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An antiphospholipid autoantibody that reacts with beta-2-glycoprotein 1, and a member of family of autoantibodies that cause antiphospholipid antibody syndrome and may be found in system lupus erythematosus.
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A type of antinuclear antibody that specifically targets double stranded DNA; while these antibodies are sometimes detectable in multiple different autoimmune disorders, their presence is generally considered highly specific for systemic lupus erythematosus.
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An autoantibody that recognizes histidyl-tRNA synthetase, cytoplasmic protein.
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An antinuclear antibody directed against a 47 kDa RNA-binding protein in the nucleus. They can be associated with Sjogren syndrome and system lupus erythematosus. Maternal anti-La antibody positivity can be associated with neonatal lupus.
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An antinuclear antibody directed against U1 snRNP, that is strongly associated with mixed connective tissue disease and commonly detected in lupus.
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An antinuclear antibody directed against 52 or 60 kDa RNA-binding proteins in the nucleus. They can be associated with multiple autoimmune disorders, primarily Sjogren syndrome and system lupus erythematosus. Maternal anti-Ro antibody positivity can be associated with neonatal lupus.
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An antinuclear antibody directed against small nuclear ribonucleoproteins (snRNPs), that is highly specific, but has poor sensitivity for systemic lupus erythematosus (SLE). Presence of anti-Sm antibodies are associated with central nervous system, kidney, lung and cardiac involvement in SLE, but are not indicative of disease activity.
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An autoantibody that reacts with cardiolipin. Different immunoglobulin subclasses and isotypes are associated with different diseases and conditions. Some anticardiolipin antibodies prolong phospholipid dependent clotting while others are associated with spontaneous abortion.
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An autoantibody that recognizes antigens found in the cytoplasm of neutrophils.
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A protein complex composed of 18 complement component 1q (C1q) subcomponent chains: six C1qA, six C1qB and six C1qC. The C1q complex is part of the complement component C1 complex (C1 complex) and undergoes confirmational rearrangement following binding of pentraxins or antigen-antibody complexes that include either immunoglobulin M (IgM) or several IgG molecules. These confirmational changes activate the C1r chains of the C1 complex, which, in turn, cleaves C1s chains of the C1 complex. Following C1s cleavage, the C1 complex can proteolytically activate C2 and C4 and promotes formation of C3-convertase, which cleaves C3 and activates the classical complement pathway.
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Complement component-4 (1744 aa, ~193 kDa) is part of the complement cascade, which mediates the innate immune response to infection. The full length protein is a precursor that is secreted as a trimeric molecule containing an alpha, beta and gamma chain. When the complement cascade is initiated, the protein is cleaved. This proteolysis releases both the alpha chain, C4 anaphylatoxin, which stimulates inflammation, and a dimer of the beta and gamma chains, which mediates the interaction between the antigen-antibody complex and other complement components.
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A derivative of the natural macrocyclic lactone sirolimus with immunosuppressant and anti-angiogenic properties. In cells, everolimus binds to the immunophilin FK Binding Protein-12 (FKBP-12) to generate an immunosuppressive complex that binds to and inhibits the activation of the mammalian Target of Rapamycin (mTOR), a key regulatory kinase. Inhibition of mTOR activation results in the inhibition of T lymphocyte activation and proliferation associated with antigen and cytokine (IL-2, IL-4, and IL-15) stimulation and the inhibition of antibody production. (NCI05)