laevis XFGF-9 and mammalian FGF-9 shows that these proteins share 93 percent identity at the amino acid level. FGF-9 is found in the conditioned medium of a human glioma cell line and acts on cells of the central nervous system. It is a potent mitogen for glial cells. It activates O-2A progenitor cells, PC12 cells, murine 3T3 cells, and rat glial cells. The factor does not act on human umbilical vein endothelial cells but is active on fibroblasts. The introduction of FGF-9 cDNA into murine fibroblasts leads to malignant transformation of the cells, as has been found for other members of the FGF family. Swiss-Prot Accession Number P54130.
GCP-2
This 6 kDa protein is structurally related to other members of the IL-8 family and belongs to the family of chemotactic cytokines known as CXC-chemokines. Murine GCP-2 (isolated from mouse fibroblasts and epithelial cells) and human or bovine GCP-2 have 61 and 64 percent identical residues, respectively. GCP-2 expression is induced by TNF-alpha, IL-1-beta, and bacterial lipopolysaccharides. The chemoattractive potency of GCP-2 for neutrophilic granulocytes is comparable with that of IL-8. GCP-2 appears to utilize the receptors for IL-8, CXCR1 and CXCR2. NCBI Accession Number NP_033167.
GM-CSF
GM-CSF is produced by endothelium, macrophages and a number of other immune cells. Its receptor, G-CSF-receptor, is present on precursor cells in the bone marrow that, in response to stimulation by G-CSF, proliferate and differentiate into mature granulocytes. In oncology and hematology a recombinant form of G-CSF is used to accelerate recovery from neutropenia which can cause myelosuppression and unacceptably low levels of making animals prone for infections and sepsis. Swiss-Prot Accession Number P01587.
GST-alpha
Secretory IgA is found in tears, sweat, saliva, milk, and colostrum, and in gastrointestinal and bronchial secretions. It protects the mucosa from bacteria and viruses. The presence of secretory IgA also affects the development of allergic (IgE) reactions to various ingested antigens by binding the antigens and preventing IgE responses. Increased serum IgA is common in animals with skin, gut, respiratory, and renal infections. In portal cirrhosis, IgA is increased.
Haptoglobin
Haptoglobin is an acute phase protein used for the detection of in vivo hemolysis. The primary function of haptoglobin is the irreversible binding of free oxyhemoglobin in plasma. This complex is then removed by the reticuloendothelial system. Thus, haptoglobin prevents loss of hemoglobin to urine and conserves iron. Elevated values are present in chronic and acute inflammatory and neoplastic diseases. Decreased levels can indicate liver disease, hemolytic anemia, sickle cell anemia, and genetic haptoglobinemia. Swiss-Prot Accession Number Q61646.
Immunoglobulin A
Glossary under construction
Inducible Protein-10
IP-10 mRNA is induced by the interferons and by lipopolysaccharide in macrophages, astrocytes and microglia. Mouse IP-10 cDNA encodes a 98 amino acid residue precursor protein with a 21 residue signal peptide that is cleaved to form the 77 amino acid secreted mature protein. Mature IP-10 shares approximately 67% amino acid sequence identity with human IP-10. IP-10 has been shown to be a chemoattractant for activated T-lymphocytes. Swiss-Prot Accession Number P17515.
Interferon-gamma
IFN-?, also known as Type II interferon or immune interferon is a cytokine produced primarily by T-lymphocytes and natural killer cells. The protein shares no significant homology with IFN-ß or the various IFN-a family proteins. Mature IFN-? exists as noncovalently-linked homodimers. It was originally characterized based on its antiviral activities. The protein also exerts anti-proliferative, immunoregulatory and proinflammatory activities and is thus important in host defense mechanisms. IFN-? induces the production of cytokines, up-regulates the expression of class I and II MHC antigens, Fc receptor and leukocyte adhesion molecules. It modulates macrophage effector functions, influences isotype switching and potentiates the secretion of immunoglobulins by B cells. IFN-? also augments TH1 cell expansion and may be required for TH1 cell differentiation. Swiss-Prot Accession Number P01580.
Interleukin-1 alpha
A soluble factor produced by monocytes, macrophages, and other cells which activates T-lymphocytes and potentiates their response to mitogens or antigens. IL-1 consists of two distinct forms, IL-1 alpha and IL-1 beta which perform the same functions but are distinct proteins. Interleukin-1 alpha is a potent immuno-modulator which mediates a wide range of immune and inflammatory responses. IL-1 is of clinical significance due to its activities as a stimulator of T-cells. Peripheral blood mononuclear cells of patients with aplastic anemia show markedly decreased IL-1 production. It has been shown that IL-1 also promotes wound healing. This activity is thought to involve effects on angiogenesis, the promotion of fibroblast proliferation, and the chemotactic activity on neutrophils. Since elevated amounts of IL-1 are found in the synovial fluid of patients with rheumatoid arthritis and osteoarthritis, receptor antagonists may be of advantage. IL-1-alpha may be a pathogenetic factor in the complex processes leading to vascular occlusion and an important in situ indicator of and a potential participant in vascular injury. It is consistently present in all vessels with sclerotic histopathologic changes following aortocoronary bypass grafting of saphenous veins and internal mammary arteries. Swiss-Prot Accession Number P01582.
Interleukin-1 beta
IL-1 beta is similar in action to IL-1 alpha with the exception of its association with breast cancer. Immunoreactive IL-1beta is detected in approximately 90% of invasive breast carcinomas. IL-1beta levels are significantly higher in invasive carcinomas than in benign lesions. High IL-1beta content in invasive carcinomas was significantly associated with higher contents of hepatocyte growth factor (HGF), Von Willebrand factor (VWF), and TSP1, but not TNF alpha. There was a trend toward higher IL-1beta content in invasive carcinomas with a group of other parameters that suggest a biologically more aggressive tumor (estrogen receptor negativity, high tumor grade, p53 positivity, and bcl-2 negativity); and the proportion of invasive tumors with these characteristics was significantly increased in a subgroup of tumors having very high IL-1beta content. Swiss-Prot Accession Number P10749.
Interleukin-2
IL-2 is a central regulator of immune responses, and plays a pivotal role in anti-inflammatory reactions, in hematopoiesis and in tumor surveillance. It stimulates the synthesis of IFN-gamma in peripheral leukocytes and also induces the secretion of IL-1, TNF-alpha and TNF-beta. IL-2 displays significant anti-tumor activity for a variety of tumor cell types since it supports the proliferation and clonal expansion of T-cells that specifically attack certain tumor types. A number of diseases have been described to be associated with the aberrant expression of IL-2 or IL-2 receptors, including Hodgkin's disease, Graft-versus-Host reaction, multiple sclerosis, rheumatoid arthritis, systemic lupus erythematosis, type-1 diabetes, lepromatous leprosy, AIDS, immunodeficiency syndrome, severe burn traumas, and allogenic bone marrow transplantation. Swiss-Prot Accession Number P04351.
Interleukin-3
IL-3 is produced primarily by T-cells following cell activation by antigens and mitogens, but also by keratinocytes, NK-cells, mast cells, endothelial cells, and monocytes. IL-3 is one of the priming factors for hematopoietic stem cells in vitro and in vivo that makes the cells responsive to later-acting factors such as EPO, GM-CSF and IL-6. IL-3 also induces the increased expression of receptors for colony stimulating factors. At pico- to nanomolar concentrations, IL-3 is a chemoattractant for eosinophils and also influences the chemotactic behavior of these cells in response to other chemotactically active factors. It induces the proliferation of mast cells and macrophages and causes the synthesis of histamines by mast cells and phagocytosis in macrophages Swiss-Prot Accession Number P01586.
Interleukin-4
IL-4 is produced mainly by a subpopulation of activated T-cells (Th2) which are the biologically most active helper cells for B-cells and which also secrete IL-5 and IL-6. IL-4 may be of clinical importance in the treatment of inflammatory diseases and autoimmune diseases since it inhibits the production of inflammatory cytokines such as IL-1 , IL-6 and TNF-alpha by monocytes and of TNF by T-cells. IL-4 may be useful also in the treatment of solid tumors, of hematopoietic systemic diseases, and of immune defects. IL-4 inhibits the growth of colon and mammary carcinomas. It has been shown to augment the development of lymphokine-activated killer cells. IL-4 may play an essential role in the pathogenesis of chronic lymphocytic leukemia disease, which is characterized by the accumulation of slow-dividing and long-lived monoclonal B-cells arrested at the intermediate stage of their differentiation by preventing both the death and the proliferation of the malignant B-cells. Swiss-Prot Accession Number P07750.
Interleukin-5
IL-5, produced by T-cells, is a specific hematopoietic growth factor that is responsible for growth and differentiation of eosinophils. It also promotes the generation of cytotoxic T-cells from thymocytes. A possible clinical application is suggested by the activity of IL-5 on eosinophils. Animal experiments have shown that eosinophilia elicited by nematode infections in mice and the concomitant infiltration of the lung with eosinophils can be prevented by administration of monoclonal animals directed against IL-5. Swiss-Prot Accession Number P04401.
Interleukin-6
IL-6 is a cytokine released by leukocytes in response to a number of inciting stimuli. In addition to its role as an acute phase reactant and endogenous pyrogen, IL-6 is also involved in B-cell differentiation into plasma cells. IL- 6 is usually not detected in normal serum, plasma, CSF, or joint fluid. Elevated levels are observed in a variety of inflammatory processes, including infections and collagen vascular diseases. IL-6 is also elevated in alcoholic cirrhosis and chronic renal failure. Swiss-Prot Accession Number P08505.
Interleukin-7
IL-7 stimulates the proliferation of pre-B and pro-B-cells without affecting their differentiation. The protein does not act on mature B-cells. IL-7 stimulates the proliferation of early and mature activated T-cells and this activity is synergized by suboptimal doses of IL-1. Thymocytes proliferate in response to IL-7 independently of three other known T-cell growth factors, IL-2, IL-4, and IL-7. In Rodent peripheral monocytes, IL-7 induces the synthesis of some inflammatory mediators such as IL-1 and IL-6. It also enhances the expression and secretion of IL-3 and GM-CSF in activated Rodent T-cells. IL-7 down-regulates expression of TGF-beta in macrophages which has been suggested as an inhibitor of the anti-tumor immune response. Swiss-Prot Accession Number P10168.
Interleukin-10
IL-10 is produced by, and down-regulates the function of Th1 and Th2 cells. In macrophages stimulated by bacterial lipopolysaccharides IL-10 inhibits the synthesis of IL-1, IL-6 and TNF-alpha by promoting, among other things, the degradation of cytokine mRNA. It also leads to an inhibition of antigen presentation. In Rodent monocytes IFN-gamma and IL-10 antagonize each other's production and function. IL-10 has been shown also to be a physiologic antagonist of IL-12. Studies suggest that IL-10 indirectly suppresses tumor growth of certain tumors by inhibiting infiltration of macrophages which may provide tumor growth promoting activity. Swiss-Prot Accession Number P18893.
Interleukin-11
IL-11 is a pleiotropic cytokine that has multiple effects on both hematopoietic and non-hematopoietic cells. Many of the biological effects described for IL-11 overlap those for IL-6. IL-11 also enhances the IL-3-dependent megakaryocyte colony formation and has been found to stimulate the T cell dependent development of specific immunoglobulin-secreting B cell. Among non-hematopoietic cell populations, IL-11, like IL-6 and LIF, can stimulate the synthesis of hepatic acute-phase proteins. Consistent with the in vitro functions of IL-11, in vivo administration of rhIL-11 in normal mice was found to enhance the generation of Ig producing cells and platelets. Swiss-Prot Accession Number P47873.
Interleukin-12p70
IL-12 is produced mainly by B-cells and to a lesser extent by T-cells. The most powerful inducers of IL-12 are bacteria, bacterial products, and parasites. It has been shown to augment natural killer-cell mediated cytotoxicity in a number of conditions. The ability of IL-12 to induce the synthesis of IFN-gamma and to stimulate the proliferation of resting peripheral cells may be of interest also. IL-12 has been shown to inhibit the growth of a variety of experimental tumors in vivo and to have anti-angiogenic effects in vivo, which are, at least in part, mediated by IFN-gamma. IL-12 therefore seems to be a potential candidate also for the treatment of angiogenesis-dependent malignancies. Swiss-Prot Accession Number P43431 (alpha chain); P43432 (beta chain).
Interleukin-17
Mouse IL-17 cDNA encodes a 158 amino acid residue precursor protein with a 21 amino acid residue signal peptide that is cleaved to yield the 137 amino acid residue mature IL-17. Both recombinant and natural IL-17 have been shown to exist as disulfide linked homodimers. While the expression of IL-17 mRNA is restricted to activated alpha beta TCR+CD4-CD8-T cells, the expression of mIL-17 R mRNA has been detected in virtually all cells and tissues tested. IL-17 exhibits multiple biological activities on a variety of cells including: the induction of IL-6 and IL-8 production in fibroblasts; the enhancement of surface expression of ICAM-1 in fibroblasts; activation of NF-kB and co-stimulation of T cell proliferation. Swiss-Prot Accession Number Q62386.
KC/GRO alpha
KC/GROalpha (Melanoma Growth Stimulatory Activity Protein): Murine KC and human GRO-alpha are homologs. KC is involved in neutrophil chemotaxis and activation. It belongs to the family of chemotactic cytokines known as chemokines. The new designation for KC is CXCL1 and the gene symbol is SCYB1. A truncated form of KC with dramatically increased biological activities has been described under the name HSF (hematopoietic synergistic factor). The KC receptor and the IL-8 type B receptor are homologs. The KC receptor is capable of binding both KC and MIP-2 with high affinity. Swiss-Prot Accession Number P12850.
LIF
LIF is a lymphoid factor which promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. LIF has a number of other activities including cholinergic neuron differentiation, control of stem cell pluripotency, bone and fat metabolism, mitogenesis of certain factor dependent cell lines and promotion of megakaryocyte production in vivo. Rat LIF is a 19.9 kDa protein containing 183 amino acid residues that exhibits 91% amino acid sequence identity with murine LIF. Leukemia inhibitory factor (LIF) is a pleiotropic cytokine required for blastocyst implantation in mice. Uterine expression of LIF and that of its receptors has been demonstrated in a number of mammalian species indicating that LIF may have widespread importance in the establishment of pregnancy. Swiss-Prot Accession Number P09056.
Lymphotactin
Lymphotactin is chemotactic for lymphocytes but not for monocytes or neutrophils, a characteristic that makes it unique among chemokines. Lymphotactin is produced by NK cells and attracts both NK cells and T-cells in vivo but it does not affect the adhesiveness of NK cells to vascular endothelium. Like some other chemokines, it possesses suppressive activity against immature subsets of myeloid progenitors stimulated to proliferate by multiple growth factors. Swiss-Prot Accession Number P47993.
M-CSF
KC/GROalpha (Melanoma Growth Stimulatory Activity Protein): Murine KC and human GRO-alpha are homologs. KC is involved in neutrophil chemotaxis and activation. It belongs to the family of chemotactic cytokines known as chemokines. The new designation for KC is CXCL1 and the gene symbol is SCYB1. A truncated form of KC with dramatically increased biological activities has been described under the name HSF (hematopoietic synergistic factor). The KC receptor and the IL-8 type B receptor are homologs. The KC receptor is capable of binding both KC and MIP-2 with high affinity. Swiss-Prot Accession Number P12850.
MDC
MDC is expressed highly in macrophages and in monocyte-derived dendritic cells. High expression is detected in normal thymus and less expression in lung and spleen. MDC is expressed by a subset of macrophages within regions of advanced atherosclerotic plaques that contain plaque micro-vessels. MDC is a potent chemoattractant for neutrophilic granulocytes. They also enhance their bactericidal activity and stimulate the release of lysozyme. Swiss-Prot Accession Number Q546S6.
MIP-1 alpha
MIP-1 alpha is expressed and secreted in lung, spleen, and pancreas. It is a monokine with inflammatory, pyrogenic and chemokinetic properties. It has a potent chemotactic activity for eosinophils. Binding to a high-affinity receptor activates calcium release in neutrophils. MIPs are involved in the cell activation of rodent granulocytes (neutrophils, eosinophils, and basophils) and appear to be involved in acute neutrophilic inflammation. All forms of MIP-1 stimulate the production of reactive oxygen species in neutrophils and the release of lysosomal enzymes. They also induce the synthesis of other pro-inflammatory cytokines such as IL-1, IL-6 and TNF in fibroblasts and macrophages. MIP-1 alpha is a potent basophil agonist, inducing a rapid change of cytosolic free calcium, the release of histamine and sulfido-leukotrienes. Swiss-Prot Accession Number P10855.
MIP-1 beta
MIP-1 beta is a monokine with inflammatory and chemokinetic properties. MIPs are involved in the cell activation of rodent granulocytes (neutrophils, eosinophils, and basophils) and appear to be involved in acute neutrophilic inflammation. All forms of MIP-1 stimulate the production of reactive oxygen species in neutrophils and the release of lysosomal enzymes. They also induce the synthesis of other pro-inflammatory cytokines such as IL-1, IL-6 and TNF in fibroblasts and macrophages. Swiss-Prot Accession Number P14097.
MIP-1 gamma
MIP-1 gamma is expressed mainly in the liver, lung, and the thymus, although some expression has been detected in a wide variety of tissues except brain. It is a monokine with inflammatory, pyrogenic and chemokinetic properties. It circulates at high concentrations in the blood of healthy animals. Binding to a high-affinity receptor activates calcium release in neutrophils. It also inhibits colony formation of bone marrow myeloid immature progenitors. It is induced by IL-4 in the bone marrow macrophage. Recombinant MIP-1? has consistently been shown to induce chemotaxis and Ca2+ flux in CD4+ or CD8+ T cells. Swiss-Prot Accession Number P51670.
MIP-2
Murine MIP-2 was originally identified as a heparin-binding protein secreted from a murine macrophage cell line in response to endotoxin stimulation. Based on its protein and DNA sequences, MIP-2 is a member of the alpha (C-X-C) subfamily of chemokines. MIP-2 cDNA encodes a 100 amino acid residue precursor protein from which the amino-terminal 27 amino acid residues are cleaved to generate the mature MIP-2. The protein sequence of murine MIP-2 shows approximately 63% identity to that of murine KC, another murine alpha chemokine whose expression is induced by PDGF. In addition, the protein sequence of MIP-2 is also 60% identical to human GROß and GRO?. It has been suggested that mouse KC and MIP-2 are the homologs of the human GROs and rat CINCs. Similarly to other alpha chemokines, murine MIP-2 is a potent neutrophil attractant and activator. MIP-2 can bind the murine IL-8 type B receptor homologue with high affinity. The expression of MIP-2 was found to be associated with neutrophil influx in pulmonary inflammation and glomerulonephritis, suggesting that MIP-2 may contribute to the pathogenesis of inflammatory diseases. Swiss-Prot Accession Number P10889.
MIP-3 beta
MIP-3 beta is expressed at high levels in the lymph nodes, thymus and appendix. Intermediate levels are seen in colon and trachea, while low levels found in spleen, small intestine, lung, kidney and stomach. It may play a role not only in inflammatory and immunological responses but also in normal lymphocyte recirculation and homing. It may also play an important role in trafficking of T-cells in thymus, and T-cell and B-cell migration to secondary lymphoid organs. Mouse MIP-3 beta cDNA encodes a 108 amino acid residue precursor protein with a predicted 25 amino acid residue signal peptide that is cleaved to form the 83 amino acid residue mature secreted protein. Mouse MIP-3 beta shares 83% amino acid sequence homology with human MIP-3 beta. Its expression is down-regulated by the anti-inflammatory cytokine IL-10. NCBI Gene ID: 2404.
MMP-9
MMPs are involved in extracellular degradation and breakdown of matrix proteins during normal tissue remodeling processes such as wound healing, pregnancy, and angiogenesis. MMPs are believed to facilitate cellular migration across basement membranes. The release of these enzymes by various cell types has been implicated in the pathogenesis of many diseases and diverse invasive processes, including tissue destruction during inflammatory reactions, and diseases such as arthritis, periodontitis, glomerulonephritis, atherosclerosis, tissue ulceration, cancer, and multiple sclerosis. It has been found that tissue destruction in disease processes often correlates with an imbalance of MMPs over their protein inhibitors, TIMPs. MMP-9 is also known as gelatinase B. Swiss-Prot Accession Number P41245.
MCP-1
MCP-1 plays a role in the recruitment of monocytes to sites of injury and infection. It has been found in the joints of people with rheumatoid arthritis where it may serve to recruit macrophages and perpetuate the inflammation in the joints. MPC-1 is also elevated in the urine as an indicator of kidney inflammation. MCP-1 has also been called small inducible cytokine A2 (SCYA2) and monocyte chemotactic and activating factor (MCAF). Swiss-Prot Accession Number P10148.
MCP-3
MCP-3 (Monocyte Chemotactic Protein-3): Mouse MCP-3 was initially identified as a transcript induced in a mouse mast cell line after Fc epsilon RI triggering by IgE plus antigen. MCP-3 expression has also been detected during murine experimental allergic encephalomyelitis in the spinal cord, and in LPS-stimulated murine WEHI -3 cells and Swiss 3T3 cells where its expression is glucocorticoid-attenuated. The mouse MCP-3 cDNA encodes a 97 amino acid residue precursor protein with a 23 amino acid residue signal peptide that is cleaved to yield a 74 amino acid residue mature protein. The E. coli-expressed mouse MCP-3 produced at R&D Systems has been shown to be a monocyte and T-lymphocyte chemoattractant. Swiss-Prot Accession Number Q03366.
MCP-5
MCP-5 (Monocyte Chemotactic Protein-5) - Mouse MCP-5 is closely related to human MCP-1 (66% amino acid sequence identity in the mature protein). Mouse MCP-5 encodes a 104 amino acid residue precursor protein with a 22 amino acid residue predicted hydrophobic signal sequence that is cleaved to generate an 82 amino acid residue mature protein. MCP-5 is expressed constitutively in the thymus and lymph nodes. Under inflammatory conditions, MCP-5 expression is induced in activated macrophages and mast cells. Recombinant MCP-5 has been shown to be a potent chemoattractant for monocytes and lymphocytes but not neutrophils. At high concentrations, MCP-5 also attracts eosinophils. Swiss-Prot Accession Number Q62401.
Myeloperoxidase
MPO is an enzyme most abundantly present in neutrophil granulocytes. It is a lysosomal protein stored in azurophilic granules of the neutrophil. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. It uses hydrogen peroxidase to convert chloride to hypochlorous acid. The produced hypochlorous acid reacts with and destroys bacteria. In many inflammatory pathologies, such as cystic fibrosis and rheumatoid arthritis, neutrophils are also causing tissue damage. It is also produced when arteries are inflamed and have rupture-prone fatty deposits. An inflammation in the arteries can lead to a blood clot and eventually to a heart attack or stroke. Swiss-Prot Accession Number: P05164.
Myoglobin
Myoglobin: Myoglobin is a monomeric heme protein that is structurally related to hemoglobin. Very little free myoglobin circulates. It is synthesized and found predominantly in skeletal and cardiac muscle. During the course of a myocardial infarction (MI), myoglobin escapes from the ischemic cardiac muscle and can reach levels 5-10 times normal during the first 5-18 hours. A wide variety of pathological processes damage skeletal muscles, causing release of myoglobin into the circulation. Muscle damage resulting in high levels of myoglobinuria is clinically referred to as rhabdomyolysis. Measurement of myoglobin in rhabdomyolysis may be useful to determine the likelihood of significant renal toxicity. A high serum myoglobin level associated with a low urine myoglobin clearance rate indicates high risk for renal failure. A high serum myoglobin level with high myoglobin clearance rate indicates low risk for renal failure. A relatively low serum myoglobin level indicates minimal risk for renal failure. Swiss-Prot Accession Number P04247.
Oncostatin M
Osteopontin acts as a cytokine involved in enhancing production of interferon-gamma and IL-12 and it reduces production of IL-10. It is essential in the pathway that leads to type I immunity. It appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Swiss-Prot Accession Number P08721.
RANTES
RANTES is chemotactic for T-cells, rodent eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. RANTES also activates eosinophils to release eosinophilic cationic protein. It changes the density of eosinophils and makes them hypodense, which is thought to represent a state of generalized cell activation and is associated most often with diseases such as asthma and allergic rhinitis. Swiss-Prot Accession Number P30882.
Serum Amyloid P
SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits. It is a homopentamer with a discoid arrangement of 5 non-covalently bound subunits. SAP is an acute-phase reactant. Swiss-Prot Accession Number P12246.
SGOT
SGOT is an enzyme found in the liver, heart, and other tissues. A high level of SGOT released into the blood may be a sign of liver or heart damage, cancer, or other diseases. Also called aspartate transaminase. It is also an acute phase reactant suggestive of inflammation. Swiss-Prot Accession Number P05201.
Stem Cell Factor
SCF is a stromal cell-derived cytokine synthesized by fibroblasts and other cell types. It is of clinical significance because of it induces differentiation in lymphoid and erythroid progenitor cells and mast cells. Improved in vitro erythropoiesis with SCF has been demonstrated to occur in several types of inherited marrow failure syndromes, including Diamond-Blackfan anemia, Fanconi's anemia, dyskeratosis congenita, amegakaryocytic thrombocytopenia, and transient erythroblastopenia of childhood. Swiss-Prot Accession Number P20826.
Thrombopoietin
TPO is a lineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets. Although IL-6 possesses thrombopoietin activity that stimulates in vitro the production of megakaryocytes and increases platelet counts in vivo it does not appear to be the only factor with TPO activity. Swiss-Prot Accession Number P40226.
TIMP 1
TIMP 1 is a major regulator of extracellular matrix synthesis and degradation. A certain balance of MMPs and TIMPs is essential for tumor growth and health. Swiss-Prot Accession Number P12032.
Tissue Factor
TNF-alpha is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is a potent pyrogen causing fever by direct action or by stimulation of IL-1 secretion and is implicated in the induction of cachexia. Under certain conditions it can stimulate cell proliferation and induce cell differentiation. TNF-alpha appears to be an important autocrine modulator promoting the survival of hairy cell leukemia cells. It may be important, therefore, in the pathogenesis of this disease. Studies with an experimental fibrosarcoma metastasis model have shown that TNF alpha induces significant enhancement of the number of metastases in the lung. Swiss-Prot Accession Number P06804.
TNF-alpha
TNF-alpha is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is a potent pyrogen causing fever by direct action or by stimulation of IL-1 secretion and is implicated in the induction of cachexia. Under certain conditions it can stimulate cell proliferation and induce cell differentiation. TNF-alpha appears to be an important autocrine modulator promoting the survival of hairy cell leukemia cells. It may be important, therefore, in the pathogenesis of this disease. Studies with an experimental fibrosarcoma metastasis model have shown that TNF alpha induces significant enhancement of the number of metastases in the lung. Swiss-Prot Accession Number P06804.
VCAM-1
TIMP 1 is a major regulator of extracellular matrix synthesis and degradation. A certain balance of MMPs and TIMPs is essential for tumor growth and health. Swiss-Prot Accession Number P12032.
VEGF
VEGF is a growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. It induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. It is important in the pathophysiology of neuronal and other tumors, probably functioning as a potent promoter of angiogenesis. Due to its influences on vascular permeability, VEGF may be involved in altering blood-brain-barrier functions under normal and pathological conditions. The production and secretion of VEGF by rodent retinal pigment epithelial cells may be important in the pathogenesis of ocular neovascularization. Swiss-Prot Accession Number Q00731.
von Willebrand Factor
vWF is synthesized in endothelial cells and in megakaryocytes as a number of subunits that polymerize and combine with the factor VIII to form a large complex. In the plasma, vWF (also known as ristocetin cofactor) exists as a heterogenous population of large polymers to which the coagulant factor VIII is complexed by non-covalent bonds. It is an acute-phase reactant. Swiss-Prot Accession Number Q8CIZ8.
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