메뉴 건너뛰기




Volumn 89, Issue 8, 1997, Pages 2807-2816

Naturally occurring Arg-1 to His mutation in human protein C leads to aberrant propeptide processing and secretion of dysfunctional protein C

Author keywords

[No Author keywords available]

Indexed keywords

ANTITHROMBIN; ARGININE; BLOOD CLOTTING FACTOR 5; DNA; FIBRINOGEN; HISTIDINE; PLASMINOGEN; PLASMINOGEN ACTIVATOR INHIBITOR 1; PROTEIN C; PROTEIN S;

EID: 0030894792     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v89.8.2807     Document Type: Article
Times cited : (16)

References (49)
  • 1
    • 0026591793 scopus 로고
    • The protein C anticoagulant pathway
    • Esmon CT: The protein C anticoagulant pathway. Arterioscler Thromb 12:135, 1992
    • (1992) Arterioscler Thromb , vol.12 , pp. 135
    • Esmon, C.T.1
  • 2
    • 0028832910 scopus 로고
    • The protein C anticoagulant system: Inherited defects as basis for venous thrombosis
    • Dahlbäck B: The protein C anticoagulant system: inherited defects as basis for venous thrombosis. Thromb Res 77:1, 1995
    • (1995) Thromb Res , vol.77 , pp. 1
    • Dahlbäck, B.1
  • 5
    • 0027123107 scopus 로고
    • Molecular and cellular biology of blood coagulation
    • Furie B, Furie BC: Molecular and cellular biology of blood coagulation. N Engl J Med 326:800, 1992
    • (1992) N Engl J Med , vol.326 , pp. 800
    • Furie, B.1    Furie, B.C.2
  • 6
    • 0010548624 scopus 로고
    • Introduction to hemostasis and the vitamin K-dependent coagulation factors
    • Scriver CR, Beaudet AL, Sly WS, Valle D (eds). New York, McGraw-Hill
    • Reiner AP, Davie EW: Introduction to hemostasis and the vitamin K-dependent coagulation factors, in Scriver CR, Beaudet AL, Sly WS, Valle D (eds): The Metabolic and Molecular Bases of Inherited Disease. New York, McGraw-Hill, 1995, p 3181
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 3181
    • Reiner, A.P.1    Davie, E.W.2
  • 7
    • 0027499804 scopus 로고
    • Synthesis of vitamin K-dependent proteins
    • Suttie JW: Synthesis of vitamin K-dependent proteins. FASEB J 7:445, 1993
    • (1993) FASEB J , vol.7 , pp. 445
    • Suttie, J.W.1
  • 8
    • 0025272678 scopus 로고
    • Molecular basis of vitamin K-dependent γ-carboxylation
    • Furie B, Furie BC: Molecular basis of vitamin K-dependent γ-carboxylation. Blood 75:1753, 1990
    • (1990) Blood , vol.75 , pp. 1753
    • Furie, B.1    Furie, B.C.2
  • 10
    • 0023733887 scopus 로고
    • Amino-terminal alanine functions in a calcium-specific process essential for membrane binding by prothrombin fragment 1
    • Welsch DJ, Nelsestuen GL: Amino-terminal alanine functions in a calcium-specific process essential for membrane binding by prothrombin fragment 1. Biochemistry 27:4939, 1988
    • (1988) Biochemistry , vol.27 , pp. 4939
    • Welsch, D.J.1    Nelsestuen, G.L.2
  • 11
    • 0026610682 scopus 로고
    • The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1
    • Soriana-Garcia M, Padmanabhan K, De Vos AM, Tulinsky A: The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1. Biochemistry 31:2554, 1992
    • (1992) Biochemistry , vol.31 , pp. 2554
    • Soriana-Garcia, M.1    Padmanabhan, K.2    De Vos, A.M.3    Tulinsky, A.4
  • 12
    • 0028986860 scopus 로고
    • Structure of the metal-free γ-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy
    • Freedman SJ, Furie BC, Furie B, Baleja JD: Structure of the metal-free γ-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy. J Biol Chem 270:7980, 1995
    • (1995) J Biol Chem , vol.270 , pp. 7980
    • Freedman, S.J.1    Furie, B.C.2    Furie, B.3    Baleja, J.D.4
  • 13
    • 0029148317 scopus 로고
    • Hydrophobic amino acid residues of human anticoagulation protein C that contribute to its functional binding to phospholipid vesicles
    • Christiansen WT, Jalbert LR, Robertson RM, Jhingan A, Prorok M, Castellino FJ: Hydrophobic amino acid residues of human anticoagulation protein C that contribute to its functional binding to phospholipid vesicles. Biochemistry 34:10376, 1995
    • (1995) Biochemistry , vol.34 , pp. 10376
    • Christiansen, W.T.1    Jalbert, L.R.2    Robertson, R.M.3    Jhingan, A.4    Prorok, M.5    Castellino, F.J.6
  • 14
    • 0027502870 scopus 로고
    • PACE/ furin can process the vitamin K-dependent pro-factor IX precursor within the secretory pathway
    • Wasley LC, Rehemtulla A, Bristol JA, Kaufman RJ: PACE/ furin can process the vitamin K-dependent pro-factor IX precursor within the secretory pathway. J Biol Chem 268:8458, 1993
    • (1993) J Biol Chem , vol.268 , pp. 8458
    • Wasley, L.C.1    Rehemtulla, A.2    Bristol, J.A.3    Kaufman, R.J.4
  • 15
    • 0027474512 scopus 로고
    • Propeptide processing during factor IX biosynthesis. Effect of point mutations adjacent to the propeptide cleavage site
    • Bristol JA, Furie BC, Furie B: Propeptide processing during factor IX biosynthesis. Effect of point mutations adjacent to the propeptide cleavage site. J Biol Chem 268:7577, 1993
    • (1993) J Biol Chem , vol.268 , pp. 7577
    • Bristol, J.A.1    Furie, B.C.2    Furie, B.3
  • 16
    • 0026674167 scopus 로고
    • A microsomal endopeptidase from liver with substrate specificity for processing proproteins such as the vitamin K-dependent proteins in plasma
    • Davie EW, Kawabata S: A microsomal endopeptidase from liver with substrate specificity for processing proproteins such as the vitamin K-dependent proteins in plasma. J Biol Chem 267:10331, 1992
    • (1992) J Biol Chem , vol.267 , pp. 10331
    • Davie, E.W.1    Kawabata, S.2
  • 18
    • 0028674393 scopus 로고
    • Pro-protein convertases of subtilisin/ kexin family
    • Seidah NG, Chrétien M: Pro-protein convertases of subtilisin/ kexin family. Methods Enzymol 244:175, 1994
    • (1994) Methods Enzymol , vol.244 , pp. 175
    • Seidah, N.G.1    Chrétien, M.2
  • 19
    • 0026720791 scopus 로고
    • Preferred sequence requirements for cleavage of pro-von Willebrand factor by propeptide-processing enzymes
    • Rehemtulla A, Kaufman RJ: Preferred sequence requirements for cleavage of pro-von Willebrand factor by propeptide-processing enzymes. Blood 79:2349, 1992
    • (1992) Blood , vol.79 , pp. 2349
    • Rehemtulla, A.1    Kaufman, R.J.2
  • 20
    • 0027077840 scopus 로고
    • Proteolytic cleavages of proalbumin and complement pro-C3 in vitro by a truncated soluble form of furin, a mammalian homologue of the yeast Kex2 protease
    • Oda K, Misumi Y, Ikehara Y, Brennan SO, Hatsuzawa K, Nakayama K: Proteolytic cleavages of proalbumin and complement pro-C3 in vitro by a truncated soluble form of furin, a mammalian homologue of the yeast Kex2 protease. Biochem Biophys Res Commun 189:1353, 1992
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1353
    • Oda, K.1    Misumi, Y.2    Ikehara, Y.3    Brennan, S.O.4    Hatsuzawa, K.5    Nakayama, K.6
  • 22
    • 0028851870 scopus 로고
    • Protein C Osaka 10 with aberrant propeptide processing: Loss of anticoagulant activity due to an amino acid substitution in the protein C precursor
    • Miyata T, Zheng YZ, Sakata T, Kato H: Protein C Osaka 10 with aberrant propeptide processing: loss of anticoagulant activity due to an amino acid substitution in the protein C precursor. Thromb Haemost 74:1003, 1995
    • (1995) Thromb Haemost , vol.74 , pp. 1003
    • Miyata, T.1    Zheng, Y.Z.2    Sakata, T.3    Kato, H.4
  • 23
    • 0028871033 scopus 로고
    • Identification of 15 different candidate causal point mutations and three polymorphisms in 19 patients with protein S deficiency using a scanning method for the analysis of the protein S active gene
    • Gandrille S, Borgel D, Eschwege-Gufflet V, Aillaud M, Dreyfus M, Matheron C, Gaussem P, Abgrall JF, Jude B, Sie P, Toulon P, Aiach M: Identification of 15 different candidate causal point mutations and three polymorphisms in 19 patients with protein S deficiency using a scanning method for the analysis of the protein S active gene. Blood 85:130, 1995
    • (1995) Blood , vol.85 , pp. 130
    • Gandrille, S.1    Borgel, D.2    Eschwege-Gufflet, V.3    Aillaud, M.4    Dreyfus, M.5    Matheron, C.6    Gaussem, P.7    Abgrall, J.F.8    Jude, B.9    Sie, P.10    Toulon, P.11    Aiach, M.12
  • 25
    • 0022450813 scopus 로고
    • Molecular basis of hemophilia B: A defective enzyme due to an unprocessed propeptide is caused by a point mutation in the factor IX precursor
    • Diuguid DL, Rabiet M-J, Furie BC, Liebman HA, Furie B: Molecular basis of hemophilia B: A defective enzyme due to an unprocessed propeptide is caused by a point mutation in the factor IX precursor. Proc Natl Acad Sci USA 83:5803, 1986
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 5803
    • Diuguid, D.L.1    Rabiet, M.-J.2    Furie, B.C.3    Liebman, H.A.4    Furie, B.5
  • 26
    • 0024323339 scopus 로고
    • Factor IX Kawachinagano: Impaired function of the Gladomain caused by attached propeptide region due to substitution of arginine by glutamine at position -4
    • Sugimoto M, Miyata T, Kawabata S, Yoshioka A, Fukui H, Iwanaga S: Factor IX Kawachinagano: impaired function of the Gladomain caused by attached propeptide region due to substitution of arginine by glutamine at position -4. Br J Haematol 72:216, 1989
    • (1989) Br J Haematol , vol.72 , pp. 216
    • Sugimoto, M.1    Miyata, T.2    Kawabata, S.3    Yoshioka, A.4    Fukui, H.5    Iwanaga, S.6
  • 27
    • 0022500039 scopus 로고
    • Defective propeptide processing of blood clotting factor IX caused by mutation of arginine to glutamine at position -4
    • Bentley AK, Rees DJG, Rizza C, Brownlee GG; Defective propeptide processing of blood clotting factor IX caused by mutation of arginine to glutamine at position -4. Cell 45:343, 1986
    • (1986) Cell , vol.45 , pp. 343
    • Bentley, A.K.1    Rees, D.J.G.2    Rizza, C.3    Brownlee, G.G.4
  • 28
    • 0025272062 scopus 로고
    • In vitro γ-carboxylation of a 59-residue recombinant peptide including the propeptide and the γ-carboxyglutamic acid domain of coagulation factor IX
    • Wu S-M, Soute BAM, Vermeer C, Stafford DW: In vitro γ-carboxylation of a 59-residue recombinant peptide including the propeptide and the γ-carboxyglutamic acid domain of coagulation factor IX. J Biol Chem 265:13124, 1990
    • (1990) J Biol Chem , vol.265 , pp. 13124
    • Wu, S.-M.1    Soute, B.A.M.2    Vermeer, C.3    Stafford, D.W.4
  • 29
    • 0027269964 scopus 로고
    • Five novel mutations located in exons III and IX of the protein C gene in patients presenting with defective protein C anticoagulant activity
    • Gandrille S, Alhenc-Gelas M, Gaussem P, Aillaud M-F, Dupuy E, Juhan-Vague I, Aiach M: Five novel mutations located in exons III and IX of the protein C gene in patients presenting with defective protein C anticoagulant activity. Blood 82:159, 1993
    • (1993) Blood , vol.82 , pp. 159
    • Gandrille, S.1    Alhenc-Gelas, M.2    Gaussem, P.3    Aillaud, M.-F.4    Dupuy, E.5    Juhan-Vague, I.6    Aiach, M.7
  • 32
    • 0027517303 scopus 로고
    • Splice site mutation in the human protein C gene associated with venous thrombosis: Demonstration of exon skipping by ectopic transcript analysis
    • Lind B, Van Solinge WW, Schwartz M, Thorsen S: Splice site mutation in the human protein C gene associated with venous thrombosis: Demonstration of exon skipping by ectopic transcript analysis. Blood 82:2423, 1993
    • (1993) Blood , vol.82 , pp. 2423
    • Lind, B.1    Van Solinge, W.W.2    Schwartz, M.3    Thorsen, S.4
  • 33
    • 0028861492 scopus 로고
    • Six different point mutations in seven Danish families with symptomatic protein C deficiency
    • Lind B, Schwartz M, Thorsen S: Six different point mutations in seven Danish families with symptomatic protein C deficiency. Thromb Haemost 73:186, 1995
    • (1995) Thromb Haemost , vol.73 , pp. 186
    • Lind, B.1    Schwartz, M.2    Thorsen, S.3
  • 34
    • 0029816870 scopus 로고    scopus 로고
    • Two mutations in exon XII of the protein Sα gene in four thrombophilic families resulting in premature stop codons and depressed levels of mutated mRNA
    • Andersen BD, Lind B, Philips M, Hansen AB, Ingerslev J, Thorsen S: Two mutations in exon XII of the protein Sα gene in four thrombophilic families resulting in premature stop codons and depressed levels of mutated mRNA. Thromb Haemost 76:143, 1996
    • (1996) Thromb Haemost , vol.76 , pp. 143
    • Andersen, B.D.1    Lind, B.2    Philips, M.3    Hansen, A.B.4    Ingerslev, J.5    Thorsen, S.6
  • 35
    • 0026445730 scopus 로고
    • A specific immunologic assay for functional plasminogen activator inhibitor 1 in plasma - Standardized measurements of the inhibitor and related parameters in patients with venous thromboembolic disease
    • Philips M, Juul A-G, Selmer J, Lind B, Thorsen S: A specific immunologic assay for functional plasminogen activator inhibitor 1 in plasma - standardized measurements of the inhibitor and related parameters in patients with venous thromboembolic disease. Thromb Haemost 68:486, 1992
    • (1992) Thromb Haemost , vol.68 , pp. 486
    • Philips, M.1    Juul, A.-G.2    Selmer, J.3    Lind, B.4    Thorsen, S.5
  • 36
    • 0020628416 scopus 로고
    • Inactivation of human coagulation factor V by activated protein C
    • Suzuki K, Stenflo J, Dahlbäck B, Teodorsson B: Inactivation of human coagulation factor V by activated protein C. J Biol Chem 258:1914, 1983
    • (1983) J Biol Chem , vol.258 , pp. 1914
    • Suzuki, K.1    Stenflo, J.2    Dahlbäck, B.3    Teodorsson, B.4
  • 37
    • 0021741550 scopus 로고
    • Familial protein S deficiency is associated with recurrent thrombosis
    • Comp PC, Nixon RR, Cooper MR, Esmon CT: Familial protein S deficiency is associated with recurrent thrombosis. J Clin Invest 74:2082, 1984
    • (1984) J Clin Invest , vol.74 , pp. 2082
    • Comp, P.C.1    Nixon, R.R.2    Cooper, M.R.3    Esmon, C.T.4
  • 39
    • 0026048715 scopus 로고
    • Direct identification of γ-carboxyglutamic acid in the sequencing of vitamin K-dependent proteins
    • Cairns JR, Williamson MK, Price PA: Direct identification of γ-carboxyglutamic acid in the sequencing of vitamin K-dependent proteins. Anal Biochem 199:93, 1991
    • (1991) Anal Biochem , vol.199 , pp. 93
    • Cairns, J.R.1    Williamson, M.K.2    Price, P.A.3
  • 40
    • 0000553533 scopus 로고
    • Sequence determination
    • Needleham SB (ed). New York, NY, Springer-Verlag
    • Edman P, Henschen A: Sequence determination, in Needleham SB (ed): Protein Sequence Determination. New York, NY, Springer-Verlag, 1975, p 239
    • (1975) Protein Sequence Determination , pp. 239
    • Edman, P.1    Henschen, A.2
  • 43
    • 0026063331 scopus 로고
    • Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors
    • Stenflo J: Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors. Blood 78:1637, 1991
    • (1991) Blood , vol.78 , pp. 1637
    • Stenflo, J.1
  • 44
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides
    • Geiger T, Clarke S: Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. J Biol Chem 262:785, 1987
    • (1987) J Biol Chem , vol.262 , pp. 785
    • Geiger, T.1    Clarke, S.2
  • 47
    • 0025370072 scopus 로고
    • Identification of amino acids in the γ-carboxylation recognition site on the propeptide of prothrombin
    • Huber P, Schmitz T, Griffin J, Jacobs M, Walsh C, Furie B, Furie BC: Identification of amino acids in the γ-carboxylation recognition site on the propeptide of prothrombin. J Biol Chem 265:12467, 1990
    • (1990) J Biol Chem , vol.265 , pp. 12467
    • Huber, P.1    Schmitz, T.2    Griffin, J.3    Jacobs, M.4    Walsh, C.5    Furie, B.6    Furie, B.C.7
  • 48
    • 0027942676 scopus 로고
    • Membrane binding properties of the factor IX γ-carboxyglutamic acid-rich domain prepared by chemical synthesis
    • Jacobs M, Freedman SJ, Furie BC, Furie B: Membrane binding properties of the factor IX γ-carboxyglutamic acid-rich domain prepared by chemical synthesis. J Biol Chem 269:25494, 1994
    • (1994) J Biol Chem , vol.269 , pp. 25494
    • Jacobs, M.1    Freedman, S.J.2    Furie, B.C.3    Furie, B.4
  • 49
    • 0028029621 scopus 로고
    • Profactor IX: The propeptide inhibits binding to membrane surfaces and activation by factor XIa
    • Bristol JA, Freedman SJ, Furie BC, Furie B: Profactor IX: The propeptide inhibits binding to membrane surfaces and activation by factor XIa. Biochemistry 33:14136, 1994
    • (1994) Biochemistry , vol.33 , pp. 14136
    • Bristol, J.A.1    Freedman, S.J.2    Furie, B.C.3    Furie, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.