Regulation of factor V and factor V-short by TFPIα: Relationship between B-domain proteolysis and binding.
coagulation factor
factor V
factor Va
hemostasis
protein complex
prothrombin
prothrombinase
thrombin
tissue factor pathway inhibitor
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
Historique:
received:
08
10
2020
revised:
17
12
2020
accepted:
29
12
2020
pubmed:
31
12
2020
medline:
25
8
2021
entrez:
30
12
2020
Statut:
ppublish
Résumé
Coagulation factor V (FV) plays an anticoagulant role but serves as a procoagulant cofactor in the prothrombinase complex once activated to FVa. At the heart of these opposing effects is the proteolytic removal of its central B-domain, including conserved functional landmarks (basic region, BR; 963-1008 and acidic region 2, AR2; 1493-1537) that enforce the inactive FV procofactor state. Tissue factor pathway inhibitor α (TFPIα) has been associated with FV as well as FV-short, a physiologically relevant isoform with a shortened B-domain missing the BR. However, it is unclear which forms of FV are physiologic ligands for TFPIα. Here, we characterize the binding and regulation of FV and FV-short by TFPIα via its positively charged C-terminus (TFPIα-BR) and examine how bond cleavage in the B-domain influences these interactions. We show that FV-short is constitutively active and functions in prothrombinase like FVa. Unlike FVa, FV-short binds with high affinity (K
Identifiants
pubmed: 33376137
pii: S0021-9258(20)00349-X
doi: 10.1074/jbc.RA120.016341
pmc: PMC7948760
pii:
doi:
Substances chimiques
Ligands
0
Lipoproteins
0
lipoprotein-associated coagulation inhibitor
0
prothrombinase complex
0
Factor Va
65522-14-7
Factor V
9001-24-5
Thromboplastin
9035-58-9
Thrombin
EC 3.4.21.5
Factor Xa
EC 3.4.21.6
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
100234Subventions
Organisme : NHLBI NIH HHS
ID : P01 HL139420
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL131833
Pays : United States
Organisme : NHLBI NIH HHS
ID : T32 HL007971
Pays : United States
Informations de copyright
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest R Camire is a consultant for and receives research support from Pfizer and Bayer.
Références
J Biol Chem. 2007 May 18;282(20):15033-9
pubmed: 17387173
Biochim Biophys Acta. 1983 Feb 15;742(3):558-64
pubmed: 6838889
J Thromb Haemost. 2017 Jan;15(1):140-149
pubmed: 27801970
Thromb Haemost. 2016 Mar;115(3):580-90
pubmed: 26607136
Blood. 2011 Jan 6;117(1):290-8
pubmed: 20864578
Biochemistry. 1990 Jul 24;29(29):6762-8
pubmed: 2397212
J Biol Chem. 1998 Apr 24;273(17):10709-18
pubmed: 9553135
Blood. 1982 Jul;60(1):59-63
pubmed: 7082847
Blood. 2008 Nov 1;112(9):3615-23
pubmed: 18695002
Biochemistry. 1997 Oct 7;36(40):12080-6
pubmed: 9315846
Blood. 2001 Mar 15;97(6):1549-54
pubmed: 11238089
Thromb Res. 2012 May;129 Suppl 2:S21-2
pubmed: 22425319
J Biol Chem. 2017 Jun 2;292(22):9335-9344
pubmed: 28420729
Blood. 2014 May 8;123(19):2934-43
pubmed: 24620349
J Thromb Haemost. 2015 Jun;13 Suppl 1:S200-7
pubmed: 26149025
J Biol Chem. 1983 May 25;258(10):6503-8
pubmed: 6406482
Blood. 1996 Mar 1;87(5):1845-50
pubmed: 8634431
Int J Hematol. 2020 Jan;111(1):42-50
pubmed: 30302740
Proc Natl Acad Sci U S A. 1981 Jan;78(1):162-6
pubmed: 6941242
J Thromb Haemost. 2009 Dec;7(12):1951-61
pubmed: 19765210
Biochemistry. 1998 Aug 25;37(34):11896-906
pubmed: 9718313
J Biol Chem. 2004 May 14;279(20):21643-50
pubmed: 15004010
J Clin Invest. 2013 Sep;123(9):3777-87
pubmed: 23979162
J Biol Chem. 1996 Jul 5;271(27):16126-34
pubmed: 8663201
Eur J Biochem. 1997 Jul 1;247(1):12-20
pubmed: 9249003
Front Biosci (Landmark Ed). 2012 Jan 01;17:262-80
pubmed: 22201743
Curr Opin Hematol. 2011 Sep;18(5):338-42
pubmed: 21730834
Pathophysiol Haemost Thromb. 2003;33(1):4-15
pubmed: 12853707
J Biol Chem. 2010 Feb 19;285(8):5212-23
pubmed: 20022942
Biochemistry. 1995 Mar 28;34(12):4118-24
pubmed: 7696276
J Thromb Haemost. 2017 Jul;15(7):1241-1250
pubmed: 28671348
Res Pract Thromb Haemost. 2017 Dec 20;2(1):114-124
pubmed: 30046712
J Biol Chem. 2013 Oct 18;288(42):30151-30160
pubmed: 24014022
J Biol Chem. 1993 Feb 25;268(6):3993-4000
pubmed: 8440691
Blood. 2003 Jan 1;101(1):20-30
pubmed: 12393635
Proc Natl Acad Sci U S A. 1987 Jul;84(14):4846-50
pubmed: 3110773
J Biol Chem. 2019 Feb 15;294(7):2422-2435
pubmed: 30578302
J Vis Exp. 2014 Nov 20;(93):e52099
pubmed: 25490604
Annu Rev Biochem. 1988;57:915-56
pubmed: 3052293
J Biol Chem. 1979 Feb 10;254(3):964-73
pubmed: 762106
J Biol Chem. 1984 Mar 10;259(5):3187-96
pubmed: 6421819
Methods Enzymol. 1993;222:224-36
pubmed: 8412796
Haemophilia. 2016 Jul;22 Suppl 5:3-8
pubmed: 27405668
J Biol Chem. 2012 Jul 27;287(31):26342-51
pubmed: 22707727
J Biol Chem. 2002 Jul 19;277(29):26689-98
pubmed: 12011050
Int J Lab Hematol. 2016 May;38 Suppl 1:4-11
pubmed: 27161771
Blood. 1990 Jul 1;76(1):1-16
pubmed: 2194585
Methods Enzymol. 1976;45:156-76
pubmed: 1011989
J Thromb Haemost. 2012 Sep;10(9):1944-6
pubmed: 22738072
J Biol Chem. 2013 Sep 27;288(39):27789-800
pubmed: 23940050
Blood. 2015 Mar 12;125(11):1822-5
pubmed: 25634741
J Biol Chem. 1993 Dec 25;268(36):26950-5
pubmed: 8262929
Blood. 1988 Dec;72(6):2020-5
pubmed: 3143429
J Biol Chem. 1990 Mar 5;265(7):3708-18
pubmed: 2303476
Biophys J. 2006 Nov 1;91(9):3170-81
pubmed: 16891373
J Biol Chem. 1979 Feb 25;254(4):1326-34
pubmed: 762131
Proc Natl Acad Sci U S A. 2013 Oct 29;110(44):17838-43
pubmed: 24127605
J Thromb Haemost. 2019 Apr;17(4):585-595
pubmed: 30740865
Semin Thromb Hemost. 2013 Sep;39(6):607-12
pubmed: 23893775
Front Biosci (Schol Ed). 2011 Jun 01;3:1457-62
pubmed: 21622281
J Biol Chem. 1990 Oct 5;265(28):17132-40
pubmed: 2211616
Blood Adv. 2017 Dec 26;1(27):2692-2702
pubmed: 29291252
J Biol Chem. 1982 Jun 10;257(11):6556-64
pubmed: 7076681
J Biol Chem. 2002 Oct 4;277(40):37863-70
pubmed: 12149252