| ¿µ¹® | glia cell | ÇÑ±Û | ¾Æ±³¼¼Æ÷ |
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| ¼³¸í | ½Å°æ¼¼Æ÷ »çÀÌ¿¡¼ ±×¹°±¸Á¶¸¦ ÀÌ·ç¸ç À̸¦ ÁöÁöÇÏ´Â Á¶Á÷. ½Å°æ¾Æ±³¼¼Æ÷´Â ½Å°æ¸ð¼¼Æ÷¿Í °¥¶óÁø ¾Æ±³¸ð¼¼Æ÷°¡ ´Ù½Ã ¿©·¯ ÇüÅ·ΠºÐÈ-¼ºÀåÇÑ °ÍÀÌ´Ù. ³ú½ÇÀ̳ª ô¼öÁ߽ɰüÀÇ º®À» µ¤°í ¿øÁÖ»ó ¶Ç´Â ÀÔ¹æÇüÀ̸ç, Ãʱ⿡´Â À¯¸®¸é¿¡ ¼¶¸ð°¡ ÀÖ´Ù. ´ëÇü¼¼Æ÷´Â º°³ú½Ç¸·¼¼Æ÷´Â ¾Æ±³¼¼Æ÷¶ó°í Çϸç, ½Å°æ¼¼Æ÷³ª ½Å°æ¼¶À¯ »çÀÌ¿¡ »êÀçÇÑ´Ù. ±× ¿Ü¿¡ Èñ¼Òµ¹±â¾Æ±³¼¼Æ÷µµ Æ÷ÇԵȴÙ. |
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| ¿µ¹® | reserve cell | ÇÑ±Û | ¿¹ºñ¼¼Æ÷ |
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| ¼³¸í | ÀϹÝÀûÀ¸·Î »óÇÇÁ¶Á÷¿¡¼ ÀÌ¹Ì ÀÖ´ø »óÇǼ¼Æ÷°¡ ¼Õ»óÀ» ¹Þ¾Æ »ç¸êÇÏ¸é ¸Å²ãÁö´Â ±× ¹Ø¿¡ ÀÖ´Â ¹ÌºÐȼ¼Æ÷ ¿¹¸¦ µé¸é, ±â°üÁö ³»Ç¥¸éÀ» µ¤´Â ÁßÃþ ¿øÁÖ »óÇÇÀÇ ±âÀú¿¡ ÀÖ´Â ÀÛÀº ¹ÌºÐÈ »óÇÇ ¼¼Æ÷. |
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| ¿µ¹® | stem cell | ÇÑ±Û | Áٱ⼼Æ÷, °£¼¼Æ÷ |
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| ¼³¸í | Àڱ⠺¹Á¦¸¦ ÇÏ¿© ÀÚ½ÅÀ» Á¸¼Ó½ÃŰ¸é¼ ÇÑÆíÀ¸·Î´Â Áõ½Ä°ú ºÐȸ¦ ÇÏ¿© »õ·Î¿î ¼¼Æ÷¸¦ Çü¼ºÇÏ´Â ¼¼Æ÷·Î¼ Á¶Ç÷Áٱ⼼Æ÷°¡ ´ëÇ¥ÀûÀÌ´Ù. Á¶Ç÷Áٱ⼼Æ÷´Â °ñ¼ö¿¡ ÀÖ´Â ¼¼Æ÷·Î¼ ¸ðµç Ç÷±¸¼¼Æ÷°¡ ¿©±â¿¡¼ ºÐÈµÇ¾î ¹ß»ýÇÑ´Ù. |
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| ¿µ¹® | renal cell carcinoma | ÇÑ±Û | ÄáÆÏ¼¼Æ÷¾ÏÁ¾ |
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| ¼³¸í | ÄáÆÏ¿¡ »ý±ä ¿ø½ÃÄáÆÏÁ¶Á÷¿¡¼ ¹ß»ýÇÑ ¾Ï. ÁÖ·Î ¿ø½Ã¼¼´¢°üÁ¶Á÷¿¡¼ ¹ß»ýÇÑ´Ù. ´ëÇ¥ÀûÀÎ ¼¼Æ÷Á¶Á÷ÇüÀº ¿°»ö½Ã ¼¼Æ÷ÁúÀÌ ¸¼°Ô ºñ¾îº¸ÀÌ´Â ¸¼Àº¼¼Æ÷¾ÏÁ¾ÀÌ´Ù. Ä¡·á´Â ¼ö¼ú°ú Ç×¾ÏÈÇпä¹ýÀÌ¸ç ¾ÆÁÖ µå¹°Áö¸¸ ÀúÀý·Î ³´´Â °æ¿ìµµ ÀÖ´Â °ÍÀ¸·Î º¸°íµÇ¾î ÀÖ´Ù. |
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| ¿µ¹® | squamous cell carcinoma | ÇÑ±Û | ÆíÆò¼¼Æ÷¾ÏÁ¾ |
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| ¼³¸í | ÆíÆò¼¼Æ÷ ±â¿øÀÇ ¾ÏÀ¸·Î¼, ÆíÆò¼¼Æ÷°¡ ÀÖ´Â ¾î¶² °÷¿¡¼µç ¹ß»ý°¡´ÉÇÔ. µû¶ó¼ ½Äµµ¾Ï, ÇǺξÏ, Æó¾Ï, ÀÚ±Ã¾Ï µîÀÌ ¿©±â¿¡ ÇØ´çµÈ´Ù. ƯÈ÷ ÇǺξÏÀº ¸¹Àº Àڿܼ±Á¶»ç¿¡ ÀÇÇØ »ý±â´Â ±¤¼±°¢ÈÁõ¿¡¼ ¹ß»ý°¡´ÉÇÏ´Ù. º´¸®Á¶Á÷ÇÐÀû Ư¼ºÀ¸·Î¼ °¢ÁúÀ» »ý¼ºÇÑ´Ù. |
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| PAF | paroxysmal atrial fibrillation; peroxisomal assembly factor; phosphodiesterase-activating factor; pl... |
|---|---|
| TF | free thyroxine; tactile fremitus; tail flick [reflex]; temperature factor; testicular feminization; ... |
| NG | nasogastric; neoplastic growth; new growth; nitroglycerin; nodose ganglion; no growth; not given |
| ACC | accommodation; acetyl coenzyme A carboxylase; acinic cell carcinoma; acute care center; adenoid cyst... |
| DF | decapacitation factor; decontamination factor; deferoxamine; deficiency factor; defined flora [anima... |
| insulin-like growth-factor-binding proteins | A family of soluble proteins that bind insulin-like growth factors and modulate their biological actions at the cellular level. (int j gynaecol obstet 1992;39(1):3-9) (12 Dec 1998) |
|---|---|
| insulin-like growth factor I | <chemical> A well-characterised basic peptide believed to be secreted by the liver and to circulate in the blood. It has growth-regulating, insulin-like, and mitogenic activities. This growth factor has a major, but not absolute, dependence on somatotropin. It is believed to be mainly active in adults in contrast to insulin-like growth factor II, which is a major foetal growth factor. Chemical name: Insulin-like growth factor I (12 Dec 1998) |
| insulin-like growth factor II | <chemical> A well-characterised neutral peptide believed to be secreted by the liver and to circulate in the blood. It has growth-regulating, insulin-like and mitogenic activities. The growth factor has a major, but not absolute, dependence on somatotropin. It is believed to be a major foetal growth factor in contrast to insulin-like growth factor I, which is a major growth factor in adults. Chemical name: Insulin-like growth factor II (12 Dec 1998) |
| transforming growth factor | <growth factor> Proteins secreted by transformed cells that can stimulate growth of normal cells. Unfortunate misnomer, since they induce aspects of transformed phenotype, such as growth in semi solid agar, but do not actually transform. Transforming growth factor alpha, 50 amino acid polypeptide originally isolated from viral transformed rodent cells, contains EGF like domain and binds to EGF receptor. Stimulates growth of microvascular endothelial cells, i.e. Is angiogenic. Transforming growth factor beta a homodimer of two 112 chains, polypeptide is secreted by many different cell types, stimulates wound healing but in vitro is also a growth inhibitor for certain cell types. The transforming growth factor family includes many of the bone morphogenetic proteins. Acronym: TGF (18 Nov 1997) |
| transforming growth factor alpha | Factor isolated in a variety of tissues including epithelium, and maternal decidua. It is closely related to epidermal growth factor (epidermal growth factor-urogasterone) and binds to the egf receptor. Tgf-alpha acts synergistically with tgf-beta in inducing phenotypic transformation, but its physiological role is unknown. (12 Dec 1998) |
| transforming growth factor beta | Factor synthesised in a wide variety of tissues including platelets, placenta, and both normal and transformed cell lines. It acts synergistically with tgf-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. Tgf-beta also has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. There are at least three forms of tgf-beta: tgf-beta1, tgf-beta2, and tgf-beta1.2. The latter is a heterodimer made up of both tgf-beta1 and tgf-beta2. (12 Dec 1998) |
| endothelium-derived growth factor synthase | <enzyme> Converts l-arginine to a smooth muscle relaxing factor and stimulates the formation of cyclic-GMP Registry number: EC 1.5.1.- Synonym: edrf synthase (26 Jun 1999) |
| epidermal growth factor | <growth factor> A mitogenic polypeptide initially isolated from male mouse submaxillary gland. The name refers to the early bioassay, but epidermal growth factor is active on a variety of cell types, especially but not exclusively epithelial. Human equivalent originally named urogastrone owing to its hormone activity. Acronym: EGF (18 Nov 1997) |
| epidermal growth factor receptor protein-tyrosine kinase | <enzyme> The catalytic protein-tyrosine kinase domain found on the cytoplasmic beta-portion of epidermal growth factor receptor. Registry number: EC 2.7.1.- (12 Dec 1998) |
| epidermal growth factor-urogastrone | <chemical> Single chain, nonhelical, acidic polypeptides of about 52 amino acids found in most mammals. Epidermal growth factor and urogastrone are not identical but seem to share biological acivities. They promote growth of, and cell proliferation in, certain tissues, especially epidermal structures and inhibit acid secretion by the stomach. They have been used to treat gastrointestinal ulcers. Chemical name: Epidermal growth factor (12 Dec 1998) |
| keratinocyte growth factor | <growth factor> A growth factor structurally related to fibroblast growth factor. (18 Nov 1997) |
| fibroblast 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) |
| fibroblast growth factor, acidic | <chemical> A growth factor which has been isolated from a variety of cells. It contains 154 amino acid residues and has potent heparin-binding activity. Heparin potentiates the biological activities of afgf. The growth factor is an extremely potent inducer of DNA synthesis in a variety of normal diploid mammalian cell types from mesoderm and neuroectoderm lineages and also has chemotactic and mitogenic activities. Chemical name: Fibroblast growth factor (human brain acidic protein moiety reduced) (12 Dec 1998) |
| fibroblast growth factor, basic | A single-chain polypeptide of approximately 15-16 kD which has been isolated from a variety of cells. It has a 55% amino acid residue identity to acidic fibroblast growth factor and has potent heparin-binding activity. However, in contrast to the acidic fibroblast growth factor, heparin does not potentiate the biological activities of bfgf. The growth factor is an extremely potent inducer of DNA synthesis in a variety of normal diploid mammalian cell types from mesoderm and neuroectoderm lineages and promotes cellular differentiation in vitro. (12 Dec 1998) |
| fibroblast growth factor receptor | Family of receptor tyrosine kinases for fibroblast growth factor. (18 Nov 1997) |
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