| ¿µ¹® | angiotensin | ÇÑ±Û | ¾ÈÁö¿ÀÅٽŠ|
|---|---|---|---|
| ¼³¸í | ÄáÆÏ¿¡¼ ½ÅÀåÀÇ Ç÷·ù¿Í Ç÷¾ÐÀ» °¨ÁöÇÏ´Â ¼¼Æ÷ÀÎ Ä¡¹Ð¹ÝÁ¡(macula densa)°ú Å丮°ç¼¼Æ÷(JG cell)¿¡¼ Ç÷·ù¿Í Ç÷¾ÐÀÇ ÀúÇϰ¡ ÀÖÀ» °æ¿ì¿¡ ·¹´ÑÀ̶ó´Â ¹°ÁúÀÌ ºÐºñµÇ°Ô µÈ´Ù. ÀÌ ·¹´ÑÀ̶ó´Â ¹°ÁúÀº Ç÷Áß¿¡ Á¸ÀçÇÏ´Â ¾ÈÁö¿ÀÅÙ½ÅÀ̶ó´Â ¹°ÁúÀ» ¾ÈÁö¿ÀÅٽŠIÀ¸·Î º¯È½Ã۰í ÀÌ ¾ÈÁö¿ÀÅٽŠIÀ̶ó´Â ¹°ÁúÀº ¾ÈÁö¿ÀÅٽŠI Àüȯȿ¼Ò¿¡ ÀÇÇØ¼ ¾ÈÁö¿ÀÅÙ½ÅII¶ó´Â ¹°Áú·Î µÈ´Ù. ¾ÈÁö¿ÀÅٽŰú ¾ÈÁö¿ÀÅٽŠIÀ̶ó´Â ¹°ÁúÀº ±× ÀÛ¿ëÀÌ °ÅÀÇ ¾øÁö¸¸ ¾ÈÁö¿ÀÅٽŠII¶ó´Â ¹°ÁúÀº °·ÂÇÏ°Ô Ç÷°ü¼öÃàÀ» ½Ã۰í ÀÌ·Î ÀÎÇØ¼ Ç÷¾ÐÀÇ »ó½ÂÀ» °¡Á®¿À¸ç µ¿½Ã¿¡ ºÎ½ÅÀ» ÀÚ±ØÇÏ¿© ¾Ëµµ½ºÅ×·ÐÀ» ºÐºñÇÏ°Ô ÇÑ´Ù. ¾ÈÁö¿ÀÅÙ½ÅÀ̶õ Ç÷°üÀ» ¼öÃà½ÃŰ°í ¾Ëµµ½ºÅ×·ÐÀÇ ºÐºñ¸¦ À¯µµÇÔÀ¸·Î½á Ç÷¾ÐÀÇ »ó½ÂÀ» °¡Á®¿À´Â ¹°ÁúÀÌ´Ù. ±×¸®°í ±× ÀÛ¿ëÀº ·¹´Ñ-¾ÈÁö¿ÀÅÙ½Å-¾Ëµµ½ºÅ×·ÐÀ¸·Î À̾îÁö´Â ü°è¿¡ ÀÇÇØ¼ Á¶ÀýµÇ°í ÀÌ·ç¾îÁø´Ù. |
||
| ¿µ¹® | serum enzyme | ÇÑ±Û | Ç÷ûȿ¼Ò |
|---|---|---|---|
| ¼³¸í | Ç÷û ³»¿¡ Æ÷ÇԵǾî ÀÖ´Â ¿©·¯ °¡Áö È¿¼Ò¸¦ ÀÏÄ´ ¸»ÀÌ´Ù. |
||
| ¿µ¹® | enzyme | ÇÑ±Û | È¿¼Ò |
|---|---|---|---|
| ¼³¸í | »ý¹°Ã¼ ¼¼Æ÷¼Ó¿¡¼ ÇÕ¼ºµÇ°í, ÁÖ·Î ¼¼Æ÷³»¿¡¼ ÁøÇàµÇ´Â ÈÇйÝÀÀÀ» Ã˸ÅÇÏ´Â ´Ü¹éÁú·Î ½ÃÇè°ü³»¿¡¼µµ °°Àº Ã˸ÅÀÛ¿ëÀ» ÇÑ´Ù. ÀÌ È¿¼Ò´Â ÀΰøÀûÀ¸·Î ¸¸µç ¾î¶² Ã˸ÅÁ¦º¸´Ù ±× ƯÀ̼º°ú Ã˸ÅÀÛ¿ëÀÌ Å¹¿ùÇÑ Æ¯º°ÇÑ »ýüºÐÀÚÀÌ´Ù. ½ÅÁø´ë»ç, Áï ¼¼Æ÷³»¿¡¼ ÀϾ´Â ¹°ÁúÀÇ ÈÇÐÀû º¯È¯Àº È¿¼ÒÀÇ ÀÛ¿ë¿¡ ÀÇÇØ ¸Å¿ì ºü¸£°í ¿øÇÒÇÏ°Ô ÀÌ·ç¾îÁø´Ù. À̰ÍÀº È¿¼ÒÀÇ Ã˸ŠȿÀ²ÀÌ ³ôÀº Á¡°ú È¿¼ÒÀÇ ±âÁú ƯÀ̼º ¶§¹®ÀÌ´Ù. È¿¼Ò¹ÝÀÀÀº »ó¿Â, »ó¾Ð, ÃÖÀû pH µî ÀûÀýÇÑ Á¶°Ç ¾Æ·¡¿¡¼ ÁøÇàµÈ´Ù. ¶Ç È¿¼ÒÀÇ ÁÖü°¡ ´Ü¹éÁúÀ̱⠶§¹®¿¡ ´Ü¹éÁúÀ» º¯¼º½ÃŰ´Â ¿, °»ê, °¾ËÄ®¸®, À¯±â¿ë¸Å µî¿¡ ÀÇÇØ ±× ÀÛ¿ëÀ» ÀҴ´Ù. È¿¼Ò´Â »ýü¿¡ ³Î¸® ºÐÆ÷Çϸç, º¹ÀâÇÏ°í ´Ù¾çÇÑ ´ë»ç¹ÝÀÀÀ» Ã˸ÅÇϱ⠶§¹®¿¡ Á¾·ùµµ ¸¹´Ù. ¾Õ¼ ¸»ÇÑ ¹Ù¿Í °°ÀÌ ´ëºÎºÐÀÇ È¿¼Ò´Â ¼¼Æ÷³»¿¡ Á¸ÀçÇÏÁö¸¸, Ç÷¾×°ú ±×¿ÜÀÇ °£Áú¾×¿¡ µé¾î Àֱ⵵ ÇÏ°í ¼ÒÈÈ¿¼Ò·ùó·³ ü¿Ü·Î ºÐºñµÇ´Â °Íµµ ÀÖ´Ù. |
||
| ¿µ¹® | enzyme-linked immunoabsorbent assay | ÇÑ±Û | È¿¼Ò¸é¿ªÃøÁ¤¹ý |
|---|---|---|---|
| ¼³¸í | È¿¼Ò°áÇո鿪ÈíÂøÁ¦ °ËÁ¤¹ýÀ¸·Î ¹ø¿ªµÇ°í ÀÖ´Ù. ÀÌ ¹ýÀº Ç׿ø(¶Ç´Â Ç×ü)¿¡ ¾ËÄ®¸® Æ÷½ºÆÄŸ¾ÆÁ¦ ¶Ç´Â Æä¸£¿Á½Ãµð¾ÆÁ¦ µîÀÇ »ê¼Ò¸¦ °áÇÕ½ÃÄÑ µÎ°í ±× »ê¼ÒȰ¼ºÀ» ÁöÇ¥·Î »ï¾Æ Ç׿øÇ×ü¹ÝÀÀÀÇ Á¤µµ¸¦ ¾È ´ÙÀ½ ¿©±â¿¡¼ Ç׿ø(¶Ç´Â Ç×ü)ÀÇ ¾çÀ» ±¸ÇÏ´Â °ÍÀÌ´Ù. ÀÌ ¹ýÀÇ ÀÌÁ¡À¸·Î¼ °í°¨µµ, Á¶ÀÛÀÇ °£´ÜÇÔ ¹× ¹æ»ç¼±¸é¿ªÃøÁ¤¹ýó·³ ¹æ»ç¼º¹°ÁúÀ» »ç¿ëÇÏÁö ¾Ê¾Æµµ µÈ´Ù´Â Á¡À» µé ¼ö ÀÖ´Ù. È£¸£¸óÀ̳ª ¸é¿ª±Û·ÎºÒ¸°ÀÇ Á¤·®¹ýÀ¸·Î¼ ÀÀ¿ë µÇ°í ÀÖÀ¸¸ç ÃøÁ¤¿ë ŰƮµµ ½ÃÆÇµÇ°í ÀÌÀÖ´Ù. |
||
| ACEI | angiotensin-converting enzyme inhibitor |
|---|---|
| PACE | Pacing and Clinical Electrophysiology; paired basic amino acid cleaving enzyme; personalized aerobic... |
| ACE | Angiotensin Converting Enzyme = Kininase II = Dipeptidyl Carboxypepti... |
| ACE | acetonitrile; acetylcholine esterase; acute cerebral encephalopathy; acute coronary event; adrenocor... |
| ACEDS | angiotensin-converting enzyme dysfunction syndrome |
| ACEI | Angiotensin Converting Enzyme Inhibitor |
|---|---|
| ACEi | Angiotensin I converting enzyme inhibition |
| ACE inhibitor | angiotensin converting enzyme inhibitor |
| ACE | ANGIOTENSIN CONVERTING ENZYME |
| ACE | Angiotensin converting enzyme activity |
| angiotensin-converting enzyme inhibitor | <pharmacology> A class of drugs used in the treatment of hypertension and heart failure. They exert their haemodynamic effect mainly by inhibiting the renin-angiotensin system and produce a reduction of peripheral arterial resistance. They also modulate sympathetic nervous system activity and increase prostaglandin synthesis. They cause mainly vasodilation and mild natriuresis without affecting heart rate and contractility. (14 Aug 2000) |
|---|---|
| angiotensin-converting enzyme | <enzyme> This hydrolase enzyme cleaves the decapeptide angiotensin I (biologically inactive) to form active angiotensin II by angiotensin-converting enzyme which removes a dipeptide (histidylleucine) from angiotensin I. Angiotensin II causes contraction of vascular smooth muscle and thus raises blood pressure and stimulates aldosterone release from the adrenal glands. Angiotensin is finally broken down by angiotensinases. Elevations in angiotensin converting enzyme are seen sarcoidosis, histoplasmosis, alcoholic cirrhosis, asbestosis, berylliosis, diabetes, Hodgkin's disease, hyperthyroidism, amyloidosis, primary biliary cirrhosis, idiopathic pulmonary fibrosis, pulmonary embolism, scleroderma, silicosis, tuberculosis, Gaucher's disease and leprosy. The normal values are 18 to 67 U/ml over 20 years of age (people under 20 have higher levels). Drugs that inhibit ACE are used to treat hypertension and congestive heart failure. See: angiotensin-converting enzyme inhibitor Acronym: ACE (12 Aug 2000) |
| angiotensin-converting enzyme secretase | <enzyme> Converts ace from a membrane-bound to a soluble form; not inhibited by thiol, serine or acid enzyme inhibitor but is inhibited by edta and 1,10-phenanthroline Registry number: EC 3.4.99.- Synonym: ace secretase (26 Jun 1999) |
| interleukin-1 converting enzyme | <biochemistry> Cytoplasmic cysteine protease that is uniquely responsible for cleaving proIL-1_ (31 or 33 kD) into mature IL-1_ (17.5 kD), the active cytokine is then released by a nonstandard mechanism (there is no signal sequence and it does not pass through the Golgi). The enzyme seems to be composed of two nonidentical subunits derived from a single proenzyme. The ICE gene has some homology with the ced 9 gene of C. Elegans, the product of which is involved in mediating cell death by apoptosis. (11 Mar 1998) |
| vasopressin-converting aminopeptidase | <enzyme> Activity found in brain which converts vasopressin into centrally active metabolites Registry number: EC 3.4.11.- Synonym: vp-c aminopeptidase (26 Jun 1999) |
| dynorphin-converting endopeptidase | <enzyme> Enzyme from human cerebrospinal fluid; cleaves dynorphin a and b and neoendorphin at the arg(6)-arg(7) or arg(6)-lys(7) bonds Registry number: EC 3.4.21.- Synonym: dynorphin-neo-endorphin endopeptidase, dc-endopeptidase (26 Jun 1999) |
| urokinase-converting protease | <enzyme> Degrades synthetic urokinase substrates and stimulates urokinase Registry number: EC 3.4.21.- Synonym: urokinase cofactor (26 Jun 1999) |
| angiotensin | <hormone> A family of oligopeptides ranging in size from angiotensin precursors with 14 amino acids to the active vasoconstrictor angiotensin II with 8 amino acids, or their analogs or derivatives. The amino acid content varies with the species and changes in that content produce antagonistic or inactive compounds. Angiotensinogen (renin substrate) is a 60 kD polypeptide released from the liver and cleaved in the circulation by renin to form the biologically inactive decapeptide angiotensin I. This is in turn cleaved to form active angiotensin II by Angiotensin-converting Enzyme (ACE). Angiotensin II causes contraction of vascular smooth muscle and thus raises blood pressure and stimulates aldosterone release from the adrenal glands. Angiotensin is finally broken down by angiotensinases. (12 Aug 2000) |
| angiotensin amide | <chemical> 1-l-asparagine-5-l-valine-angiotensin II. The octapeptide amide of bovine angiotensin II used to increase blood pressure by vasoconstriction. Pharmacological action: vasoconstrictor agents. Chemical name: Angiotensin II, 1-L-asparagine-5-L-valine- (12 Dec 1998) |
| angiotensin I | <chemical> The decapeptide precursor of angiotensin II, generated by the action of renin on angiotensinogen. It has limited pharmacologic activity. Chemical name: Angiotensin I (12 Dec 1998) |
| angiotensin II | <chemical> The active form of angiotensin. An octapeptide found in blood, it is synthesised from angiotensin I and quickly destroyed. Angiotensin II causes profound vasoconstriction with resulting increase in blood pressure. The clinically and experimentally used bovine form has valine in position 5 where the human form has isoleucine. Pharmacological action: vasoconstrictor agents. Chemical name: Angiotensin II (12 Dec 1998) |
| angiotensin III | <chemical> A heptapeptide formed by the enzymatic hydrolysis of angiotensin II. It has greater activity than angiotensin II for stimulating aldosterone synthesis and in the release of prostaglandins but only 20% of the pressor activity. Chemical name: Angiotensin II, 1-de-L-aspartic acid- (12 Dec 1998) |
| angiotensin I (Phe 8-His 9) hydrolase | <enzyme> Cleaves the cooh-terminal dipeptide his(9)-leu(10) from the decapeptide angiotensin i Registry number: EC 3.4.15.- Synonym: atypical angiotensin-converting enzyme (26 Jun 1999) |
| angiotensin precursor | angiotensin |
| angiotensin-related carboxypeptidase | <enzyme> Rat and bovine brain synaptosomal enzyme can hydrolyze angiotensin I to des-leu angiotensin I, but no further Registry number: EC 3.4.- Synonym: angiotensin-specific carboxypeptidase (26 Jun 1999) |
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¿© |
|---|