Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Selective adhesion of macrophages to denatured forms of type I collagen ismediated by scavenger receptors
Autore:
Gowen, BB; Borg, TK; Ghaffar, A; Mayer, EP;
Indirizzi:
Univ S Carolina, Sch Med, Dept Microbiol & Immunol, Columbia, SC 29208 USAUniv S Carolina Columbia SC USA 29208 l & Immunol, Columbia, SC 29208 USA Univ S Carolina, Sch Med, Dept Dev Biol & Anat, Columbia, SC 29208 USA Univ S Carolina Columbia SC USA 29208 Biol & Anat, Columbia, SC 29208 USA
Titolo Testata:
MATRIX BIOLOGY
fascicolo: 1, volume: 19, anno: 2000,
pagine: 61 - 71
SICI:
0945-053X(200002)19:1<61:SAOMTD>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN ATHEROSCLEROTIC LESIONS; ARG-GLY-ASP; EXTRACELLULAR-MATRIX; CELL-ADHESION; APOPTOTIC THYMOCYTES; ALZHEIMERS-DISEASE; BETA-2 INTEGRINS; GENE-EXPRESSION; END-PRODUCTS; BINDING;
Keywords:
cell adhesion; collagen; macrophage scavenger receptor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Gowen, BB Univ S Carolina, Sch Med, Dept Microbiol & Immunol, Columbia, SC29208 USA Univ S Carolina Columbia SC USA 29208 l, Columbia, SC 29208 USA
Citazione:
B.B. Gowen et al., "Selective adhesion of macrophages to denatured forms of type I collagen ismediated by scavenger receptors", MATRIX BIOL, 19(1), 2000, pp. 61-71

Abstract

Macrophages (M phi s) are multifunctional immune cells which are involved in the regulation of immune and inflammatory responses, as well as in tissue repair and remodeling. In tissues, M phi s reside in areas which are richin extracellular matrix (ECM), the structural component which also plays an essential role in regulating a variety of cellular functions. A major ECMprotein encountered by M phi s is type I collagen, the most abundant of the fibril-forming collagens. In this study, the adhesion of RAW 264.7 murineM phi s to native fibrillar, monomeric, and denatured type I collagen was investigated. Using atomic force microscopy, structural differences betweenfibrillar and monomeric type I collagen were clearly resolved. When cultured on fibrillar type I collagen, M phi s adhered poorly. In contrast, they adhered significantly to monomeric, heat-denatured, or collagenase-modifiedtype I collagen. Studies utilizing anti-beta 1 and -beta 2 integrin adhesion-blocking antibodies, RGD-containing peptides, or divalent cation-free conditions did not inhibit M phi adhesion to monomeric or denatured type I collagen. However, macrophage scavenger receptor (MSR) ligands and anti-MSR antibodies significantly blocked M phi adhesion to denatured and monomeric type I collagen strongly suggesting the involvement of the MSR as an adhesion molecule for denatured type I collagen. Further analysis by Western blot identified the MSR as the primary receptor for denatured type I collagen among M phi proteins purified from a heat-denatured type I collagen affinity column. These findings indicate that M phi s adhere selectively to denatured forms of type I collagen, but not the native fibrillar conformation, via their scavenger receptors. (C) 2000 Elsevier Science B.V./International Society of Matrix Biology. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/06/20 alle ore 11:19:20