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Volume 271, Number 25, Issue of June 21, 1996 pp. 14897-14902
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Characterization of the Binding of Serum Amyloid P to Type IV Collagen

(Received for publication, August 14, 1995, and in revised form, March 18, 1996)

From the Division of Nephrology, Children's Hospital Research Foundation and Department of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, Ohio 45229-3039

Serum amyloid P (SAP), a member of the evolutionarily conserved pentraxin family, is a normal component of a number of basement membranes, including glomerular and alveolar. In vitro SAP binds to a variety of proteins including fibronectin, proteoglycans, and the collagen-like region of the complement component C1q. In these studies, binding of SAP to type IV collagen, a major component of basement membrane, was examined. Purified SAP binds to human and mouse type IV collagen but not type I, II, or III collagens. Binding of SAP to type IV collagen is dependent on the presence of Ca²⁺. This binding is saturable with a K_d  1.2 × 10⁷ M based on solid phase binding and 4 × 10⁸ M based on the IC₅₀ value from fluid phase binding data. Binding of SAP to type IV collagen was inhibited by both SAP and C-reactive protein (CRP). However, a 5-fold molar excess of CRP as compared with SAP was required to inhibit the SAP binding by 50%. Binding of SAP to type IV collagen was inhibited by both collagen IV and C1q but not by phosphatidylethanolamine or bovine serum albumin. The inhibition data indicate that SAP may bind to the triple helical region of type IV collagen via a site distinct from its galactan binding site. The most likely site of SAP involved in its interaction with type IV collagen may be the region spanning amino acid residues 108-120, which shows a great deal of sequence homology (60% strict identity) with the CRP region implicated in its binding to the collagen-like region of the C1q molecule.

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