| EPA | eicosapentaenoic acid; empiric phrase association; Environmental Protection Agency; erect posterior-... |
|---|---|
| EPA/RCRA | Environmental Protection Agency Resource Conservation and Recovery Act |
| ICPEMC | International Commission for Protection against Environmental Mutagens and Carcinogens |
| ICRP | International Commission on Radiological Protection |
| NCRP | National Council on Radiation Protection [and Measurements] |
| HB-EGF | Heparin binding epidermal growth factor-like growth factor |
|---|---|
| HB-EGF | Heparin-binding epidermal growth factor (EGF)-like growth factor |
| HGF | Hepatocyte Growth Factor-Scatter Factor |
| HGF-SF | Hepatocyte Growth Factor-Scatter Factor |
| SF/HGF | Scatter factor/hepatocyte growth factor |
D factor
edaphic factor
| mammotropic factor | <protein> Pituitary lactogenic hormone (23 kD) Synthesised on endoplasmic reticulum bound ribosomes as preprolactin that has an N terminal signal peptide that is cleaved from the mature form. The conversion of preprolactin to prolactin has been much used as an assay for membrane insertion. (18 Nov 1997) |
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| receptors, atrial natriuretic factor | Cell surface proteins that bind atrial natriuretic factor with high affinity and trigger intracellular changes influencing the behaviour of cells. (12 Dec 1998) |
| receptors, colony-stimulating factor | Cell surface receptors for colony-stimulating factors, local mediators, and hormones that regulate the survival, proliferation, and differentiation of haemopoietic cells. (12 Dec 1998) |
| receptors, epidermal growth factor-urogastrone | Glycoproteins of about 170 kD that have protein kinase activity and span the plasma membranes of growing cells, including tumours. They are activated by the binding of epidermal growth factor-urogastrone which then initiates DNA and protein synthesis. They are not found on mitotically quiescent cells except in the stomach where they control the synthesis and release of digestive enzymes and gastric acid. Transforming growth factor alpha also binds to and activates these receptors. (12 Dec 1998) |
| receptors, fibroblast growth factor | Specific molecular sites or structures on cell membranes that react with fibroblast growth factors (both the basic and acidic forms), their analogs, or their antagonists to elicit or to inhibit the specific response of the cell to these factors. These receptors frequently possess tyrosine kinase activity. (12 Dec 1998) |
| receptors, granulocyte-colony-stimulating factor | Receptors that bind and internalise granulocyte-colony-stimulating factor. Their mw is believed to be 150 kD. These receptors are found mainly on a subset of myelomonocytic cells. (12 Dec 1998) |
| receptors, granulocyte-macrophage colony-stimulating factor | Receptors that bind and internalise the granulocyte-macrophage stimulating factor. Their mw is believed to be 84 kD. The most mature myelomonocytic cells, specifically human neutrophils, macrophages, and eosinophils, express the highest number of affinity receptors for this growth factor. (12 Dec 1998) |
| receptors, growth factor | Cell surface receptors that bind growth or trophic factors with high affinity, triggering intracellular responses which influence the growth, differentiation, or survival of cells. (12 Dec 1998) |
| receptors, insulin-like-growth factor I | Specific proteins on or in cells to which insulin-like growth factor I (somatomedin c) binds and thereby modifies the function of the cells. These receptors contain transmembrane and cytosolic domains, bind igf-I preferentially, and have high-affinity sites for igf-II. The alpha-subunit has a mw of 130 kD and the beta subunit possesses tyrosine kinase activity. (12 Dec 1998) |
| receptors, insulin-like-growth-factor II | Specific proteins on or in cells to which insulin-like growth factor II and mannose-6-phosphate bind and thereby modify the function of the cells. These receptors have a mw of 250 kD and possess no tyrosine kinase activity. (12 Dec 1998) |
| receptors, macrophage colony-stimulating factor | Glycoproteins of mw 165 kD which are encoded by the c-fms proto-oncogene. The binding of csf-1 to its receptors activates an intrinsic tyrosine kinase activity resulting in autophosphorylation of the receptors on tyrosine, rapid receptor down-regulation, and phosphorylation of as yet unidentified physiologic substrates that initiate a mitogenic response. (12 Dec 1998) |
| receptors, nerve growth factor | Cell surface receptors that bind nerve growth factor (ngf) and trigger intracellular changes influencing the behaviour of cells. Nerve growth factor receptors mediate the effects of nerve growth factor on the survival and growth of neurons. (12 Dec 1998) |
| receptors, platelet-derived growth factor | Specific molecular sites or structures on cell membranes that react with platelet-derived growth factor, its analogs, or antagonists, to elicit or to inhibit the specific response of the cell to this factor. Pdgf binds with different affinities and specificities to two structurally related receptors, the alpha-receptor and the beta-receptor. Both of these receptors are transmembrane proteins with an intracellular, ligand-stimulatable protein kinase domain. (12 Dec 1998) |
| receptors, transforming growth factor beta | Cell-surface proteins that bind transforming growth factor beta and trigger changes influencing the behaviour of cells. Two types of transforming growth factor receptors have been recognised. They differ in affinity for different members of the transforming growth factor beta family and in cellular mechanisms of action. Transforming growth factor alpha binds to the same receptors as epidermal growth factor (see receptors, epidermal growth factor-urogastrone). (12 Dec 1998) |
| receptors, tumour necrosis factor | Cell surface receptors that bind tumour necrosis factor and trigger changes which influence the behaviour of cells. The two recognised tumour necrosis factor receptors are designated alpha and beta receptors. Both receptors bind both alpha and beta tumour necrosis factors with high affinity, and both are members of the nerve growth factor receptor family. (12 Dec 1998) |