| ¿µ¹® | activation | ÇÑ±Û | Ȱ¼º, Ȱ¼ºÈ |
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| ¼³¸í | ÀϹÝÀûÀ¸·Î, »ýü³ª »ýü ¹°ÁúÀÌ ±× ±â´ÉÀ» Ȱ¹ßÇÏ°Ô ³ªÅ¸³»°Ô µÇ´Â °Í, ¿¹¸¦ µé¸é ¨ç Ã˸Šµî¿¡¼, ±× Ç¥¸é »óÅÂÀÇ º¯È³ª, ´Ù¸¥ ¹°ÁúÀÇ Ã·°¡ µî¿¡ ÀÇÇÏ¿©, ±× ±â´ÉÀÌ ÇöÀúÇÏ°Ô ³ô¾ÆÁö´Â °Í. ¨è È¿¼ÒÀü±¸Ã¼ÀÇ È°¼ºÈ·Î¼ È¿¼ÒÀÛ¿ëÀ» °¡ÁöÁö ¾Ê´Â È¿¼Ò Àü±¸Ã¼°¡ Ȱ¼ºÀÖ´Â È¿¼Ò·Î º¯È´Â °Í. ¶Ç Ȳȼö¼Ò³ª ½Ã¾Èȼö¼Ò»ê µîÀ¸·Î ÆÄÆÄÀÎÀÌ È°¼ºÈµÇ´Â °æ¿ìµµ ÀÖ´Ù. |
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| ¿µ¹® | connective tissue | ÇÑ±Û | °áÇÕÁ¶Á÷ |
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| ¼³¸í | ü³»¿¡ ³Î¸® ºÐÆ÷Çϸç, Àå±â, Á¶Á÷»çÀ̸¦ ¸Þ¿ì°í ±×°ÍÀ» ±â°èÀûÀ¸·Î ÁöÁö, Á¶Á÷ÀÌ´Ù. ±×¹Û¿¡ Ç÷°ü, ¸²ÇÁ°ü, ½Å°æÀ» ÀεµÇÏ¸ç ¿µ¾ç, ´ë»ç»ê¹°ÀÇ ¼ö¼Û ¶Ç´Â Àú·ù, ³ª¾Æ°¡¼´Â ¼Õ»ó, °¨¿°¿¡ ´ëÇÑ ¹æ¾î ¶Ç´Â ¼öº¹ µî¿¡µµ ÀÛ¿ëÇÑ´Ù. °áÇÕÁ¶Á÷Àº ¼¼Æ÷°£ÁúÀÌ Ç³ºÎÇϸç, ¼¼Æ÷°£ÁúÀ» ±¸¼ºÇÏ´Â ±âÁú°ú ¼¶À¯ÀÇ ¼º»ó¿¡ µû¶ó °£¿±Á¶Á÷, ¼¶À¯¼º °áÇÕÁ¶Á÷(¼º±ä¼¶À¯¼º °áÇÕÁ¶Á÷, ÃÎÃÎÇÑ ¼¶À¯¼º °áÇÕÁ¶Á÷), Áö¹æÁ¶Á÷, ź¼ºÁ¶Á÷, ¼¼¸Á Á¶Á÷ µîÀ¸·Î ºÐ·ùµÈ´Ù. |
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| ¿µ¹® | osseous tissue | ÇÑ±Û | »ÀÁ¶Á÷, °ñÁ¶Á÷ |
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| ¼³¸í | °ñ¼¼Æ÷¿Í °ñ¼¼Æ÷ÁÖÀ§ÀÇ µüµüÇÑ Ä®½·Á¶Á÷À¸·Î µÑ·¯½ÎÀÎ ¹ÐÁýµÈ °áÇÕÁ¶Á÷À» ¶æÇÑ´Ù. ÀÌ °ñÁ¶Á÷¿¡ ÀÇÇØ¼ »À°¡ ÀÌ·ç¾îÁ® ÀÎüÀÇ °ñ°ÝÀ» Çü¼ºÇÑ´Ù. |
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| ¿µ¹® | epithelial tissue | ÇÑ±Û | »óÇÇÁ¶Á÷ |
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| ¼³¸í | »óÇÇ´Â ÇÑ Ãþ ¶Ç´Â ¿©·¯ ÃþÀÇ ¼¼Æ÷·Î ÀÌ·ç¾îÁø ÆÇ ¸ð¾çÀÇ ±¸Á¶·Î ½ÅüÀÇ Ç¥¸é°ú °ü»ó±¸Á¶ÀÇ ³»°À» µÑ·¯½Î°í ÀÖ´Ù. »óÇǼ¼Æ÷¿Í »óÇǼ¼Æ÷»çÀÌÀÇ ÀûÀº ¾çÀ¸·Î Á¸ÀçÇÏ¿© »óÇÇ»çÀÌÀÇ °ø°£À» ä¿ì°í ÀÖ´Â ¼¼Æ÷°£ÁúÀ» ÇÕÃÄ »óÇÇÁ¶Á÷À̶ó ÇÑ´Ù. »óÇÇÁ¶Á÷¿¡´Â ¿øÄ¢ÀûÀ¸·Î Ç÷°üÀÌ ºÐÆ÷µÇ¾î ÀÖÁö ¾Ê´Ù. |
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| ¿µ¹® | granulation tissue | ÇÑ±Û | À°¾ÆÁ¶Á÷ |
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| ¼³¸í | ¸ð¼¼Ç÷°üÀÌ Ç³ºÎÇÏ¸ç ¿Õ¼ºÇÏ°Ô Áõ½ÄÀ» °è¼ÓÇÏ´Â ¾î¸° °áÇÕÁ¶Á÷. â»ó µî Á¶Á÷ °á¼Õ¿¡ ´ëÇÑ ¼öº¹, À̹°Ã³¸®ÀÇ ±âÁúÈ, ¿°ÁõÀÌ ¸¸¼ºÀûÀÎ °æ°ú¿¡ Àְųª Á¾¾çÁõ½Ä¿¡ µ¿¹ÝµÈ »çÀ̹°ÁúÀÇ ¹ÝÀÀ¼º ¿°Áõ¿¡¼ °üÂûµÈ´Ù. ±¸¼º¼ººÐÀº »ý±äÁö ¾ó¸¶ ¾ÈµÇ´Â ¾î¸° À°¾ÆÁ¶Á÷Àº ¼¶À¯¸ð¼¼Æ÷ÀÇ Áõ½Ä, »õ·Î »ý±ä ¸ð¼¼Ç÷°ü°ú ¿©·¯ À¯ÁÖ¼¼Æ÷ ¹× ´Ù¸¥ Áß°£¿±¼¼Æ÷(¹éÇ÷±¸, ¸²ÇÁ±¸, ÇüÁú¼¼Æ÷, Á¶Á÷±¸, ´ÜÇÙ±¸, °Å´ë¼¼Æ÷)µîÀ¸·Î ±¸¼ºµÈ´Ù. À̰ÍÀÌ ½Ã°£ÀÌ Áö³ª ±×¸®µÇ¸é, ¸ð¼¼Ç÷°ü°ú À¯ÁÖ¼¼·Î, ´Ù¸¥Á¶Á÷¼ººÐÀ» °¨¼Ò½ÃÄÑ ¸¸¼ºÈÇÏ¿© ¿À·¡µÈ À°¾Æ°¡ µÇ¸ç °á±¹Àº ¼¶À¯¼¼Æ÷¿Í ¾Æ±³Áú¼¶À¯·Î ±¸¼ºµÈ ¹ÝÈçÁ¶Á÷À¸·Î º¯ÇÑ´Ù. |
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| TPAI | tissue plasminogen activator inhibitor |
|---|---|
| BPTI | basic pancreatic trypsin inhibitor; basic polyvalent trypsin inhibitor; bovine pancreatic trypsin in... |
| PI | first meiotic prophase; isoelectric point; pacing impulse; package insert; pancreatic insufficiency;... |
| APSAC | 1) Acylating the Plasminogen Streptokinase Activated Complex 2) Anisoylat... |
| APSAC | acylated plasminogen-streptokinase activator complex; anisoylated plasminogen streptokinase activato... |
| PA | Plasminogen activation |
|---|---|
| r-tPA | Recombinant Tissue-Type Plasminogen Activator |
| rt-PA | Recombinant human tissue plasminogen activator |
| rt-PA | Recombinant human tissue-type plasminogen activator |
| r-TPA | Recombinant tissue plasminogen activator |
| plasminogen activator inhibitor 1 | <chemical> A member of the serpin family of proteins. It inhibits both the tissue-type and urokinase-type plasminogen activator. Pharmacological action: serine proteinase inhibitors. (12 Dec 1998) |
|---|---|
| plasminogen activator inhibitor 2 | <chemical> Member of the serpin family of proteins. It inhibits both the tissue-type and urokinase-type plasminogen activator. Pharmacological action: serine proteinase inhibitors. (12 Dec 1998) |
| tissue plasminogen activator | <enzyme> Plasma serine protease, one of a closely related group of plasminogen activators. Contains an EGF like domain and multiple copies of the kringle domain. (18 Nov 1997) |
| 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) |
| plasminogen | <enzyme> The inactive precursor of plasmin. (18 Nov 1997) |
| plasminogen activator | <enzyme> Serine protease that acts on plasminogen to generate plasmin. Has also been implicated in invasiveness and is produced by many normal and invasive cells. The vascular form (tPA, 55 kD) is very similar to tissue plasminogen activator (uPA, 70 kD) and to streptokinase and urokinase. (18 Nov 1997) |
| plasminogen inactivators | <chemical> Important modulators of the activity of plasminogen activator. Four inhibitors, all belonging to the serpin family of proteins, have been implicated in plasminogen activation inhibition. They are pai-1, pai-2, protease-nexin, and protein c inhibitor (pai-3). All inhibit both the tissue-type and urokinase-type plasminogen activator. Pharmacological action: serine proteinase inhibitors. (12 Dec 1998) |
| kidney plasminogen activator | <protein> A precursor to the enzyme urokinase that has blood clotting properties. (14 Nov 1997) |
| activation | <radiobiology> Activation occurs when a particle interacts with an atomic nucleus, shifting the nucleus into an unstable state, and causing it to become radioactive. In fusion research, where deuterium-tritium is a common fuel mixture, the neutron released when (D + T) combine to form (4He + n) can activate the reactor structure. In this case the 4He is inert, the neutron sticks to another nucleus, and the neutron + nucleus reaction creates an actvation product. Sometimes called radioactivation. See: activation product, activation analysis. (09 Oct 1997) |
| activation analysis | <radiobiology> Method for identifying and measuring chemical elements in a sample of material. Sample is first made radioactive by bombardment with neutrons, charged particles, or gamma rays. Newly formed radioactive atoms in the sample then give off characteristic radiations (such as gamma rays) that tell what kinds of atoms are present, and how many. (09 Oct 1997) |
| activation energy | <chemistry> The amount of energy (expressed in joules) that is needed to convert all the molecules in one mole of a reacting substance from a ground state to the transition state. (06 May 1997) |
| activation product | <radiobiology> The unstable nucleus formed when activation occurs. (See activation above.) (09 Oct 1997) |
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