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Titolo:
Type V collagen: heterotypic type I/V collagen interactions in the regulation of fibril assembly
Autore:
Birk, DE;
Indirizzi:
Thomas Jefferson Univ, Dept Pathol Anat & Cell Biol, Philadelphia, PA 19107 USA Thomas Jefferson Univ Philadelphia PA USA 19107 hiladelphia, PA 19107 USA
Titolo Testata:
MICRON
fascicolo: 3, volume: 32, anno: 2001,
pagine: 223 - 237
SICI:
0968-4328(200104)32:3<223:TVCHTI>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
EHLERS-DANLOS-SYNDROME; FIBRILLOGENESIS IN-SITU; III COLLAGEN; DIFFERENTIAL EXPRESSION; TYROSINE SULFATION; SKIN FRAGILITY; HUMAN-PLACENTA; MESSENGER-RNA; XI COLLAGEN; TENDON;
Keywords:
type V collagen; collagen fibril; regulation of fibril assembly; cornea; development; fibril formation; matrix assembly;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Birk, DE Thomas Jefferson Univ, Dept Pathol Anat & Cell Biol, 1020 Locust St,JAH 543, Philadelphia, PA 19107 USA Thomas Jefferson Univ 1020 Locust St,JAH 543 Philadelphia PA USA 19107
Citazione:
D.E. Birk, "Type V collagen: heterotypic type I/V collagen interactions in the regulation of fibril assembly", MICRON, 32(3), 2001, pp. 223-237

Abstract

Type V collagen is a quantitatively minor fibrillar collagen with a broad tissue distribution. The most common type V collagen isoform is alpha1(V)(2)alpha2(V) found in cornea. However, other isoforms exist, including an for[alpha1(V)alpha2(V)alpha3(V)] form, an alpha1(V)(3) homotrimer and hybrid type V/XI forms. The functional role and fibrillar organization of these isoforms is not understood. In the cornea, type V collagen has a key role in the regulation of initial fibril assembly. Type I and type V collagen co-assemble into heterotypic fibrils, The entire triple-helical domain of the type V collagen molecules is buried within the fibril and type I collagen molecules are present along the fibril surface. The retained NH2-terminal domains of the type V collagen are exposed at the surface, extending outward through the gap zones. The molecular model of the NH2-terminal domain indicates that the short or helical region is a flexible hinge-like region allowing the peptide to project away from the major axis of the molecule; the short triple-helical regions serve as an extension through the hole zone, placing the tyrosine-rich domain at the surface. The assembly of early, immaturefibril intermediates (segments) is regulated by the NH2-terminal domain oftype V collagen. These NH2-terminal domains alter accretion of collagen molecules onto fibrils and therefore lateral growth. A critical density wouldfavor the initiation of new fibrils rather than the continued growth of existing fibrils, Other type V collagen isoforms are likely to have an important role in non-cornea tissues. This role may be mediated by supramolecularaggregates different from those in the corneal stroma or by an alteration of the interactions mediated by tissue-specific type V collagen domains generated by different isoforms or aggregate structures. Presumably, the aggregate structure or specific domains are involved in the regionalization of fibril-associated macromolecules necessary for the tissue-specific regulation of later fibril growth and matrix assembly stages, (C) 2000 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 09:53:37