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Titolo:
Identification of four novel PMM2 mutations in congenital disorders of glycosylation (CDG) Ia French patients
Autore:
Vuillaumier-Barrot, S; Hetet, G; Barnier, A; Dupre, T; Cuer, M; de Lonlay, P; Cormier-Daire, V; Durand, G; Grandchamp, B; Seta, N;
Indirizzi:
Hop Bichat Claude Bernard, F-75877 Paris 18, France Hop Bichat Claude Bernard Paris France 18 nard, F-75877 Paris 18, France Fac Med Xavier Bichat, INSERM, U409, F-75870 Paris, France Fac Med Xavier Bichat Paris France F-75870 , U409, F-75870 Paris, France Hop Necker Enfants Malad, F-75743 Paris 15, France Hop Necker Enfants Malad Paris France 15 Malad, F-75743 Paris 15, France Fac Pharm, Lab Sante Publ, F-75270 Paris, France Fac Pharm Paris France F-75270 rm, Lab Sante Publ, F-75270 Paris, France
Titolo Testata:
JOURNAL OF MEDICAL GENETICS
fascicolo: 8, volume: 37, anno: 2000,
pagine: 579 - 580
SICI:
0022-2593(200008)37:8<579:IOFNPM>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLYCOPROTEIN SYNDROME TYPE-1; PHOSPHOMANNOMUTASE-2; GENE;
Keywords:
CDG; phosphomannomutase; PMM2 mutations;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
8
Recensione:
Indirizzi per estratti:
Indirizzo: Seta, N Hop Bichat Claude Bernard, 46 Rue henri Huchard, F-75877 Paris 18,France Hop Bichat Claude Bernard 46 Rue henri Huchard Paris France 18 ce
Citazione:
S. Vuillaumier-Barrot et al., "Identification of four novel PMM2 mutations in congenital disorders of glycosylation (CDG) Ia French patients", J MED GENET, 37(8), 2000, pp. 579-580

Abstract

We screened 11 unrelated French patients with congenital disorders of glycosylation (CDG) Ia for PMM2 mutations. Twenty one missense mutations on the22 chromosomes (95%) including four novel mutations were identified: C9Y (G26A) in exon 1, L32R (TA95GC) in exon 2, and T226S (C677G) and C241S (G722C) in exon 8. We studied the PMM activity of these four novel mutant proteins and of the R141H mutant protein in an E coli expression system. The T226S, C9Y, L32R, and C241S mutant proteins have decreased specific activity (23 to 41% of normal), are all more or less thermolabile, and R141H has no detectable activity. Our results indicate that the new mutations identified here are less severe than the inactive R141H mutant protein, conferring residual PMM activity compatible with life.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 03:28:20