Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
EPIDERMOLYSIS-BULLOSA SIMPLEX - A KERATIN-5 MUTATION IS A FULLY DOMINANT ALLELE IN EPIDERMAL CYTOSKELETON FUNCTION
Autore:
STEPHENS K; ZLOTOGORSKI A; SMITH L; EHRLICH P; WIJSMAN E; LIVINGSTON RJ; SYBERT VP;
Indirizzi:
UNIV WASHINGTON,DEPT MED,DIV MED GENET,RG-25,1959 NE PACIFIC ST SEATTLE WA 98195 UNIV WASHINGTON,DEPT MED,DIV DERMATOL SEATTLE WA 98195 UNIV WASHINGTON,DEPT BIOL STRUCT SEATTLE WA 98195 UNIV WASHINGTON,DEPT BIOSTAT SEATTLE WA 98195 UNIV WASHINGTON,DEPT PEDIAT SEATTLE WA 98195 CHILDRENS HOSP & MED CTR SEATTLE WA 98105 HADASSAH UNIV HOSP,DEPT DERMATOL IL-91120 JERUSALEM ISRAEL
Titolo Testata:
American journal of human genetics
fascicolo: 3, volume: 56, anno: 1995,
pagine: 577 - 585
SICI:
0002-9297(1995)56:3<577:ES-AKM>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMPERFECTA TYPE-I; OSTEOGENESIS IMPERFECTA; COLLAGEN GENE; INTERMEDIATE FILAMENTS; FRAMESHIFT MUTATION; POINT MUTATIONS; DISEASE; ABNORMALITIES; EXPRESSION; DIAGNOSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
K. Stephens et al., "EPIDERMOLYSIS-BULLOSA SIMPLEX - A KERATIN-5 MUTATION IS A FULLY DOMINANT ALLELE IN EPIDERMAL CYTOSKELETON FUNCTION", American journal of human genetics, 56(3), 1995, pp. 577-585

Abstract

To explore the relationship between abnormal keratin molecules, 10-nmintermediate filament (IF) organization, and epidermal fragility and blistering, we sought to determine the functional consequences of homozygosity for a dominant keratin defect. We describe a family with an autosomal dominant skin-blistering disorder, epidermolysis bullosa simplex, Koebner subtype (EBS-K), that has a novel point mutation, occurring in the keratin 5 gene (KRT5), that predicts the substitution of an evolutionarily conserved lysine by an asparagine residue (K173N). Unlike previous heterozygous mutations located within the initial segment of domain 1A of keratin molecules, K173N heterozygosity did not resultin severe disease or clumping of keratin filaments. One family memberwas found to be homozygous for the K173N allele, having inherited it hem each of her affected first-cousin parents. Despite a lack of normal keratin 5 molecules, and an effective doubling of abnormal molecules, available for heterodimerization with keratin 14 during IF formation, there were no significant differences in the clinical severity or the ultrastructural organization of the keratin IF cytoskeleton of the homozygous individual. These data demonstrate that the K173N mutation behaves as a fully dominant allele and indicate that a limited number of abnormal keratin molecules are sufficient to impair cytoskeletal function and elicit epidermal fragility and blistering.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 05:35:47