| ¿µ¹® | growth factor | ÇÑ±Û | ¼ºÀåÀÎÀÚ |
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| ¿µ¹® | growth hormone | ÇÑ±Û | ¼ºÀåÈ£¸£¸ó |
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| ¿µ¹® | rheumatoid factor | ÇÑ±Û | ·ù¸¶Æ¼½º ÀÎÀÚ |
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| ¿µ¹® | risk factor | ÇÑ±Û | À§ÇèÀÎÀÚ |
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| CF | calcaneal fibular [ligament]; calcium leucovorin; calf blood flow; calibration factor; cancer-free; ... |
|---|---|
| TGF | T-cell growth factor; transforming growth factor; tuboglomerular feedback; tumor growth factor |
| EF | ectopic focus; edema factor; ejection fraction; elastic fibril; electric field; elongation factor; e... |
| PF | pair feeding; peak flow; perfusion fluid; pericardial fluid; periosteal fibroblast; peritoneal fluid... |
| GRF | gastrin-releasing factor; genetically related macrophage factor; gonadotropin-releasing factor; grow... |
| EGFr | Epithelial Growth Factor receptors |
|---|---|
| PDGFR | Platelet Derived Growth Factor Receptors |
| VEGFR | Vascular Endothelial Growth Factor Receptors |
| HB-EGF | Heparin binding epidermal growth factor-like growth factor |
| HB-EGF | Heparin-binding epidermal growth factor (EGF)-like growth factor |
IGF-II : insulin like growth factor-IIÀÇ ¾àÀÚ. ¸¹Àº Àå±â¿Í Á¶Á÷¿¡ ÀÛ¿ëÇÏ¿© ´Ü¹é ÇÕ¼º°ú DNA, RNAÀÇ ÇÕ¼ºÀ» Áõ°¡½ÃÄÑ ¼¼Æ÷ÀÇ ¼ö¿Í ¾çÀ» Áõ°¡
| 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) |
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| 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) |
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| 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, 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, 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, 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) |
| brain-derived growth factor | <growth factor> Small basic protein purified from pig brain, a member of the family of neurotrophic factors that also includes Nerve Growth Factor and neurotrophin 3. In contrast to nerve growth factor, brain-derived neurotrophic factor is predominanantly (though not exclusively) localised in the CNS. It supports the survival of primary sensory neurons originating from the neural crest and ectodermal placodes that are not responsive to NGF. In the brain brain-derived neurotrophic factor has a trophic action on retinal, cholinergic, and dopaminergic neurons, and in the peripheral nervous system it acts on both motor and sensory neurons. Acronym: BDGF (12 Dec 1998) |
| vascular endothelial growth factor | A growth factor that is responsible for the growth of blood vessels. (12 Dec 1998) |
| growth factor | <biochemistry> A complex family of polypeptide hormones or biological factors that are produced by the body to control growth, division and maturation of blood cells by the bone marrow. They regulate the division and proliferation of cells and influence the growth rate of some cancers. These factors occur naturally but some can be synthesised using molecular biology techniques and are used clinically to stimulate normal white cell production following chemotherapy or bone marrow transplantation. Examples include epidermal growth factor, platelet-derived growth factor, fibroblast growth factor. Insulin and somatomedin are also growth factors, the status of nerve growth factor is more uncertain. Perturbation of growth factor production or of the response to growth factor is important in neoplastic transformation. (29 Sep 1997) |
| growth hormone-releasing factor | <endocrinology> Peptide hormone related to the glucagon family, released from the pituitary, acts on the adenohypophysis to release growth hormone. Synonym: somatoliberin, growth hormone-releasing factor. (20 Sep 2002) |
| platelet-derived growth factor | <growth factor> The major mitogen in serum for growth in culture of cells of connective tissue origin. It consists of 2 different but homologous polypeptides A and B (~30,000 D) linked by disulphide bonds. Believed to play a role in wound healing. It is carried in the alpha-granules of platelets and is released when platelets adhere to traumatised tissues. Connective tissue cells near the traumatised region respond by initiating the process of replication. The B chain is almost identical in sequence to p28sis, the transforming protein of simian sarcoma virus, that can transform only those cells that express receptors for platelet derived growth factor, suggesting that transformation is caused by autocrine stimulation. The receptor is a tyrosine kinase. Acronym: PDGF (12 Dec 1998) |
| sarcoma growth factor | <growth factor> Polypeptide released by sarcoma cells that promotes the growth of cells by binding to a cell surface receptor, the sarcoma cell is therefore self sufficient and independent of normal growth control. See: growth factors. The name is no longer commonly used. (18 Nov 1997) |
| heparin binding growth factor | <growth factor> Acidic fibroblast growth factor (alpha FGF, HBGF 1) and basic FGF (beta FGF, HBGF 2) are the two founder members of a family of structurally related growth factors for mesodermal or neuroectodermal cells. Synonym: heparin binding growth factor. Acronym: FGF (18 Nov 1997) |
| hepatocyte growth factor | <growth factor> Polypeptide mitogen originally shown to cause cell division in hepatocytes. In the liver, the main sources of hepatocyte growth factor are nonparenchymal cells. It is now clear that hepatocyte growth factor is a mitogen for a number of cell types and it is found in many cells outside the liver, including platelets. Hepatocyte growth factor is synthesised as a single chain precursor that is proteolytically cleaved to give a heavy chain (70 kD) and a light chain (30 kD) linked by a single disulphide bond. It contains multiple copies of the kringle domain. However, both the single chain precursor and the two chain forms of hepatocyte growth factor are biologically active and hepatocyte growth factor is generally isolated as a mixture of the two forms. Hepatocyte growth factor also alters cell motility and is now known to be identical to scatter factor. Acronym: HGF (18 Nov 1997) |
Synonyms : PDGF Receptor, Platelet-Derived Growth Factor Receptor, Platelet Derived Growth Factor Receptor, Platelet Derived Growth Factor Receptors, Receptor, PDGF, Receptors, Platelet Derived Growth Factor
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