| ¿µ¹® | growth factor | ÇÑ±Û | ¼ºÀåÀÎÀÚ |
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| ¿µ¹® | growth hormone | ÇÑ±Û | ¼ºÀåÈ£¸£¸ó |
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| ¼³¸í | ³úÇϼöü Àü¿±¿¡¼ ºÐºñµÇ´Â È£¸£¸óÁß Çϳª·Î¼ ½Ã»óÇϺÎÀÇ ¼ºÀåÈ£¸£¸ó¹æÃâ È£¸£¸ó¿¡ ÀÇÇØ ºÐºñ°¡ ÀÚ±ØµÇ¸ç ¼Ò¸¶Å佺Ÿƾ(somatostatin: ÀÌÀÚ¿¡¼ ºÐºñµÇ¸ç, ¼ºÀåÈ£¸£¸ó¿¡ ¹Ý´ëµÇ´Â ÀÛ¿ëÀ» ÇÔ)¿¡ ÀÇÇØ ºÐºñ°¡ ¾ïÁ¦µÈ´Ù. ¼ºÀå È£¸£¸ó ¹æÃâ È£¸£¸óÀº µµÆÄ¹Î(dopamine)À¸·Î ¾Ë·ÁÁ® ÀÖ´Ù. ¼ºÀå È£¸£¸óÀº ¼¼Æ÷ÀÇ ¼ºÀåÀ» ÃËÁø½Ã۸ç ƯÈ÷ °ñÀÇ ¼ºÀåÀ» ÀÚ±ØÇϴµ¥ ±× ÀÛ¿ëÀº Á÷Á¢ ¼¼Æ÷¿¡ ÀÛ¿ëÇÏ´Â °ÍÀÌ ¾Æ´Ï¶ó °£°ú ±ÙÀ°¿¡ ÀÛ¿ëÇÏ¿© ±×°÷¿¡¼ ¼Ò¸¶Åä¸ÞµòÀ» »ý¼ºÇϸç ÀÌ ¼Ò¸¶Åä¸ÞµòÀÌ ¼¼Æ÷ÀÇ ¼ºÀåÀ» ÃËÁø½ÃŲ´Ù. ÇÑÆí ¼ºÀå È£¸£¸óÀº ¼ºÀå¿¡ ÇÊ¿äÇÑ ´Ü¹éÁú ÇÕ¼ºÀ» Ç×Áø½ÃŰ°í ¿¡³ÊÁö´Â Áö¹æÀ» ÀÌ¿ëÇÏ¿© ¾ò°ÔÇϹǷΠÁö¹æÀÌ¿ëÈ£¸£¸óÀ̶ó°íµµ ºÒ¸°´Ù. ¼ºÀå È£¸£¸óÀÌ °ú´Ù ºÐºñµÇ¸é °ÅÀÎÁõ, ¸»´Üºñ´ëÁõÀÌ À¯¹ßµÇ¸ç ¼ºÀå È£¸£¸óÀÌ °áÇÌµÇ¸é ¼ºÀåºÎÁøÀÌ ¿Â´Ù. |
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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; ... |
|---|---|
| VEGF | vascular endothelial growth factor |
| 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... |
| VEGF/VPF | Vascular endothelial growth factor/ vascular permeability factor |
|---|---|
| VPF/VEGF | Vascular permeability factor/vascular endothelial growth factor |
| VEGFR | Vascular Endothelial Growth Factor Receptors |
| VEGF | Vascular Endothelial Growth Factor |
| VEGFR-3 | Vascular Endothelial Growth Factor Receptor-3 |
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°¡
| vascular endothelial growth factor | A growth factor that is responsible for the growth of blood vessels. (12 Dec 1998) |
|---|---|
| endothelial growth factors | These growth factors are soluble mitogens secreted by a variety of organs. The factors are a mixture of two single chain polypeptides which have affinity to heparin. Their molecular weight are organ and species dependent. They have mitogenic and chemotactic effects and can stimulate endothelial cells to grow and synthesise DNA. The factors are related to both the basic and acidic fibroblast growth factors but have different amino acid sequences. (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, 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, 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) |
| endothelial relaxing factor | A molecule functioning as a neurotransmitter and produced by activated macrophages. It is capable of killing tumour cells, parasites, and intracellular bacteria. (05 Mar 2000) |
| 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) |
| 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) |
Synonyms : Endothelial Growth Factor Receptor, Receptor, Endothelial Growth Factors, Receptor, Vascular Endothelial Cell Growth Factor, Receptor, Vascular Permeability Factor, VEGF Receptor, VEGF Receptors, VPF Receptor, Vascular Endothelial Cell Growth Factor Receptor
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