Carboxypeptidase B2

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Carboxypeptidase B2 (plasma)
Identifiers
Symbol(s) CPB2; PCPB; CPU; TAFI
External IDs OMIM: 603101 MGI1891837 HomoloGene55610
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 1361 56373
Ensembl ENSG00000080618 ENSMUSG00000021999
Uniprot Q96IY4 Q9JHH6
Refseq NM_001872 (mRNA)
NP_001863 (protein)
NM_019775 (mRNA)
NP_062749 (protein)
Location Chr 13: 45.53 - 45.58 Mb Chr 14: 73.98 - 74.02 Mb
Pubmed search [1] [2]

Carboxypeptidase B2 (plasma), also known as CPB2, is a human gene.

Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for this gene and its promoter region. Available sequence data analyses indicate splice variants that encode different isoforms.[1]

[edit] See also

[edit] References

[edit] Further reading

  • Bouma BN, Mosnier LO (2005). "Thrombin activatable fibrinolysis inhibitor (TAFI) at the interface between coagulation and fibrinolysis.". Pathophysiol. Haemost. Thromb. 33 (5-6): 375-81. doi:10.1159/000083832. PMID 15692247. 
  • Marinkovic DV, Marinkovic JN, Erdös EG, Robinson CJ (1977). "Purification of carboxypeptidase B from human pancreas.". Biochem. J. 163 (2): 253-60. PMID 17398. 
  • Tsai SP, Drayna D (1992). "The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome 13.". Genomics 14 (2): 549-50. PMID 1427879. 
  • Eaton DL, Malloy BE, Tsai SP, et al. (1991). "Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma.". J. Biol. Chem. 266 (32): 21833-8. PMID 1939207. 
  • Pascual R, Burgos FJ, Salva M, et al. (1989). "Purification and properties of five different forms of human procarboxypeptidases.". Eur. J. Biochem. 179 (3): 609-16. PMID 2920728. 
  • Valnickova Z, Thogersen IB, Christensen S, et al. (1996). "Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein.". J. Biol. Chem. 271 (22): 12937-43. PMID 8662763. 
  • Bajzar L, Morser J, Nesheim M (1996). "TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex.". J. Biol. Chem. 271 (28): 16603-8. PMID 8663147. 
  • Vanhoof G, Wauters J, Schatteman K, et al. (1997). "The gene for human carboxypeptidase U (CPU)--a proposed novel regulator of plasminogen activation--maps to 13q14.11.". Genomics 38 (3): 454-5. doi:10.1006/geno.1996.0656. PMID 8975730. 
  • Zhao L, Morser J, Bajzar L, et al. (1999). "Identification and characterization of two thrombin-activatable fibrinolysis inhibitor isoforms.". Thromb. Haemost. 80 (6): 949-55. PMID 9869166. 
  • Boffa MB, Reid TS, Joo E, et al. (1999). "Characterization of the gene encoding human TAFI (thrombin-activable fibrinolysis inhibitor; plasma procarboxypeptidase B).". Biochemistry 38 (20): 6547-58. doi:10.1021/bi990229v. PMID 10350473. 
  • Matsumoto A, Itoh K, Matsumoto R (2000). "A novel carboxypeptidase B that processes native beta-amyloid precursor protein is present in human hippocampus.". Eur. J. Neurosci. 12 (1): 227-38. PMID 10651877. 
  • Marx PF, Hackeng TM, Dawson PE, et al. (2000). "Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage.". J. Biol. Chem. 275 (17): 12410-5. PMID 10777524. 
  • Mosnier LO, Lisman T, van den Berg HM, et al. (2002). "The defective down regulation of fibrinolysis in haemophilia A can be restored by increasing the TAFI plasma concentration.". Thromb. Haemost. 86 (4): 1035-9. PMID 11686321. 
  • Mosnier LO, Meijers JC, Bouma BN (2002). "The role of protein S in the activation of thrombin activatable fibrinolysis inhibitor (TAFI) and regulation of fibrinolysis.". Thromb. Haemost. 86 (4): 1040-6. PMID 11686322. 
  • Mosnier LO, Elisen MG, Bouma BN, Meijers JC (2002). "Protein C inhibitor regulates the thrombin-thrombomodulin complex in the up- and down regulation of TAFI activation.". Thromb. Haemost. 86 (4): 1057-64. PMID 11686324. 
  • Morange PE, Aillaud MF, Nicaud V, et al. (2002). "Ala147Thr and C+1542G polymorphisms in the TAFI gene are not associated with a higher risk of venous thrombosis in FV Leiden carriers.". Thromb. Haemost. 86 (6): 1583-4. PMID 11776333. 
  • Schneider M, Nagashima M, Knappe S, et al. (2002). "Amino acid residues in the P6-P'3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation.". J. Biol. Chem. 277 (12): 9944-51. doi:10.1074/jbc.M111685200. PMID 11786552. 
  • Koschinsky ML, Boffa MB, Nesheim ME, et al. (2002). "Association of a single nucleotide polymorphism in CPB2 encoding the thrombin-activable fibrinolysis inhibitor (TAF1) with blood pressure.". Clin. Genet. 60 (5): 345-9. PMID 11903334. 
  • Yano Y, Gabazza EC, Hori Y, et al. (2002). "Association between plasma thrombin-activatable fibrinolysis inhibitor levels and activated protein C in normotensive type 2 diabetic patients.". Diabetes Care 25 (7): 1245-6. PMID 12087030. 
  • Antovic JP, Blombäck M (2003). "Thrombin-activatable fibrinolysis inhibitor antigen and TAFI activity in patients with APC resistance caused by factor V Leiden mutation.". Thromb. Res. 106 (1): 59-62. PMID 12165290. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.