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Titolo:
A 'hot-spot' mutation alters the mechanical properties of keratin filamentnetworks
Autore:
Ma, LL; Yamada, S; Wirtz, D; Coulombe, PA;
Indirizzi:
Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA JohnsHopkins Univ Baltimore MD USA 21205 l Chem, Baltimore, MD 21205 USA Johns Hopkins Univ, Sch Med, Dept Dermatol, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 rmatol, Baltimore, MD 21205 USA Johns Hopkins Univ, Dept Chem Engn, Baltimore, MD 21218 USA Johns Hopkins Univ Baltimore MD USA 21218 m Engn, Baltimore, MD 21218 USA
Titolo Testata:
NATURE CELL BIOLOGY
fascicolo: 5, volume: 3, anno: 2001,
pagine: 503 - 506
SICI:
1465-7392(200105)3:5<503:A'MATM>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPIDERMOLYSIS-BULLOSA SIMPLEX; DYNAMIC CROSS-LINKING; MUSCULAR-DYSTROPHY; ASSEMBLY INVITRO; POINT MUTATIONS; ALPHA-ACTININ; DISEASE; ORGANIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Ma, LL Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 Baltimore, MD 21205 USA
Citazione:
L.L. Ma et al., "A 'hot-spot' mutation alters the mechanical properties of keratin filamentnetworks", NAT CELL BI, 3(5), 2001, pp. 503-506

Abstract

Keratins 5 and 14 polymerize to form the intermediate filament network in the progenitor basal cells of many stratified epithelia including epidermis, where it provides crucial mechanical support. Inherited mutations in K5 or K14 result in epidermolysis bullosa simplex (EBS), a skin-fragility disorder(1). The impact that such mutations exert on the intrinsic mechanical properties of K5/K14 filaments is unknown. Here we show, by using differential interference contrast microscopy, that a 'hot-spot' mutation in K14 greatly reduces the ability of reconstituted mutant filaments to bundle under crosslinking conditions. Rheological assays measure similar small-deformationmechanical responses for crosslinked solutions of wild-type and mutant keratins. The mutation, however, markedly reduces the resilience of crosslinked networks against large deformations. Single-particle tracking, which probes the local organization of filament networks, shows that the mutant polymer exhibits highly heterogeneous structures compared to those of wild-type filaments. Our results indicate that the fragility of epithelial cells expressing mutant keratin may result from an impaired ability of keratin polymers to be crosslinked into a functional network.

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Documento generato il 18/01/20 alle ore 07:24:49