Carboxypeptidase B2: Difference between revisions

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'''Carboxypeptidase B2''' ('''CPB2'''), also known as '''carboxypeptidase U''' ('''CPU'''), '''plasma carboxypeptidase B''' (pCPB) or '''thrombin-activatable fibrinolysis inhibitor''' ('''TAFI'''), is an [[enzyme]] that, in humans, is encoded by the [[gene]] ''CPB2''.<ref name="pmid1939207">{{cite journal |vauthors=Eaton DL, Malloy BE, Tsai SP, Henzel W, Drayna D |title=Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma |journal=J Biol Chem |volume=266 |issue=32 |pages=21833–8 |date=Dec 1991 |pmid=1939207 |pmc= |doi=}}</ref><ref name="pmid1427879">{{cite journal |vauthors=Tsai SP, Drayna D |title=The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome 13 |journal=Genomics |volume=14 |issue=2 |pages=549–50 |date=Dec 1992 |pmid=1427879 |pmc= |doi=10.1016/S0888-7543(05)80268-X}}</ref>
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| update_citations = yes
==Function==
}}
CPB2 is synthesized by the liver<ref name="Williams2010-8">Kaushansky K, Lichtman M, Beutler E, Kipps T, Prchal J, Seligsohn U. (2010; edition 8: pages 1833-1834 and 2040-2041) ''Williams Hematology''. McGraw-Hill. {{ISBN|978-0071621519}}</ref> and circulates in the plasma as a [[plasminogen]]-bound [[zymogen]]. When it is activated by proteolysis at residue Arg92 by the [[thrombin]]/[[thrombomodulin]] complex, CPB2 exhibits carboxypeptidase activity. Activated CPB2 reduces fibrinolysis by removing the [[fibrin]] [[C-terminus|C-terminal]] residues that are important for the binding and activation of [[plasminogen]].<ref name="pmid9869166">{{cite journal |vauthors=Zhao L, Morser J, Bajzar L, Nesheim M, Nagashima M | title = Identification and characterization of two thrombin-activatable fibrinolysis inhibitor isoforms | journal = Thromb. Haemost. | volume = 80 | issue = 6 | pages = 949–55 |date=December 1998 | pmid = 9869166 | doi = | url = }}</ref><ref name="pmid10350473">{{cite journal |vauthors=Boffa MB, Reid TS, Joo E, Nesheim ME, Koschinsky ML | title = Characterization of the gene encoding human TAFI (thrombin-activable fibrinolysis inhibitor; plasma procarboxypeptidase B) | journal = Biochemistry | volume = 38 | issue = 20 | pages = 6547–58 |date=May 1999 | pmid = 10350473 | doi = 10.1021/bi990229v | url = }}</ref>
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{{GNF_Protein_box
[[Carboxypeptidase]]s 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 [[thrombin]] and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates [[fibrinolysis]].<ref name = "entrez">{{cite web | title = Entrez Gene: CPB2 carboxypeptidase B2 (plasma)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1361| accessdate = }}</ref>
| image =
 
| image_source =
{|
| PDB =
|[[Image:Fibrinolysis.png|left|framed|Fibrinolysis (simplified). Blue arrows denote stimulation, and red arrows inhibition.]]
| Name = Carboxypeptidase B2 (plasma)
|}
| HGNCid = 2300
 
| Symbol = CPB2
==Isozymes==
| AltSymbols =; PCPB; CPU; TAFI
Polymorphisms have been described for this gene and its promoter region. Available sequence data analyses indicate splice variants that encode different isoforms.<ref name = "entrez"/>
| OMIM = 603101
| ECnumber =
| Homologene = 55610
| MGIid = 1891837
| GeneAtlas_image1 = PBB_GE_CPB2_206651_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004182 |text = carboxypeptidase A activity}} {{GNF_GO|id=GO:0004184 |text = lysine carboxypeptidase activity}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}  
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}  
  | Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1361
    | Hs_Ensembl = ENSG00000080618
    | Hs_RefseqProtein = NP_001863
    | Hs_RefseqmRNA = NM_001872
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 13
    | Hs_GenLoc_start = 45525323
    | Hs_GenLoc_end = 45577169
    | Hs_Uniprot = Q96IY4
    | Mm_EntrezGene = 56373
    | Mm_Ensembl = ENSMUSG00000021999
    | Mm_RefseqmRNA = NM_019775
    | Mm_RefseqProtein = NP_062749
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 73976442
    | Mm_GenLoc_end = 74017703
    | Mm_Uniprot = Q9JHH6
  }}
}}
'''Carboxypeptidase B2 (plasma)''', also known as '''CPB2''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: CPB2 carboxypeptidase B2 (plasma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1361| accessdate = }}</ref>
}}
==See also==
==See also==
*[[Carboxypeptidase B]]
*[[Carboxypeptidase B]]


==References==
==References==
{{reflist|2}}
{{Reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Bouma BN, Mosnier LO |title=Thrombin activatable fibrinolysis inhibitor (TAFI) at the interface between coagulation and fibrinolysis. |journal=Pathophysiol. Haemost. Thromb. |volume=33 |issue= 5-6 |pages= 375-81 |year= 2005 |pmid= 15692247 |doi= 10.1159/000083832 }}
*{{cite journal  |vauthors=Bouma BN, Mosnier LO |title=Thrombin activatable fibrinolysis inhibitor (TAFI) at the interface between coagulation and fibrinolysis. |journal=Pathophysiol. Haemost. Thromb. |volume=33 |issue= 5–6 |pages= 375–81 |year= 2005 |pmid= 15692247 |doi= 10.1159/000083832 }}
*{{cite journal  | author=Marinkovic DV, Marinkovic JN, Erdös EG, Robinson CJ |title=Purification of carboxypeptidase B from human pancreas. |journal=Biochem. J. |volume=163 |issue= 2 |pages= 253-60 |year= 1977 |pmid= 17398 |doi= }}
*{{cite journal  |vauthors=Marinkovic DV, Marinkovic JN, Erdös EG, Robinson CJ |title=Purification of carboxypeptidase B from human pancreas |journal=Biochem. J. |volume=163 |issue= 2 |pages= 253–60 |year= 1977 |pmid= 17398 |doi=  | pmc=1164691 }}
*{{cite journal | author=Tsai SP, Drayna D |title=The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome 13. |journal=Genomics |volume=14 |issue= 2 |pages= 549-50 |year= 1992 |pmid= 1427879 |doi=  }}
*{{cite journal  |vauthors=Pascual R, Burgos FJ, Salva M |title=Purification and properties of five different forms of human procarboxypeptidases |journal=Eur. J. Biochem. |volume=179 |issue= 3 |pages= 609–16 |year= 1989 |pmid= 2920728 |doi=10.1111/j.1432-1033.1989.tb14590.x |display-authors=etal}}
*{{cite journal  | author=Eaton DL, Malloy BE, Tsai SP, ''et al.'' |title=Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. |journal=J. Biol. Chem. |volume=266 |issue= 32 |pages= 21833-8 |year= 1991 |pmid= 1939207 |doi=  }}
*{{cite journal  |vauthors=Valnickova Z, Thogersen IB, Christensen S |title=Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein |journal=J. Biol. Chem. |volume=271 |issue= 22 |pages= 12937–43 |year= 1996 |pmid= 8662763 |doi=10.1074/jbc.271.22.12937 |display-authors=etal}}
*{{cite journal  | author=Pascual R, Burgos FJ, Salva M, ''et al.'' |title=Purification and properties of five different forms of human procarboxypeptidases. |journal=Eur. J. Biochem. |volume=179 |issue= 3 |pages= 609-16 |year= 1989 |pmid= 2920728 |doi=  }}
*{{cite journal  |vauthors=Bajzar L, Morser J, Nesheim M |title=TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex |journal=J. Biol. Chem. |volume=271 |issue= 28 |pages= 16603–8 |year= 1996 |pmid= 8663147 |doi=10.1074/jbc.271.28.16603 }}
*{{cite journal  | author=Valnickova Z, Thogersen IB, Christensen S, ''et al.'' |title=Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein. |journal=J. Biol. Chem. |volume=271 |issue= 22 |pages= 12937-43 |year= 1996 |pmid= 8662763 |doi=  }}
*{{cite journal  |vauthors=Vanhoof G, Wauters J, Schatteman K |title=The gene for human carboxypeptidase U (CPU)--a proposed novel regulator of plasminogen activation--maps to 13q14.11 |journal=Genomics |volume=38 |issue= 3 |pages= 454–5 |year= 1997 |pmid= 8975730 |doi= 10.1006/geno.1996.0656 |display-authors=etal}}
*{{cite journal  | author=Bajzar L, Morser J, Nesheim M |title=TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. |journal=J. Biol. Chem. |volume=271 |issue= 28 |pages= 16603-8 |year= 1996 |pmid= 8663147 |doi=  }}
*{{cite journal  |vauthors=Matsumoto A, Itoh K, Matsumoto R |title=A novel carboxypeptidase B that processes native beta-amyloid precursor protein is present in human hippocampus |journal=Eur. J. Neurosci. |volume=12 |issue= 1 |pages= 227–38 |year= 2000 |pmid= 10651877 |doi=10.1046/j.1460-9568.2000.00908.x }}
*{{cite journal  | author=Vanhoof G, Wauters J, Schatteman K, ''et al.'' |title=The gene for human carboxypeptidase U (CPU)--a proposed novel regulator of plasminogen activation--maps to 13q14.11. |journal=Genomics |volume=38 |issue= 3 |pages= 454-5 |year= 1997 |pmid= 8975730 |doi= 10.1006/geno.1996.0656 }}
*{{cite journal  |vauthors=Marx PF, Hackeng TM, Dawson PE |title=Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage |journal=J. Biol. Chem. |volume=275 |issue= 17 |pages= 12410–5 |year= 2000 |pmid= 10777524 |doi=10.1074/jbc.275.17.12410 |display-authors=etal}}
*{{cite journal  | author=Zhao L, Morser J, Bajzar L, ''et al.'' |title=Identification and characterization of two thrombin-activatable fibrinolysis inhibitor isoforms. |journal=Thromb. Haemost. |volume=80 |issue= 6 |pages= 949-55 |year= 1999 |pmid= 9869166 |doi=  }}
*{{cite journal  |vauthors=Mosnier LO, Lisman T, van den Berg HM |title=The defective down regulation of fibrinolysis in haemophilia A can be restored by increasing the TAFI plasma concentration |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 1035–9 |year= 2002 |pmid= 11686321 |doi=  |display-authors=etal}}
*{{cite journal  | author=Boffa MB, Reid TS, Joo E, ''et al.'' |title=Characterization of the gene encoding human TAFI (thrombin-activable fibrinolysis inhibitor; plasma procarboxypeptidase B). |journal=Biochemistry |volume=38 |issue= 20 |pages= 6547-58 |year= 1999 |pmid= 10350473 |doi= 10.1021/bi990229v }}
*{{cite journal  |vauthors=Mosnier LO, Meijers JC, Bouma BN |title=The role of protein S in the activation of thrombin activatable fibrinolysis inhibitor (TAFI) and regulation of fibrinolysis |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 1040–6 |year= 2002 |pmid= 11686322 |doi=  }}
*{{cite journal  | author=Matsumoto A, Itoh K, Matsumoto R |title=A novel carboxypeptidase B that processes native beta-amyloid precursor protein is present in human hippocampus. |journal=Eur. J. Neurosci. |volume=12 |issue= 1 |pages= 227-38 |year= 2000 |pmid= 10651877 |doi=  }}
*{{cite journal  |vauthors=Mosnier LO, Elisen MG, Bouma BN, Meijers JC |title=Protein C inhibitor regulates the thrombin-thrombomodulin complex in the up- and down regulation of TAFI activation |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 1057–64 |year= 2002 |pmid= 11686324 |doi=  }}
*{{cite journal  | author=Marx PF, Hackeng TM, Dawson PE, ''et al.'' |title=Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage. |journal=J. Biol. Chem. |volume=275 |issue= 17 |pages= 12410-5 |year= 2000 |pmid= 10777524 |doi=  }}
*{{cite journal  |vauthors=Morange PE, Aillaud MF, Nicaud V |title=Ala147Thr and C+1542G polymorphisms in the TAFI gene are not associated with a higher risk of venous thrombosis in FV Leiden carriers |journal=Thromb. Haemost. |volume=86 |issue= 6 |pages= 1583–4 |year= 2002 |pmid= 11776333 |doi=  |display-authors=etal}}
*{{cite journal  | author=Mosnier LO, Lisman T, van den Berg HM, ''et al.'' |title=The defective down regulation of fibrinolysis in haemophilia A can be restored by increasing the TAFI plasma concentration. |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 1035-9 |year= 2002 |pmid= 11686321 |doi=  }}
*{{cite journal  |vauthors=Schneider M, Nagashima M, Knappe S |title=Amino acid residues in the P6-P'3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 9944–51 |year= 2002 |pmid= 11786552 |doi= 10.1074/jbc.M111685200 |display-authors=etal}}
*{{cite journal  | author=Mosnier LO, Meijers JC, Bouma BN |title=The role of protein S in the activation of thrombin activatable fibrinolysis inhibitor (TAFI) and regulation of fibrinolysis. |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 1040-6 |year= 2002 |pmid= 11686322 |doi=  }}
*{{cite journal  |vauthors=Koschinsky ML, Boffa MB, Nesheim ME |title=Association of a single nucleotide polymorphism in CPB2 encoding the thrombin-activable fibrinolysis inhibitor (TAF1) with blood pressure |journal=Clin. Genet. |volume=60 |issue= 5 |pages= 345–9 |year= 2002 |pmid= 11903334 |doi=10.1034/j.1399-0004.2001.600504.x |display-authors=etal}}
*{{cite journal  | author=Mosnier LO, Elisen MG, Bouma BN, Meijers JC |title=Protein C inhibitor regulates the thrombin-thrombomodulin complex in the up- and down regulation of TAFI activation. |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 1057-64 |year= 2002 |pmid= 11686324 |doi=  }}
*{{cite journal  |vauthors=Yano Y, Gabazza EC, Hori Y |title=Association between plasma thrombin-activatable fibrinolysis inhibitor levels and activated protein C in normotensive type 2 diabetic patients |journal=Diabetes Care |volume=25 |issue= 7 |pages= 1245–6 |year= 2002 |pmid= 12087030 |doi=10.2337/diacare.25.7.1245 |display-authors=etal}}
*{{cite journal  | author=Morange PE, Aillaud MF, Nicaud V, ''et al.'' |title=Ala147Thr and C+1542G polymorphisms in the TAFI gene are not asssociated with a higher risk of venous thrombosis in FV Leiden carriers. |journal=Thromb. Haemost. |volume=86 |issue= 6 |pages= 1583-4 |year= 2002 |pmid= 11776333 |doi=  }}
*{{cite journal  |vauthors=Antovic JP, Blombäck M |title=Thrombin-activatable fibrinolysis inhibitor antigen and TAFI activity in patients with APC resistance caused by factor V Leiden mutation |journal=Thromb. Res. |volume=106 |issue= 1 |pages= 59–62 |year= 2003 |pmid= 12165290 |doi=10.1016/S0049-3848(02)00072-5 }}
*{{cite journal  | author=Schneider M, Nagashima M, Knappe S, ''et al.'' |title=Amino acid residues in the P6-P'3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 9944-51 |year= 2002 |pmid= 11786552 |doi= 10.1074/jbc.M111685200 }}
*{{cite journal  | author=Koschinsky ML, Boffa MB, Nesheim ME, ''et al.'' |title=Association of a single nucleotide polymorphism in CPB2 encoding the thrombin-activable fibrinolysis inhibitor (TAF1) with blood pressure. |journal=Clin. Genet. |volume=60 |issue= 5 |pages= 345-9 |year= 2002 |pmid= 11903334 |doi=  }}
*{{cite journal  | author=Yano Y, Gabazza EC, Hori Y, ''et al.'' |title=Association between plasma thrombin-activatable fibrinolysis inhibitor levels and activated protein C in normotensive type 2 diabetic patients. |journal=Diabetes Care |volume=25 |issue= 7 |pages= 1245-6 |year= 2002 |pmid= 12087030 |doi=  }}
*{{cite journal  | author=Antovic JP, Blombäck M |title=Thrombin-activatable fibrinolysis inhibitor antigen and TAFI activity in patients with APC resistance caused by factor V Leiden mutation. |journal=Thromb. Res. |volume=106 |issue= 1 |pages= 59-62 |year= 2003 |pmid= 12165290 |doi=  }}
}}
}}
{{refend}}
{{refend}}


{{NLM content}}
{{NLM content}}
{{Hydrolase-stub}}


{{Proteases}}
{{Proteases}}
{{Coagulation}}
{{PBB_Controls
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| require_manual_inspection = no
| update_protein_box = yes
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{{DEFAULTSORT:Thrombin-Activatable Fibrinolysis Inhibitor}}
[[Category:Fibrinolytic system]]
{{Hydrolase-stub}}

Latest revision as of 20:46, 20 October 2017

"TAFI" redirects here. For other uses, see TAFI (disambiguation).
On Wikipedia, "TAFI" refers to Wikipedia:Today's articles for improvement.
VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Carboxypeptidase B2 (CPB2), also known as carboxypeptidase U (CPU), plasma carboxypeptidase B (pCPB) or thrombin-activatable fibrinolysis inhibitor (TAFI), is an enzyme that, in humans, is encoded by the gene CPB2.[1][2]

Function

CPB2 is synthesized by the liver[3] and circulates in the plasma as a plasminogen-bound zymogen. When it is activated by proteolysis at residue Arg92 by the thrombin/thrombomodulin complex, CPB2 exhibits carboxypeptidase activity. Activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen.[4][5]

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 thrombin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis.[6]

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

Isozymes

Polymorphisms have been described for this gene and its promoter region. Available sequence data analyses indicate splice variants that encode different isoforms.[6]

See also

References

  1. ↑ Eaton DL, Malloy BE, Tsai SP, Henzel W, Drayna D (Dec 1991). "Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma". J Biol Chem. 266 (32): 21833–8. PMID 1939207.
  2. ↑ Tsai SP, Drayna D (Dec 1992). "The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome 13". Genomics. 14 (2): 549–50. doi:10.1016/S0888-7543(05)80268-X. PMID 1427879.
  3. ↑ Kaushansky K, Lichtman M, Beutler E, Kipps T, Prchal J, Seligsohn U. (2010; edition 8: pages 1833-1834 and 2040-2041) Williams Hematology. McGraw-Hill. ISBN 978-0071621519
  4. ↑ Zhao L, Morser J, Bajzar L, Nesheim M, Nagashima M (December 1998). "Identification and characterization of two thrombin-activatable fibrinolysis inhibitor isoforms". Thromb. Haemost. 80 (6): 949–55. PMID 9869166.
  5. ↑ Boffa MB, Reid TS, Joo E, Nesheim ME, Koschinsky ML (May 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.
  6. ↑ 6.0 6.1 "Entrez Gene: CPB2 carboxypeptidase B2 (plasma)".

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. PMC 1164691. PMID 17398.
  • 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. doi:10.1111/j.1432-1033.1989.tb14590.x. 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. doi:10.1074/jbc.271.22.12937. 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. doi:10.1074/jbc.271.28.16603. 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.
  • 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. doi:10.1046/j.1460-9568.2000.00908.x. 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. doi:10.1074/jbc.275.17.12410. 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. doi:10.1034/j.1399-0004.2001.600504.x. PMID 11903334.
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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