The collagenous domain of classA scavenger receptors is involved in macrophage adhesion to collagens

Document Type

Article

Journal/Book Title/Conference

Journal of Leukocyte Biology

Volume

69

Publication Date

2001

Abstract

Class A macrophage scavenger receptors (MSRs) have a remarkably broadligand specificity and are well‐known for their roles in atherogenesisand host defense. Recently, we demonstrated that these receptors also recognize and mediate adhesion to denatured forms of type I collagen.In this study, the involvement of the collagenous domain of MSRs in binding to denatured type I collagen was investigated. Transient expression of full‐length, native type II MSR in COS‐1 cells conferred adhesion to denatured type I collagens, whereas expression of a truncated receptor lacking the distal portion of the collagenous domain did not. Further, a synthetic peptide derived from the collagenous domain was effective in abrogating Mφ adhesion to denatured forms of type I collagen. We also addressed collagen‐type specificity by examining MSR affinity for type III and type IV collagens. As with typeI collagen, Mφs adhered only to denatured forms of type III collagen.Moreover, the adhesion was mediated by MSRs. In contrast, adhesion to denatured type IV collagen was not shown to be MSR‐dependent, but adhesion to the native form was. MSR‐mediated adhesion to types III andIV collagens was also shown to be dependent on the collagenous domain.Taken together, these data strongly suggest that the collagenous domain is involved in MSR‐mediated adhesion to denatured forms of types I andIII collagens and native, but not denatured, type IV collagen.

Comments

J. Leukoc. Biol. (2001) 69, 575-82

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