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J. Biol. Chem., Vol. 275, Issue 29, 21801-21804, July 21, 2000

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ACCELERATED PUBLICATION
Decorin Binds Near the C Terminus of Type I Collagen^*

Douglas R. Keene, James D. San Antonio^§, Richard Mayne^¶, David J. McQuillan, George Sarris^**, Samuel A. Santoro^**, and Renato V. Iozzo^§§

From the  Shriners Hospital Research Facilities, Portland, Oregon 97201, the ^§ Department of Medicine and the Cardeza Foundation, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, the ^¶ Department of Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294, the  LifeCell Corporation, Branchburg, New Jersey 08876, the ^** Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110, and the  Department of Pathology, Anatomy and Cell Biology, and the Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107

Decorin belongs to a family of small leucine-rich proteoglycans that are directly involved in the control of matrix organization and cell growth. Genetic evidence indicates that decorin is required for the proper assembly of collagenous matrices. Here, we sought to establish the precise binding site of decorin on type I collagen. Using rotary shadowing electron microscopy and photoaffinity labeling, we mapped the binding site of decorin protein core to a narrow region near the C terminus of type I collagen. This region is located within the cyanogen bromide peptide fragment 1(I) CB6 and is ~25 nm from the C terminus, in a zone that coincides with the c₁ band of the collagen fibril D-period. This location is very close to one of the major intermolecular cross-linking sites of collagen heterotrimers. Thus, decorin protein core possesses a unique binding specificity that could potentially regulate collagen fibril stability.

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