Factor X Shanghai and disruption of translocation to the endoplasmic reticulum

Haematologica

Volumn 90, Issue 12, 2005, Pages 1659-1664

  Wang, Wen Bin ^a   Fu, Qi Hua ^b   Yin, Jun ^c   Wu, Wen Man ^a   Ding, Qiu Lan ^a   Zhou, Rong Fu ^a   Hu, Yi Qun ^a   Wang, Xue Feng ^a   Wang, Zhen Yi ^a   Wang, Hong Li ^a  

^a SHANGHAI SECOND MEDICAL UNIVERSITY   (China)

^b BLOOD CENTER OF ZHEJIANG PROVINCE   (China)

^c SHANTOU UNIVERSITY MEDICAL COLLEGE   (China)

Author keywords

Deficiency; Factor X; Mutation; Signal peptide; Translocation

Indexed keywords

ANTIGEN; ARGININE; BLOOD CLOTTING FACTOR 10; MUTANT PROTEIN; SERINE; SIGNAL PEPTIDE;

ADULT; AMINO ACID SUBSTITUTION; ANTIGEN DETECTION; ARTICLE; BIOACCUMULATION; BLOOD CLOTTING FACTOR 10 DEFICIENCY; CASE REPORT; CELL FATE; CELL FREE SYSTEM; CELL LYSATE; CELL STRAIN HEK293; CODON; EMBRYO; ENDOPLASMIC RETICULUM; GENE CONSTRUCT; GENE DISRUPTION; GENE MUTATION; GENE SEQUENCE; GENETIC TRANSCRIPTION; GENETIC TRANSFECTION; HOMOZYGOTE; HUMAN; HUMAN CELL; HYDROPHOBICITY; IMMUNOASSAY; MALE; MICROSOME; MUTATIONAL ANALYSIS; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN TRANSPORT; RNA TRANSLATION; WILD TYPE;

AMINO ACID SUBSTITUTION; CELL-FREE SYSTEM; CELLS, CULTURED; CONSANGUINITY; ENDOPLASMIC RETICULUM; FACTOR X; FACTOR X DEFICIENCY; GASTROINTESTINAL HEMORRHAGE; HUMANS; HYDROPHOBICITY; MALE; MIDDLE AGED; MUTATION, MISSENSE; PROTEIN SORTING SIGNALS; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECOMBINANT FUSION PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFECTION;

EID: 29144510451     PISSN: 03906078     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (32)

1. Leytus SP, Foster DC, Kurachi K, et al. Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. Biochemistry 1986;25:5098-102.
2. Mann KG, Jenny RJ, Krishnaswamy S. Cofactor proteins in the assembly and expression of blood clotting enzyme complexes. Annu Rev Biochem 1988;57:915-56.
3. Tuddenham EGD, Cooper DN. The molecular genetics of hemostasis and its inherited disorders. Oxford: Oxford University Press, 1994.
4. Mannucci PM, Duga S, Peyvandi F. Recessively inherited coagulation disorders. Blood 2004;104:1243-52.
5. Uprichard J, Perry DJ. Factor X deficiency. Blood Rev 2002;16:97-110.
6. Cooper DN, Millar DS, Wacey A, Pemberton S, Tuddenham EG. Innerited factor X deficiency: molecular genetics and pathophysiology. Thromb Haemost 1997;78:161-72.
7. Peyvandi F, Mannucci PM, Lak M, Abdoullahi M, Zeinali S, Sharifian R, et al. Congenital factor X deficiency: spectrum of bleeding symptoms in 32 Iranian patients. Br J Haematol 1998;102:626-8.
8. Millar DS, Elliston L, Deex P, Krawczak M, Wacey AI, Reynaud J, et al. Molecular analysis of the genotype-phenotype relationship in factor X deficiency. Hum Genet 2000;106:249-57.
9. Peyvandi F, Menegatti M, Santagostino E, Akhavan S, Uprichard J, Perry DJ, et al. Gene mutations and three-dimensional structural analysis in 13 families with severe factor X deficiency. Br J Haematol 2002;117:685-92.
10. Wang WTB, Fu QH, Zhou RF, Wu WM, Ding QL, Hu YQ, et al. Molecular characterization of two novel mutations causing factor X deficiency in a Chinese pedigree. Haemophilia 2005;11:31-7.
11. Pinotti M, Camire RM, Baroni M, Rajab A, Marchetti G, Bernardi F. Impaired prothrombinase activity of factor X Gly381Asp results in severe familial CRM+ FX deficiency. Thromb Haemost 2003;89:243-8.
12. Pinotti M, Marchetti G, Baroni M, Cinotti F, Morfini M Bernardi F. Reduced activation of the Gla19Ala FX variant via the extrinsic coagulation pathway results in symptomatic CRMred FX deficiency. Thromb Haemost 2002;88:236-41.
13. Pinotti M, Monti M, Baroni M, Marchetti G, Bernardi F. Molecular characterization of factor X deficiency associated with borderline plasma factor X level. Haematologica 2004;89:501-2.
14. Watzke HH, Lechner K, Roberts HR, Reddy SV, Welsch DJ, Friedman P, et al. Molecular defect (Gla+14-Lys) and its functional consequences in a hereditary factor X deficiency (factor X "Vorarlberg"). J Biol Chem 1990;265:11982-9.
15. Racchi M, Watzke HH, High KA, Lively MO. Human coagulation factor X deficiency caused by a mutant signal peptide that blocks cleavage by signal peptidase but not targeting and translocation to the endoplasmic reticulum. J Biol Chem 1993;268:5735-40.
16. Kim DJ, Girolami A, James HL. Characterization of recombinant human coagulation factor XFriuli. Thromb Haemost 1996;75:313-7.
17. Rudolph AE, Mullane MP, Porche-Sorbet R, Tsuda S, Miletich JP. Factor X St. Louis II. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein. J Biol Chem 1996;271:28601-6.
18. Nobauer-Huhmann IM, Holler W, Krinninger B, Turecek PL, Richter G, Scharrer I, et al. Factor X Frankfurt I: molecular and functional characterization of a hereditary factor X deficiency (Gla+25 to Lys). Blood Coagul Fibrinolysis 1998;9:143-52.
19. Forberg E, Huhmann I, Jimenez-Boj E, Watzke HH. The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys). Thromb Haemost 2000;83:234-8.
20. Colosimo A, Xu Z, Novelli G, Dallapiccola B, Gruenert DC. Simple version of "megaprimer" PCR for site-directed mutagenesis. Biotechniques 1999;26:870-3.
21. Wang WB, Fu QH, Ding QL, Zhou RF, Wu WM, Hu YQ, et al. Characterization of molecular defect of 13387-9delG mutated antithrombin in inherited type I antithrombin deficiency. Blood Coagul Fibrinolysis 2005;16:149-55.
22. Kaufman RJ. Post-translational modifications required for coagulation factor secretion and function. Thromb Haemost 1998;79:1068-79.
23. Walter P, Johnson AE. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu Rev Cell Biol 1994;10:87-119.
24. Karaplis AC, Lim SK, Baba H, Arnold A, Kronenberg HM. Inefficient membrane targeting, translocation, and proteolytic processing by signal peptidase of a mutant preproparathyroid hormone protein. J Biol Chem 1995;270:1629-35.
25. Seppen J, Steenken E, Lindhout D, Bosma PJ, Elferink RP. A mutation which disrupts the hydrophobic core of the signal peptide of bilirubin UDP-glucuronosyltransferase, an endoplasmic reticulum membrane protein, causes Crigler-Najjar type II. FEBS Lett 1996;390:294-8.
26. Rajpar MH, Koch MJ, Davies RM, Mellody KT, Kielty CM, Dixon MJ. Mutation of the signal peptide region of the bicistronic gene DSPP affects translocation to the endoplasmic reticulum and results in defective dentine biomineralization. Hum Mol Genet 2002;11:2559-65.
27. Fitches AC, Appleby R, Lane DA, De Stefano V, Leone G, Olds RJ. Impaired cotranslational processing as a mechanism for type I antithrombin deficiency. Blood 1998;92:4671-6.
28. Watzke HH, Wallmark A, Hamaguchi N, Giardina P, Stafford DW, High KA. Factor XSanto Domingo. Evidence that the severe clinical phenotype arises from a mutation blocking secretion. J Clin Invest 1991;88:1685-9.
29. Gierasch LM. Signal sequences. Biochemistry 1989;28:923-30.
30. Cioffi JA, Allen KL, Lively MO, Kemper B. Parallel effects of signal peptide hydrophobic core modifications on cotranslational translocation and posttranslational cleavage by purified signal peptidase. J Biol Chem 1989;264:15052-8.
31. Hopp TP, Woods KR. Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 1981;78:3824-8.
32. Kurzchalia TV, Wiedmann M, Girshovich AS, Bochkareva ES, Bielka H, Rapoport TA. The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle. Nature 1986;320:634-6.