Departments of
* Microbiology and Immunology, and
Developmental Biology and Anatomy, University of South Carolina, School of Medicine, Columbia, South Carolina
Correspondence: Eugene P. Mayer, Department of Microbiology and Immunology, University of South Carolina, School of Medicine, Columbia, SC 29208. E-mail: mayer{at}med.sc.edu
Class A macrophage scavenger receptors (MSRs) have a remarkably broad
ligand specificity and are well-known for their roles in atherogenesis
and 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 M
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 type
I collagen, Ms 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 and
IV 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 and
III collagens and native, but not denatured, type IV collagen.
Key Words: artherogenesis • extracellular matrix • nonfibrillar • monoclonal antibodies
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