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Titolo:
6 DIFFERENT POINT MUTATIONS IN 7 DANISH FAMILIES WITH SYMPTOMATIC PROTEIN-C DEFICIENCY
Autore:
LIND B; SCHWARTZ M; THORSEN S;
Indirizzi:
RIGSHOSP,DEPT CLIN BIOCHEM KB 3011,HEMOSTASIS & THROMBOSIS SECT,BLEGDAMSVEJ 9 DK-2100 COPENHAGEN DENMARK RIGSHOSP,DEPT PEDIAT,CLIN GENET SECT DK-2100 COPENHAGEN DENMARK
Titolo Testata:
Thrombosis and haemostasis
fascicolo: 2, volume: 73, anno: 1995,
pagine: 186 - 193
SICI:
0340-6245(1995)73:2<186:6DPMI7>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARBOXYGLUTAMIC ACID RESIDUES; BLOOD-COAGULATION FACTOR; RNA SPLICE JUNCTIONS; NUCLEOTIDE-SEQUENCE; MESSENGER-RNA; FACTOR-IX; VENOUS THROMBOSIS; FACTOR-X; GENE; ORGANIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
B. Lind et al., "6 DIFFERENT POINT MUTATIONS IN 7 DANISH FAMILIES WITH SYMPTOMATIC PROTEIN-C DEFICIENCY", Thrombosis and haemostasis, 73(2), 1995, pp. 186-193

Abstract

Six different point mutations of the protein C gene are described in seven Danish families with protein C deficiency associated with an increased risk of venous thromboembolism. All affected family members areheterozygotes for the mutated protein C genotype. One mutation is a G(2992)-->A transition at position +5 in the 5' splice site of intron D. The other five mutations affect the protein coding region. One is a C-1432-->T transition in exon III converting the highly conserved Arg(15) to Trp in the Gla-domain. Another mutation is a G(3157)--> transversion in exon V converting the non-conserved Gly(72) to Arg in the epidermal growth factor domain. The remaining three mutations are locatedin non-conserved amino acid positions in exon IX and affect the serine proteinase domain. The first is a G(8559)-->C transversion converting Gly(282) to Arg. The second is a C-8571-->T transition (present in two families) converting Arg(286) to CYs. The third is a C-8695-->T transition converting pro(327) to Leu. In each family the protein C deficiency cosegregates or probably cosegregates (one family, G(8559)-->C) With the mutation. All affected family members exhibit a reduction of both the antigen and the functional plasma concentration of protein C to approximately 50% of normal indicating that the mutated protein C is not present (type 1 deficiency) or only present in low amounts in plasma. Agarose gel electrophoresis followed by Western blotting shows that the Arg(15)-->Trp substitution is associated with a normal as wellas an abnormal migrating plasma protein C band. This provides positive evidence for that both the normal and mutated alleles are expressed (type 2 deficiency): The five other mutations an associated with only one band with the mobility of normal protein C. In one family a novel G(1390)-->A transition converting the normal Ala(1) to Thr was demonstrated. This mutation is not linked to the patient specific G(8559)-->Ctransversion. In conclusion one splice site mutation and five different missense mutations of the protein C gene are described.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 15:32:46