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  • ¿µ¹®
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  • enzyme precursor
    È¿¼ÒÀü±¸¹°Áú
  • precursor
    Àü±¸¹°Áú
  • angiotensin
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  • angiotensin converting enzyme
    ¾ØÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò
  • angiotensin converting enzyme inhibitor
    ¾ØÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò¾ïÁ¦Á¦
  • renin-angiotensin-aldosterone system
    ·¹´Ñ-¾ØÁö¿ÀÅÙ½Å-¾Ëµµ½ºÅ׷аèÅë
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  • ¿µ¹®
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  • precursor
    Àü±¸¹°Áú
  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
  • angiotensin converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò
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  • ¿µ¹®
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  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
  • angiotensin converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò
  • enzyme precursor
    È¿¼ÒÀü±¸Ã¼
  • precursor
    Àü±¸¹°Áú
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  • ¿µ¹®
    ÇѱÛ
  • DNA precursor
    DNA Àü±¸Ã¼, -¹°Áú
  • abnormal localization of immature precursor cells=ALIP
    ¹Ì¼º¼÷Àü±¸¼¼Æ÷ÀÇ ºñÁ¤»ó ±¹Àç
  • inactive precursor
    ºñȰ¼º Àü±¸¹°Áú.
  • ACE : angiotensin converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò.
  • ACE=> angiotensin converting enzyme
    ¾ÈÁö¿ÀÅٽŠÀüȯȿ¼Ò(ï®üµý£áÈ)
  • ACEI : angiotensin converting enzyme inhibitor
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò¾ïÁ¦Á¦(ï®ü½ý£áÈåäð¤ð¥).
  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
  • angiotensin converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò.
  • angiotensin converting enzyme inbibitor
    ¾ÈÁö¿ÀÅٽŠÀüȯȿ¼Ò ¾ïÁ¦¹°Áú<¾à>.
  • angiotensin converting enzyme inhibitor
    ¾ÈÁö¿ÀÅٽŠÀüȯȿ¼Ò ¾ïÁ¦¹°Áú<¾à>.
  • angiotensin ii
    ¾ÈÁö¿ÀÅÙ½ÅII
  • angiotensin-converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò
  • renin angiotensin aldosterone pressor
    ·¹´Ñ¾ÈÁö¿ÀÅٽž˵µ½ºÅ׷н ¾Ð°è(¡­ã°äâ
  • renin angiotensin system
    ·¹´Ñ¾ÈÁö¿ÀÅٽŰè(¡­Í§).
  • renin-angiotensin system
    ·¹´Ñ¾ÈÁö¿ÀÅÙ½Åü°è
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  • ¿µ¹®
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  • abnormal localization of immature precursor cells=ALIP
    ¹Ì¼º¼÷Àü±¸¼¼Æ÷ÀÇ ºñÁ¤»ó ±¹Àç
  • cell, precursor
    Àü±¸¼¼Æ÷
  • enzyme precursor
    È¿¼ÒÀü±¸Ã¼.
  • inactive precursor
    ºñȰ¼º Àü±¸¹°Áú.
  • thymic precursor cells
  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
  • angiotensin converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò.
  • angiotensin converting enzyme inbibitor
    ¾ÈÁö¿ÀÅٽŠÀüȯȿ¼Ò ¾ïÁ¦¹°Áú<¾à>.
  • angiotensin converting enzyme inhibitor
    ¾ÈÁö¿ÀÅٽŠÀüȯȿ¼Ò ¾ïÁ¦¹°Áú<¾à>.
  • angiotensin ii
    ¾ÈÁö¿ÀÅÙ½ÅII
  • angiotensin-converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò
  • renin angiotensin aldosterone pressor
    ·¹´Ñ¾ÈÁö¿ÀÅٽž˵µ½ºÅ׷н ¾Ð°è(¡­ã°äâ
  • renin angiotensin system
    ·¹´Ñ¾ÈÁö¿ÀÅٽŰè(¡­Í§).
  • renin-angiotensin system
    ·¹´Ñ¾ÈÁö¿ÀÅÙ½Åü°è
  • renin-angiotensin system
    ·¹´Ñ-¾ÈÁö¿ÀÅٽŰè(¡­Ìõ)
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  • angiotensin I
    ¾ÈÁö¿ÀÅٽŠI
  • angiotensin II
    ¾ÈÁö¿ÀÅٽŠII
  • precursor fragments
    Àü±¸¹°(îñÏÌÚª) Á¶°¢
  • precursor of serum prothrombin conversion accelerator
    Ç÷û(úìôè)ÇÁ·ÎÆ®·Òºó Àüȯ°¡¼ÓÁ¦ Àü±¸¹°Áú(ï®üµÊ¥áÜð¥îñÏÌÚªòõ)
  • precursor ribosomal RNA
    ¶óÀ̺¸¼Ø RNA
  • precursor transfer RNA
    Àü´Þ(îîÓ¹) RNA Àü±¸Ã¼(îñÏÌô÷)
  • ribosomal precursor RNA
    ¶óÀ̺¸¼Ø Àü±¸(îñÏÌ) RNA
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  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
  • precursor
    Àü±¸Ã¼, Àü±¸ ¹°Áú, Àü´Ü°è¹°Áú
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APP acute phase protein; alum-precipitated pyridine; aminopyrazolopyrimidine; amyloid peptide precursor;...
ECP ectrodactyly-cleft palate [syndrome]; effector cell precursor; endocardial potential; eosinophil cat...
APUD Amine Precursor Uptake & Decarboxylation
ALIP abnormal localized immature mye-loid precursor
APLP amyloid precursor-like protein
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APUD Amine Precursor Uptake and Decarboxylation
APP Amyloid Precursor Protein
APLP amyloid precursor-like protein
APP Amyloid Protein Precursor
APP Amyloid beta precursor protein
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    ¼³¸í
  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
    1. °­·ÂÇÑ Ç÷°ü ¼öÃà ÀÛ¿ë°ú ºÎ½Å ÇÇÁú¿¡¼­ÀÇ ¾Ëµµ½ºÅ×·Ð »ýÇÕ¼º ¹× ºÐºñ ÃËÁøÀÛ¿ëÀÌ ÀÖ´Ù. ºÐÀÚ·®À» ±âÁØÀ¸·Î ³ë¿¡Çdz×ÇÁ¸°¿¡ ºñÇØ ¾à 40¹è³ª °­ÇÑ Ç÷¾Ð »ó½Â È¿°ú¸¦ °¡Áö°í ÀÖ´Ù. 2. Ç÷¾×¿¡ Á¸ÀçÇÏ´Â Æú¸® ÆéŸÀ̵å·Î¼­ Ç÷ÀåÀÇ ·¹´Ñ°ú Ç÷û a2 ±Û·ÎºÒ¸°¿¡ ÀÇÇÏ¿© Çü¼ºµÈ´Ù. deca
  • angiotensin converting enzyme
    ¾ÈÁö¿ÀÅٽŠÀüȯ È¿¼Ò
  • angiotensin I
    ¾ÈÁö¿ÀÅٽŠI
    ºÒȰ¼ºÇüÀ¸·Î ÆéŸÀÌµå ºÐÇØ È¿¼ÒÀÇ ÀÛ¿ë¿¡ ÀÇÇÏ¿© ¿ÁŸÆéŸÀ̵åÀÇ ¾ÈÁö¿ÀÅٽŠ¥±·Î ÀüȯµÈ´Ù. À̰ÍÀÌ °­·ÂÇÑ Ç÷°ü ¼öÃà ¹°ÁúÀÌ¸ç ¶ÇÇÑ ºÎ½Å ÇÇÁú¿¡¼­ ¾Ëµµ½ºÅ×·Ð ºÐºñ ÃËÁø ¹°ÁúÀ̱⵵ ÇÏ´Ù.
  • angiotensin-converting enzyme
    ¾ÈÁö¿ÀÅٽŠÀüȯ È¿¼Ò
  • amine precursor uptake
    ¾Æ¹Î Àü±¸Ã¼ Èí¼ö
  • cartilagenous precursor
    ¿¬°ñ Àü±¸Ã¼
    ¿¬°ñÀÇ ¼±ÇàÇÏ´Â ¹°Áú·Î¼­, »ý¹°ÇÐÀû °úÁ¤¿¡ À־ Åë»óÀûÀ¸·Î ¿¬°ñ·ÎºÎÅÍ È°¼ºµµ°¡ ´õ ³ôµç°¡ º¸´Ù ¼º¼÷µÈ ¹°ÁúÀÌ »ý¼ºµÈ´Ù.
  • enzyme precursor
    È¿¼Ò Àü±¸Ã¼
  • phylogenetic precursor
    °èÅë ¹ß»ýÇÐÀû Àü±¸ ¹°Áú
  • precursor
    Àü±¸Ã¼, Àü±¸ ¹°Áú, Àü´Ü°è ¹°Áú
  • precursor peptide
    Àü±¸ ÆéƼµå
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
angiotensin precursor angiotensin
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Amine Precursor Uptake and Decarboxylation <pharmacology, physiology> Paracrine cells of which argentaffin cells are an example. Usage of the term APUD is neither helpful nor memorable.
Acronym: APUD
(11 Nov 1997)
amyloid beta-protein precursor A precursor to the amyloid-beta protein (beta/a4). Alterations in the expression of the amyloid beta-protein precursor (abpp) gene, located on chromosome 21, plays a role in the development of the neuropathology common to both alzheimer disease and down syndrome. Abpp is associated with the extensive extracellular matrix secreted by neuronal cells. Upon cleavage, this precursor produces three proteins of varying amino acid lengths: 695, 751, and 770. The beta/a4 (695 amino acids) or beta-amyloid protein is the principal component of the extracellular amyloid in senile plaques found in alzheimer disease, down syndrome and, to a limited extent, in normal aging.
(12 Dec 1998)
amyloid precursor protein <protein> Individuals with Alzheimer's disease are characterised by extensive accumulation of amyloid in the brain, referred to as senile plaques. These consist of a core of amyloid fibrils surrounded by dystrophic neurites. The principal component of the amyloid fibrils is B/A4, a peptide derived from the larger APP. The specific role of amyloid protein is unclear but it is thought that amyloid deposits may cause neurons to degenerate. Amyloid deposits also occur in brains of older Down's Syndrome patients.
(04 May 1997)
precursor Something that precedes.
1. <biochemistry> In biological processes, a substance from which another, usually more active or mature substance is formed.
2. In clinical medicine, a sign or symptom that heralds another.
Origin: L. Praecursor = a forerunner
(18 Nov 1997)
enzyme precursor <biochemistry> Inactive precursors that can be converted to active enzymes.
Enzyme precursors containing extra-long polypeptide chains that block activity are activated by acid or enzymatic hydrolysis to remove the inhibiting portion.
(12 Dec 1998)
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-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 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 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)
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-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)
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  • precursor
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