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the 21st letter of the Roman alphabet (同)u
(chiefly British) of or appropriate to the upper classes especially in language use

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uraniumの化学記号
上流の,上流階級にふさわしい / (映画が)児童観覧用の

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/10/17 21:19:03」(JST)

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Carboxypeptidase U (EC 3.4.17.20, arginine carboxypeptidase, carboxypeptidase R, plasma carboxypeptidase B, thrombin-activatable fibrinolysis inhibitor) is an enzyme.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

Release of C-terminal Arg and Lys from a polypeptide

Pro-carboxypeptidase U in (human) plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U.

References

^ Eaton, D.L., Malloy, B.E., Tsai, S.P., Henzel, W. and Drayna, D. (1991). "Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma". J. Biol. Chem. 266: 21833–21838. PMID 1939207.
^ Shinohara, T., Sakurada, C., Suzuki, T., Takeuchi, O., Campbell, W., Ikeda, S., Okada, N. and Okada, H. (1994). "Pro-carboxypeptidase R cleaves bradykinin following activation". Int. Arch. Allergy Immunol. 103: 400–404. doi:10.1159/000236661. PMID 8130654.
^ Wang, W., Hendriks, D.F. and Scharpé, S. (1994). "Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen". J. Biol. Chem. 269: 15937–15944. PMID 8195249.
^ Tan, A.K. and Eaton, D.L. (1995). "Activation and characterization of procarboxypeptidase B from human plasma". Biochemistry 34: 5811–5816. doi:10.1021/bi00017a012. PMID 7727441.
^ Broze, G.J., Jr. and Higuchi, D.A. (1996). "Coagulation-dependent inhibition of fibrinolysis: Role of carboxypeptidase U and the premature lysis of clots from hemophilic plasma". Blood 88: 3815–3823. PMID 8916945.

External links

Carboxypeptidase U at the US National Library of Medicine Medical Subject Headings (MeSH)

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English Journal

Activation of protein C and thrombin activable fibrinolysis inhibitor on cultured human endothelial cells.

Wu C1,2, Kim PY1,2, Swystun LL3, Liaw PC1,2, Weitz JI1,2,4.
Journal of thrombosis and haemostasis : JTH.J Thromb Haemost.2016 Feb;14(2):366-74. doi: 10.1111/jth.13222. Epub 2016 Feb 1.
Essentials It is unknown if thrombin activatable fibrinolysis inhibitor (TAFI) and protein C compete on cells. TAFI and protein C activation on endothelial cells was simultaneously quantified. TAFI and protein C do not compete for activation on endothelial cells. TAFI and protein C are independently
PMID 26663133

Structure-function relationships in Thrombin-activatable Fibrinolysis Inhibitor.

Plug T1, Meijers JC1,2.
Journal of thrombosis and haemostasis : JTH.J Thromb Haemost.2016 Jan 20. doi: 10.1111/jth.13261. [Epub ahead of print]
Thrombin-activatable fibrinolysis inhibitor (TAFI) is an important regulator in the balance of coagulation and fibrinolysis. TAFI is a metallocarboxypeptidase that circulates in plasma as zymogen. Activated TAFI (TAFIa) cleaves C-terminal lysine or arginine residues from peptide substrates. The remo
PMID 26786060

Comparative proteome analysis of saccular intracranial aneurysms with iTRAQ quantitative proteomics.

Wang J1, Yu L1, Huang X2, Wang Y2, Zhao J3.
Journal of proteomics.J Proteomics.2016 Jan 1;130:120-8. doi: 10.1016/j.jprot.2015.09.014. Epub 2015 Sep 15.
OBJECTIVE: To screen differentially expressed proteins of saccular intracranial aneurysms and superficial temporal artery by the proteomics analysis using isobaric tags for relative and absolute quantification (iTRAQ) combined with reverse phase high-performance liquid chromatography.METHODS: Collec
PMID 26385002

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Stem Cell Reports 6(1), 18-25, 2016-01-12
NAID 120005745633

An Investigation into the Gastrointestinal Stability of Exenatide in the Presence of Pure Enzymes, Everted Intestinal Rings and Intestinal Homogenates

Biological and Pharmaceutical Bulletin 39(1), 42-48, 2016
NAID 130005116507

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日本生物工学会大会講演要旨集 67, 207, 2015-09-25
NAID 110010009218

「U」

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Carboxypeptidase U
Identifiers
EC number	3.4.17.20
CAS number	156621-18-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
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PDB structures	RCSB PDB PDBe PDBsum
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「carboxypeptidase」

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カルボキシペプチダーゼ

[1] Eaton, D.L., Malloy, B.E., Tsai, S.P., Henzel, W. and Drayna, D. (1991). "Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma". J. Biol. Chem. 266: 21833–21838. PMID 1939207.

[2] Shinohara, T., Sakurada, C., Suzuki, T., Takeuchi, O., Campbell, W., Ikeda, S., Okada, N. and Okada, H. (1994). "Pro-carboxypeptidase R cleaves bradykinin following activation". Int. Arch. Allergy Immunol. 103: 400–404. doi:10.1159/000236661. PMID 8130654.

[3] Wang, W., Hendriks, D.F. and Scharpé, S. (1994). "Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen". J. Biol. Chem. 269: 15937–15944. PMID 8195249.

[4] Tan, A.K. and Eaton, D.L. (1995). "Activation and characterization of procarboxypeptidase B from human plasma". Biochemistry 34: 5811–5816. doi:10.1021/bi00017a012. PMID 7727441.

[5] Broze, G.J., Jr. and Higuchi, D.A. (1996). "Coagulation-dependent inhibition of fibrinolysis: Role of carboxypeptidase U and the premature lysis of clots from hemophilic plasma". Blood 88: 3815–3823. PMID 8916945.

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carboxypeptidase U