| AET | absorption-equivalent thickness;S-(2-aminoethyl) isothiuronium |
|---|---|
| ANAP | agglutination negative, absorption positive [reaction] |
| CA | anterior commissure [Lat. commissura anterior]; calcium antagonist; California [rabbit]; cancer; Can... |
| DAR | death after resuscitation; diacereine; differential absorption ratio |
| DOA | date of admission; dead on arrival; Department of Agriculture; depth of anesthesia; differential opt... |
| genetic complement | <biology, genetics> The set of chromosomes contained within any one particular cell. (07 May 1998) |
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| receptors, complement | Molecules on the surface of some B-lymphocytes and macrophages, that recognise and combine with the c3b, c3d, c1q, and c4b components of complement. (12 Dec 1998) |
| receptors, complement 3b | Molecular sites on or in some B-lymphocytes and macrophages that recognise and combine with complement 3b. The primary structure of these receptors reveal that they contain transmembrane and cytoplasmic domains, with their extracellular portion composed entirely of thirty short consensus repeats each having 60 to 70 amino acids. (12 Dec 1998) |
| receptors, complement 3d | Molecular sites on or in B-lymphocytes, follicular dendritic cells, lymphoid cells, and epithelial cells that recognise and combine with complement 3d. Human cr2 serves as a receptor for both c3dg and the gp350/220 glycoprotein of herpes virus 4, human, and binds the monoclonal antibody okb7, which blocks binding of both ligands to the receptor. (12 Dec 1998) |
| chromosome complement | The whole set of chromosomes for the species. In humans, the chromosome complement (which is also called the karyotype) consists of 46 chromosomes. (12 Dec 1998) |
| complement | <immunology> A term originally used to refer to the heat labile factor in serum that causes immune cytolysis, the lysis of antibody coated cells and now referring to the entire functionally related system comprising at least 20 distinct serum proteins that is the effector not only of immune cytolysis but also of other biologic functions. Complement activation occurs by two different sequences, the classic and alternative pathways. The proteins of the classic pathway are termed components of complement and are designated by the symbols C1 through C9. C1 is a calcium dependent complex of three distinct proteins C1q, C1r and C1s. The proteins of the alternative pathway (collectively referred to as the properdin system) and complement regulatory proteins are known by semisystematic or trivial names. Fragments resulting from proteolytic cleavage of complement proteins are designated with lower case letter suffixes, for example, C3a. Inactivated fragments may be designated with the suffix i, for example C3bi. Activated components or complexes with biological activity are designated by a bar over the symbol for example C1 or C4b, 2a. The classic pathway is activated by the binding of C1 to classic pathway activators, primarily antigen-antibody complexes containing IgM, IgG1, IgG3, C1q binds to a single IgM molecule or two adjacent IgG molecules. The alternative pathway can be activated by IgA immune complexes and also by nonimmunologic materials including bacterial endotoxins, microbial polysaccharides and cell walls. Activation of the classic pathway triggers an enzymatic cascade involving C1, C4, C2 and C3, activation of the alternative pathway triggers a cascade involving C3 and factors B, D and P. Both result in the cleavage of C5 and the formation of the membrane attack complex. Complement activation also results in the formation of many biologically active complement fragments that act as anaphylatoxins, opsonins or chemotactic factors. (05 Jan 1998) |
| complement 1 | The first complement component to act in the cytolysis reaction. It is a trimolecular complex held together with ca ions and when activated, has esterase activity which initiates the next step in the sequence. (12 Dec 1998) |
| complement 1 inactivators | Compounds which inhibit, antagonise, or inactivate complement 1. A well-known inhibitor is a serum glycoprotein believed to be alpha-2-neuroaminoglycoprotein. It inhibits the activated (esterase) form of complement 1 as well as kinin-forming, coagulation, and fibrinolytic systems. Deficiency of this inactivator has been found in patients with hereditary angioneurotic oedema. These compounds are members of the serpin superfamily. (12 Dec 1998) |
| complement 1q | <chemical> Subcomponent of complement 1 (c1) which recognises and binds to the heavy chain of IgG or IgM initiating the classical complement pathway. The interaction of c1q and immunoglobulin activates c1r and c1s. The activated c1r and c1s molecules are cleaved off the complex by c1-inhibitor, allowing the collagen-like region of c1q to become accessible for interaction with cell membrane c1q receptors. Chemical name: Complement C1q (12 Dec 1998) |
| complement 1r | <enzyme> Subcomponent of complement 1 which, when activated by c1q, activates subcomponent c1s by proteolytic cleavage. Registry number: EC 3.4.21.41 (12 Dec 1998) |
| complement 1s | <enzyme> The activated form of complement 1 which has hydrolase activity. In the classical pathway, it splits first c4 and then c2 into active components, thereby generating a new enzyme referred to as eac142 or c42 or c3 convertase. Registry number: EC 3.4.21.42 (12 Dec 1998) |
| complement 2 | The third component in the complement reaction sequence. It is a beta-globulin with a molecular weight of 117,000, a serum concentration of 30 micrograms/ml and a sedimentation coefficient of 4. It activates c3. (12 Dec 1998) |
| complement 3 | The fourth component to attach in the complement reaction sequence. It is a beta-globulin with a sedimentation coefficient of 5.5, a molecular weight of 185,000 and a serum concentration of 1.3 micrograms/ml. Its fragments have anaphylatoxic, chemotactic, and histaminic action and affect smooth muscle. (12 Dec 1998) |
| complement 3a | <chemical> Smaller fragment formed when c3 convertase splits c3 into c3a and c3b. C3a is a 77-amino acid peptide that includes a carboxy-terminal arginine which is crucial for its biological activities. C3a causes symptoms of immediate hypersensitivity (anaphylaxis) including smooth muscle contraction, mast cell histamine release, and local inflammation. It is considered an anaphylatoxin along with c4a, c5a, and c5a des-arginine. Chemical name: Complement C3a (12 Dec 1998) |
| complement 3b | <chemical> The larger fragment formed when c3 convertase splits c3 into c3a and c3b. In both the classical and alternate pathway, c3b participates in immune adherence and enhances phagocytosis. It also forms a cellular intermediate which continues the complement process. In the alternate pathways, c3b initiates a positive feedback activation of c3pase. Chemical name: Complement C3b (12 Dec 1998) |