| ¿µ¹® | connective tissue | ÇÑ±Û | °áÇÕÁ¶Á÷ |
|---|---|---|---|
| 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. |
||
| ¿µ¹® | osseous tissue | ÇÑ±Û | »ÀÁ¶Á÷, °ñÁ¶Á÷ |
|---|---|---|---|
| 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. |
||
| ¿µ¹® | epithelial tissue | ÇÑ±Û | »óÇÇÁ¶Á÷ |
|---|---|---|---|
| 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. |
||
| ¿µ¹® | granulation tissue | ÇÑ±Û | À°¾ÆÁ¶Á÷ |
|---|---|---|---|
| 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. |
||
| ¿µ¹® | tissue | ÇÑ±Û | Á¶Á÷ |
|---|---|---|---|
| ¼³¸í | ƯÁ¤ ±¸Á¶¿Í ±â´ÉÀ» °®´Â ¼¼Æ÷ Áý´Ü. ¼¼Æ÷ »çÀÌ¿¡´Â ´Ù¼Ò°£ ¼¼Æ÷°£ÁúÀÌ µé¾î ÀÖ´Ù. ¼¼Æ÷°£Áú¿¡´Â ±Û¸®ÄÚ»ç¹Ì³ë±Û¸®Ä, È÷µå·Ï½Ã¾ÆÆÄŸÀÌÆ®¿Í °°Àº ±âÁú°ú ¾Æ±³Áú¼¶À¯¿Í °°Àº ¼¶À¯°¡ ¹ß°ßµÈ´Ù. Á¶Á÷¼º»óÀº ±¸¼º¼¼Æ÷¿Í ¼¼Æ÷°£ÁúÀÇ Á¾·ù¿Í ¾ç¿¡ ÀÇÇØ °áÁ¤µÈ´Ù. Á¶Á÷Àº »óÇÇÁ¶Á÷, ÁöÁöÁ¶Á÷, ±ÙÀ°Á¶Á÷, ½Å°æÁ¶Á÷À¸·Î ´ëº°µÇ¸ç, »óÇÇÁ¶Á÷Àº ¼¼Æ÷°£ÁúÀ» °ÅÀÇ °®Áö ¾ÊÀ¸¸ç, ÁöÁöÁ¶Á÷Àº °áÇÕÁ¶Á÷À̳ª »ÀÁ¶Á÷°ú °°ÀÌ ¼¼Æ÷°£ÁúÀÌ Ç³ºÎÇÑ °ÍÀÌ ¸¹´Ù. |
||
| 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;... |
| MMP | matrix metalloproteinase; muscle mechanical power |
| MMPI | matrix metalloproteinase specific for collagen type I; Minnesota Multiphasic Personality Inventory |
| PUMP | putative metalloproteinase |
| TIMP-2 | Tissue Inhibitor of Metalloproteinase 2 |
|---|---|
| TIMP-1 | Tissue inhibitor of matrix metalloproteinase-1 |
| TIMP-1 | Tissue inhibitor of metalloproteinase 1 |
| TIMP-3 | Tissue inhibitor of metalloproteinase-3 |
| MMPI | matrix metalloproteinase inhibitor |
acute angle
| 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) |
|---|
| 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 inhibitors of metalloproteinase | <cell biology> Family of proteins of around 200 residues that can inhibit metalloproteinases, for example collagenase, by binding to them. (18 Nov 1997) |
| Aspergillus fumigatus metalloproteinase | <enzyme> Mol mass 82 kD; pi 5.6; hydrolyzes phenylazobenzyloxycarbonyl-pro-leu-gly-pro-arg and cleaves native rat type I collagen Registry number: EC 3.4.24.- Synonym: a. Fumigatus metalloproteinase, af-mep (26 Jun 1999) |
| BaP1 metalloproteinase | <enzyme> From bothrops asper venom; causes haemorrhage at site of venom injection and systemically in different organs Registry number: EC 3.4.24.- (26 Jun 1999) |
| membrane-type 3 matrix metalloproteinase | <enzyme> Sm3 is a soluble form of mt3-mmp, probably an alternatively sliced variant. Registry number: EC 3.4.24.- Synonym: mt3-mmp, sm3-mmp (26 Jun 1999) |
| membrane-type 4 matrix metalloproteinase | <enzyme> Cloned from breast carcinoma. Registry number: EC 3.4.24.- Synonym: mt4-mmp, mmp-17 gene product, mmp-17 (26 Jun 1999) |
| membrane-type matrix metalloproteinase | <enzyme> Activates gelatinase a; isolated from a human placenta cdna gene library; contains a transmembrane domain; do not use for any other numbered matrix metalloproteinases; genbank d26512 Registry number: EC 3.4.24.- Synonym: mt-mmp, mmp-x1 protein, matrix metalloproteinase, membrane-type, mmp14 gene product, mmp-14 gene product, mt1-mmp, matrix metalloproteinase 14, mt2-mmp, mmp15 gene product, mmp16 gene product (26 Jun 1999) |
| haemorrhagic metalloproteinase | <enzyme> Extracted from vipera berus berus venom; hydrolyzes casein, fibrinogen and splits the insulin b chain at positions ala(14)-leu(15), tyr(16)-leu(17), his(10)-leu(11); digests alpha chain of fibrinogen Registry number: EC 3.4.24.- (26 Jun 1999) |
| Xolloid metalloproteinase | <enzyme> Tolloid-like protein from xenopus with development-regulating activity; acts as a ventralizing agent that mimics low doses of bone morphogenetic protein-4 Registry number: EC 3.4.24.- Synonym: xolloid gene product (26 Jun 1999) |
| S. marcescens minor metalloproteinase | <enzyme> Precursor protein consists of 352 amino acids, mw 38.479 kD from serratia marcescens; mature protein consists of 300 amino acids mw 32.515 kD with optimal activity at pH 8.0 and 50c; do not confuse with smp protein, a membrane protein from E coli Registry number: EC 3.4.24.- Synonym: smp proteinase (26 Jun 1999) |
| Streptococcus faecalis metalloproteinase | <enzyme> Bacterial metalloproteinase from streptococcus faecalis Registry number: EC 3.4.24.- Synonym: streptococcus faecalis metalloendopeptidase, metalloproteinase (streptococcus faecalis), sf-metalloproteinase (26 Jun 1999) |
| a1-trypsin inhibitor | A glycoprotein that is the major protease inhibitor of human serum, is synthesised in the liver, and is genetically polymorphic due to the presence of over 20 alleles; individuals appropriately homozygous are deficient in a1-trypsin and are predisposed to pulmonary emphysema and juvenile hepatic cirrhosis because of alterations in the amino acid and sialic acid components of the glycoprotein. A1-Antitrypsin also inhibits thrombin. Synonym: a1-trypsin inhibitor, human a1-proteinase inhibitor. (05 Mar 2000) |
| ACE inhibitor | <pharmacology> A group of antihypertensive medications that work by inhibiting an enzyme (angiotensin-converting enzyme) that is important in the regulation of blood pressure. Studies have also indicated that it may help prevent or slow the progression of kidney disease in patients with diabetes. Examples include: captopril, ramipril, enalapril, losartan potassium, bepridil and lisinopril. (12 Mar 1998) |
Synonyms : Metalloproteinase-1 Tissue Inhibitor, Tissue Inhibitor of Metalloproteinase 1
Synonyms : Metalloproteinase-2 Tissue Inhibitor, Tissue Inhibitor of Metalloproteinase 2
Synonyms : TIMP-3 Protein, TIMP3 Protein, Metalloproteinase-3 Tissue Inhibitor, TIMP 3 Protein, Tissue Inhibitor of Metalloproteinase 3
Synonyms : Collagenase Inhibitor, TIMP, Inhibitor, Collagenase, Metalloproteinases Tissue Inhibitor
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|