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Titolo:
Molecular analysis of eight mutations in FBN1
Autore:
Halliday, D; Hutchinson, S; Kettle, S; Firth, H; Wordsworth, P; Handford, PA;
Indirizzi:
Univ Oxford, Dept Biochem, Oxford OX1 3QU, England Univ Oxford Oxford England OX1 3QU Dept Biochem, Oxford OX1 3QU, England Univ Oxford, Wellcome Trust Ctr Human Genet, Oxford OX3 7BN, England Univ Oxford Oxford England OX3 7BN Human Genet, Oxford OX3 7BN, England Univ Cambridge, Dept Med Genet, Cambridge CB2 2QQ, England Univ CambridgeCambridge England CB2 2QQ net, Cambridge CB2 2QQ, England
Titolo Testata:
HUMAN GENETICS
fascicolo: 6, volume: 105, anno: 1999,
pagine: 587 - 597
SICI:
0340-6717(199912)105:6<587:MAOEMI>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEONATAL MARFAN-SYNDROME; FACTOR-LIKE DOMAINS; EGF-LIKE DOMAIN; FIBRILLIN-1 GENE; CALCIUM-BINDING; DERMAL FIBROBLASTS; RELATIVE ABUNDANCE; VI COLLAGEN; MICROFIBRILS; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Handford, PA Univ Oxford, Dept Biochem, S Parks Rd, Oxford OX1 3QU, England Univ Oxford S Parks Rd Oxford England OX1 3QU 1 3QU, England
Citazione:
D. Halliday et al., "Molecular analysis of eight mutations in FBN1", HUM GENET, 105(6), 1999, pp. 587-597

Abstract

Mutations in the gene encoding extracellular glycoprotein fibrillin-1 (FBN1) cause Marfan syndrome (MFS) and other related connective tissue disorders. In this study, eight mutations have been detected in MFS patients by heteroduplex analysis. These comprise two mis sense mutations, C1835Y and C2258Y in calcium-binding epidermal growth factor-like domains, two nonsense mutations, R1541X and R2394X in transforming growth factor pi-binding protein-like domains, one splice site mutation, which has been detected previously, and three small insertions or deletions resulting in a frameshift. Fibroblast cells have been established from seven of the MFS patients and the biochemical effects of the mutations on fibrillin-1 synthesis and secretion assessed by pulse-chase analysis. Each cysteine mutation resulted in the delayed secretion of fibrillin-1 and both nonsense and frameshift mutations caused reduced levels of synthesis and/or deposition of fibrillin-1. Indirect immunofluorescence and rotary shadowing electron microscopy analysis of fibrillin microfibrils revealed no major differences between normal and patient samples. We discuss the relative merits of the biochemical techniques used in this study.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 11:12:16