ABCC8 p.Gly561Ser
| Predicted by SNAP2: | A: N (87%), C: N (72%), D: N (78%), E: N (87%), F: N (78%), H: N (66%), I: N (78%), K: N (66%), L: N (82%), M: N (66%), N: N (87%), P: N (61%), Q: N (72%), R: N (61%), S: N (93%), T: N (93%), V: N (82%), W: D (53%), Y: N (82%), |
| Predicted by PROVEAN: | A: N, C: N, D: N, E: N, F: N, H: N, I: N, K: N, L: N, M: N, N: N, P: N, Q: N, R: N, S: N, T: N, V: N, W: N, Y: N, |
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[hide] Identification of two mutations (Arg611Cys and Arg... Blood. 1995 Aug 1;86(3):1010-8. Hilbert L, Gaucher C, Mazurier C
Identification of two mutations (Arg611Cys and Arg611His) in the A1 loop of von Willebrand factor (vWF) responsible for type 2 von Willebrand disease with decreased platelet-dependent function of vWF.
Blood. 1995 Aug 1;86(3):1010-8., [PMID:7620154]
Abstract [show]
We report the identification of von Willebrand factor (vWF) gene mutations within exon 28 occurring in three unrelated families with an infrequent form of type 2 von Willebrand disease (vWD). A C-->T transition and a G-->A transition, both at the codon for arginine 611 of the mature vWF subunit, were found. They result in either a cysteine or an histidine substitution, respectively. Patients were found to be heterozygous for these substitutions and the vWD was transmitted dominantly. These substitutions have been reproduced by in vitro mutagenesis of full-length cDNA of vWF and transiently expressed in Cos-7 cells. The corresponding recombinant vWFs (rvWF) exhibited decreased expression and a significant decrease in the high molecular weight multimeric forms. In addition, ristocetin- and botrocetin-induced binding of mutated rvWFs to platelets were markedly decreased as compared with that for the wild-type rvWFs. Thus, the structural and functional characterization of both mutated rvWFs confirmed that the two nucleotide substitutions identified at position 611 of the mature subunit of vWF are real mutations. Although they are located in the A1 loop containing most of the type 2B mutations inducing increased affinity of vWF for platelet glycoprotein Ib, they are responsible for abnormal vWF with decreased platelet-dependent function.
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208 Furthermore, a point mutation affecting aa 561 (Gly561Ser)has been identifiedin a patient with type ATPOSITION 611 B vWD, now classified in type 2M,I7 characterized by no ristocetin-induced but normal botrocetin-induced binding to GP%. The corresponding Ser561rvWF showed the same platelet-dependent functions.40Lastly, another patient, reported to have a variant form of type 1 vWD and also displaying decreased ristocetin cofactor activity, was found to have the Phe6061le mutation very close to the mutations characterizedhere:' However, in this case, no studyof corresponding rvWF has yet been reported to confirm that this aa change is the mutation causing the loss of function.
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ABCC8 p.Gly561Ser 7620154:208:48
status: NEW