| OMI | Oocyte Maturation Inhibitor |
|---|---|
| ACEI | angiotensin-converting enzyme inhibitor |
| ACI | acceleration index; acoustic comfort index; acute cardiac ischemia; acute coronary infarction; acute... |
| AI | accidental injury; accidentally incurred; adiposity index; aggregation index; allergy and immunology... |
| AIA | allylisopropylacetamide; amylase inhibitor activity; anti-immunoglobulin antibody; anti-insulin anti... |
| protein synthesis inhibitor | Compounds which inhibit the synthesis of proteins. They are usually antibiotics or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the the a site of ribosomes, the misreading of the genetic code or the prevention of the attachment of oligosaccharide side chains to glycoproteins. (12 Dec 1998) |
|---|---|
| proton pump inhibitor | <pharmacology> A group of anti-ulcer medications which work by binding to H+/K+ ATPase, an enzyme which is found on the secretory surface of parietal cells. It thereby inhibits the final transport of hydrogen ions (via exchange with potasium) into the gastric lumen. Examples of proton pump inhibitors include omeprazole and lansoprazole. (27 Sep 1997) |
| HMG CoA reductase inhibitor | Drugs, such as lovastatin and pravastatin, which interfere with the biosynthesis of cholesterol; used to treat hyperlipidemia. (05 Mar 2000) |
| selective serotonin reuptake inhibitor | <pharmacology> This is a class of drug that are used as antidepressants. Functionally, they increase the levels of serotonin in the body. These drugs can be dangerous if they are mixed with other drugs such as other antidepressants, illicit drugs (LSD, cocaine, methamphetamine), some antihistamines (Seldane, Histmanal), some antibiotics, and calcium channel blockers. Side effects include lethargy, confusion, flushing, sweating and muscle spasms. Overdose can cause damage to red blood cells, breathing problems and kidney damage. Examples include: Prozac, Zoloft and Paxil. Acronym: SSRI (12 Jan 1998) |
| human a1-proteinase inhibitor | A glycoprotein that is the major protease inhibitor of human serum, is synthesised in the liver, and is genetically polymorphic due to the presence of over 20 alleles; individuals appropriately homozygous are deficient in a1-trypsin and are predisposed to pulmonary emphysema and juvenile hepatic cirrhosis because of alterations in the amino acid and sialic acid components of the glycoprotein. A1-Antitrypsin also inhibits thrombin. Synonym: a1-trypsin inhibitor, human a1-proteinase inhibitor. (05 Mar 2000) |
| serine protease inhibitor | A class of highly polymorphic inhibitors of trypsin, elastase, and certain other proteases synthesised by hepatocytes and macrophages See: a1-antitrypsin. Synonym: serpins. (05 Mar 2000) |
| soybean trypsin inhibitor | Single polypeptide (21 kD, 181 amino acids) that forms a stable, stoichiometric, enzymically inactive complex with trypsin. (18 Nov 1997) |
| noncompetitive inhibitor | <chemistry> Reversible inhibition of an enzyme by a compound that binds at a site other than the substrate binding site. (18 Nov 1997) |
| inhibitor | <chemistry, pharmacology> A molecule which represses or prevents another molecule from engaging in a reaction. See: inhibition. (09 Oct 1997) |
| inter-alpha-inhibitor | <chemical> Inhibits bovine trypsin and chymotrypsin; complex formed with chymotrypsin less stable; alpha-glycoprotein; shap - serum-derived hyaluronan associated protein Pharmacological action: serine proteinase inhibitors, trypsin inhibitors Chemical name: trypsin inhibitor, inter-alpha- Synonym: inter-alpha-trypsin inhibitor, protein pi, inter-alpha-trypsin inhibitor, heavy chain, shap protein (05 Dec 1998) |
| tissue-inhibitor of metalloproteinase-1 | <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a n-glycosylated protein, molecular weight 28 kD, produced by a vast range of cell types and found in a variety of tissues and body fluids. It has been shown to suppress metastasis and inhibit tumour invasion in vitro. Pharmacological action: antineoplastic agent, protease inhibitors. (12 Dec 1998) |
| tissue inhibitor-of metalloproteinase-2 | <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a 21 kD nonglycosylated protein found in tissue fluid and is secreted as a complex with progelatinase a by human fibroblast and uncomplexed from alveolar macrophages. An overexpression of timp-2 has been shown to inhibit invasive and metastatic activity of tumour cells and decrease tumour growth in vivo. Pharmacological action: antineoplastic agent, protease inhibitors. (12 Dec 1998) |
| tissue inhibitor of-metalloproteinase-3 | <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a 21 kD, nonglycosylated protein. Timp-3 does not show a high degree of structural similarity unlike timp-1 and timp-2 which are structurally similar. However, it does possess a high degree of structural similarity with that of chicken timp-3 (chimp-3). Human timp-3 is of particular concern because of its potential role in cancer, arthritis, and eye diseases. Pharmacological action: antineoplastic agent, protease inhibitors. (12 Dec 1998) |
| tissue inhibitor of metalloproteinases | <chemical> A family of secreted proteins (timp-1, timp-2, and timp-3) that play a crucial role in regulating the activity of the secreted metalloproteinases (collagenases, stromelysins, gelatinases). Of the three characterised, only timp-1 and timp-2 appear to have related primary structures and inhibitory properties. They influence the activation of the prometalloproteinase and act to modulate proteolysis of extracellular matrix, notably during tissue remodeling and inflammatory processes. On certain cell types, they can exhibit growth factor-like activity, and they can inhibit the tumourigenic and metastatic phenotype in cancer cells. (pharmacol ther 1993;59:329-41) Pharmacological action: antineoplastic agent, protease inhibitors. (12 Dec 1998) |
| trypsin inhibitor | A peptide hydrolyzed off trypsinogen under the catalytic influence of enteropeptidase, with trypsin produced as a result; so called because the peptide masks or inhibits the active site of the trypsin molecule, one of the polypeptides, from various sources (e.g., human and bovine colostrum, soybeans, egg white), that inhibit the action of trypsin. Compare: Bowman-Birk inhibitor. (05 Mar 2000) |