プラスミン・インヒビター、プラスミン阻害因子

関: antifibrinolytic agent、antifibrinolytics、antiplasmin

WordNet

limit, block, or decrease the action or function of; "inhibit the action of the enzyme"; "inhibit the rate of a chemical reaction"
control and refrain from showing; of emotions, desires, impulses, or behavior (同)bottle up, suppress
limit the range or extent of; "Contact between the young was inhibited by strict social customs"
a substance that retards or stops an activity
an enzyme that dissolves the fibrin of blood clots (同)fibrinolysin

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/02/18 16:05:11」(JST)

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[Wiki en表示]

Alpha 2-antiplasmin (or α₂-antiplasmin or plasmin inhibitor) is a serine protease inhibitor (serpin) responsible for inactivating plasmin, an important enzyme that participates in fibrinolysis and degradation of various other proteins. This protein is encoded by the SERPINF2 gene.^[1]

Fibrinolysis (simplified). Blue arrows denote stimulation, and red arrows inhibition.

Role in disease

Very few cases (<20) of A2AP deficiency have been described. As plasmin degrades blood clots, impaired inhibition of plasmin leads to a bleeding tendency, which was severe in the cases reported.

In liver cirrhosis, there is decreased production of alpha 2-antiplasmin, leading to decreased inactivation of plasmin and an increase in fibrinolysis. This is associated with an increase risk of bleeding in liver disease. ^[2]

Interactions

Alpha 2-antiplasmin has been shown to interact with Plasmin^[3]^[4] and Neutrophil elastase.^[4]^[5]

References

^ "Entrez Gene: SERPINF2 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5345.
^ Sattar, Husain. Fundamentals of Pathology. Pathoma LLC, 2011, p. 36.
^ Wiman, B; Collen D (September 1979). "On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin". J. Biol. Chem. (UNITED STATES) 254 (18): 9291–7. ISSN 0021-9258. PMID 158022.
^ ^a ^b Shieh, B H; Travis J (May. 1987). "The reactive site of human alpha 2-antiplasmin". J. Biol. Chem. (UNITED STATES) 262 (13): 6055–9. ISSN 0021-9258. PMID 2437112.
^ Brower, M S; Harpel P C (August 1982). "Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase". J. Biol. Chem. (UNITED STATES) 257 (16): 9849–54. ISSN 0021-9258. PMID 6980881.

External links

The MEROPS online database for peptidases and their inhibitors: I04.023
alpha-2+Antiplasmin at the US National Library of Medicine Medical Subject Headings (MeSH)
SERPINF2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

This article on a gene on chromosome 17 is a stub. You can help Wikipedia by expanding it.

UpToDate Contents

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1. 止血の概要 overview of hemostasis
2. 血管内皮機能および血栓溶解療法の基本的メカニズム vascular endothelial function and fundamental mechanisms of fibrinolysis thrombolysis
3. 血栓溶解異常による血栓性および出血性疾患 thrombotic and hemorrhagic disorders due to abnormal fibrinolysis
4. 糸球体半月体形成の機序 mechanisms of glomerular crescent formation
5. 遺伝性血管浮腫：一般診療および長期予防 hereditary angioedema general care and long term prophylaxis

English Journal

Synthesis and evaluation of tripeptidic plasmin inhibitors with nitrile as warhead.

Teno N, Otsubo T, Gohda K, Wanaka K, Sueda T, Ikeda K, Hijikata-Okunomiya A, Tsuda Y.SourceHiroshima International University, Faculty of Pharmaceutical Sciences, 5-1-1, Hirokoshingai, Kure, Hiroshima, 737-0112, Japan.
Journal of peptide science : an official publication of the European Peptide Society.J Pept Sci.2012 Sep 7. doi: 10.1002/psc.2442. [Epub ahead of print]
Plasmin is best known as the key molecule in the fibrinolytic system, which is critical for clot lysis and can initiate matrix metalloproteinase (MMP) activation cascade. Along with MMP, plasmin is suggested to be involved in physiological processes that are linked to the risk of carcinoma formation
PMID 22961872

Effects of antithrombin and gabexate mesilate on disseminated intravascular coagulation: a preliminary study.

Nishiyama T, Kohno Y, Koishi K.AbstractPURPOSE: We hypothesized that antithrombin is more effective for disseminated intravascular coagulation (DIC) than is gabexate mesilate, which is a protease inhibitor, suggested from the previous studies. Initially, we compared the effects of antithrombin and gabexate mesilate for treating infection-related DIC.
The American journal of emergency medicine.Am J Emerg Med.2012 Sep;30(7):1219-23. Epub 2011 Dec 26.
PURPOSE: We hypothesized that antithrombin is more effective for disseminated intravascular coagulation (DIC) than is gabexate mesilate, which is a protease inhibitor, suggested from the previous studies. Initially, we compared the effects of antithrombin and gabexate mesilate for treating infection
PMID 22204993

Japanese Journal

A Class of Novel Plasmin Inhibitors

GOHDA Keigo,TENO Naoki,WANAKA Keiko,TSUDA Yuko
Peptide science : proceedings of the ... Japanese Peptide Symposium 2010, 259, 2011-03-01
NAID 10028238100

Novel Situations of Endothelial Injury in Stroke — Mechanisms of Stroke and Strategy of Drug Development: Novel Mechanism of the Expression and Amplification of Cell Surface–Associated Fibrinolytic Activity Demonstrated by Real-Time Imaging Analysis

Suzuki Yuko,Urano Tetsumei
Journal of Pharmacological Sciences 116(1), 19-24, 2011
… PA inhibitor-1 (PAI-1) facilitated dissociation of tPA-GFP by forming a high molecular weight complex. …
NAID 130000663523

「antiplasmin」

Serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2
Identifiers
Symbols	SERPINF2; A2AP; AAP; ALPHA-2-PI; API; PLI
External IDs	OMIM: 613168 MGI: 107173 HomoloGene: 719 GeneCards: SERPINF2 Gene
Gene Ontology
Molecular function	• protease binding; • endopeptidase inhibitor activity; • serine-type endopeptidase inhibitor activity; • protein binding; • protein homodimerization activity; • eukaryotic cell surface binding;
Cellular component	• extracellular region; • fibrinogen complex; • extracellular space; • platelet alpha granule lumen;
Biological process	• regulation of blood vessel size by renin-angiotensin; • platelet degranulation; • acute-phase response; • blood coagulation; • response to organic substance; • negative regulation of plasminogen activation; • negative regulation of endopeptidase activity; • regulation of proteolysis; • platelet activation; • collagen fibril organization; • positive regulation of collagen biosynthetic process; • fibrinolysis; • positive regulation of cell differentiation; • positive regulation of transcription from RNA polymerase II promoter; • positive regulation of JNK cascade; • blood vessel morphogenesis; • positive regulation of smooth muscle cell proliferation; • positive regulation of stress fiber assembly; • negative regulation of fibrinolysis; • positive regulation of ERK1 and ERK2 cascade; • positive regulation of transforming growth factor beta production; • positive regulation of cell-cell adhesion mediated by cadherin;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

adj.

抗プラスミンの

n.

抗プラスミン薬

関: antifibrinolytic agent、antifibrinolytics、plasmin inhibitor

「antifibrinolytics」

　　[★]

抗線溶薬

関: antifibrinolytic、antifibrinolytic agent、antiplasmin、plasmin inhibitor

「プラスミン・インヒビター」

　　[★]

英: plasmin inhibitor
関: プラスミン阻害因子、抗線溶薬、抗プラスミン薬

「antifibrinolytic agent」

　　[★]

抗線溶薬

関: antifibrinolytic、antifibrinolytics、antiplasmin、plasmin inhibitor

「プラスミン阻害因子」

　　[★]

英: plasmin inhibitor
関: プラスミン・インヒビター

「plasmin α2-plasmin inhibitor complex」

　　[★] プラスミン・α2プラスミンインヒビター複合体

「α2-plasmin inhibitor deficiency」

　　[★] α2-プラスミンインヒビター欠乏症

「inhibit」

　　[★]

v.

抑制する、阻害する、阻止する

関: abrogate、block、depress、depression、deter、inhibition、interdict、prevent、prevention、repress、repression、restrain、restraint、suppress、suppression

「inhibitor」

　　[★]

n.

阻害剤、阻害薬、抑制薬、抑制剤、(内在性物質について)インヒビター、抑制物質

関: blocker、depressant、suppressant

[entrez-1] "Entrez Gene: SERPINF2 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5345.

[2] Sattar, Husain. Fundamentals of Pathology. Pathoma LLC, 2011, p. 36.

[pmid158022-3] Wiman, B; Collen D (September 1979). "On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin". J. Biol. Chem. (UNITED STATES) 254 (18): 9291–7. ISSN 0021-9258. PMID 158022.

[pmid2437112-4] Shieh, B H; Travis J (May. 1987). "The reactive site of human alpha 2-antiplasmin". J. Biol. Chem. (UNITED STATES) 262 (13): 6055–9. ISSN 0021-9258. PMID 2437112.

[pmid6980881-5] Brower, M S; Harpel P C (August 1982). "Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase". J. Biol. Chem. (UNITED STATES) 257 (16): 9849–54. ISSN 0021-9258. PMID 6980881.

リンク元	「antiplasmin」「antifibrinolytics」「プラスミン・インヒビター」「antifibrinolytic agent」「プラスミン阻害因子」
拡張検索	「plasmin α2-plasmin inhibitor complex」「α2-plasmin inhibitor deficiency」
関連記事	「inhibit」「inhibitor」

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案内

plasmin inhibitor