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J. Biol. Chem., Vol. 278, Issue 34, 32047-32057, August 22, 2003

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Type XIX Collagen Purified from Human Umbilical Cord Is Characterized by Multiple Sharp Kinks Delineating Collagenous Subdomains and by Intermolecular Aggregates via Globular, Disulfide-linked, and Heparin-binding Amino Termini^*

Jeanne C. Myers  , Deqin Li , Peter S. Amenta ¶, Charles C. Clark  ||, Chandrasekaran Nagaswami ** and John W. Weisel **

From the Departments of Biochemistry and Biophysics, ^||Orthopaedic Surgery, and ^**Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104 and the ^¶Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, New Brunswick, New Jersey 08903

Type XIX collagen was discovered from the sequence of rhabdomyosarcoma cDNA clones. The chain is composed of a 268-residue amino terminus, an 832-residue discontinuous collagenous region, and a 19-residue carboxyl peptide. Light microscopy immunohistochemistry of adult human tissues demonstrated that type XIX is localized in vascular, neuronal, mesenchymal, and some epithelial basement membrane zones. It also appears to be involved in events linked to skeletal myogenesis. In this report, we have presented the first direct evidence for the molecular structure of type XIX collagen. Using human umbilical cord, native type XIX was purified by neutral salt extraction and by ion exchange and antibody affinity chromatography. Type XIX was found to represent only 10^–6% of the dry weight of tissue, making it by far the least abundant collagen ever isolated. Transmission electron microscopy after rotary shadowing revealed the appearance of rodlike structures with multiple sharp bends, a small nodule at one end of the molecule, and a total length of 240 nm. Domain-specific antibodies were used to identify the nodule as the noncollagenous amino terminus, whereas the location of most kinks corresponds to major interruptions separating the five collagenous subdomains. More than half of the type XIX molecules observed were present in oligomers of different size and complexity, resulting from association of the amino-terminal domains. Biochemical analysis demonstrated that these supramolecular aggregates are dependent upon and/or stabilized by intermolecular disulfide cross-links and that the globular amino terminus contains a high affinity, heparin-binding site. The polymorphic conformational states of this rare collagen, and its ability to self-assemble into a higher order structure provide focal points for future determination of biologically significant functions in cell-cell and/or cell-matrix interactions.

Received for publication, May 2, 2003 , and in revised form, May 29, 2003.

^* These studies were supported by National Institutes of Health Grants GM64777, AR20553, and HL30954. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: University of Pennsylvania School of Medicine, Dept. of Biochemistry and Biophysics, 909 Stellar Chance, 422 Curie Blvd., Philadelphia, PA 19104-6059. Tel.: 215-898-0712; Fax: 215-573-2085; E-mail: myers{at}mail.med.upenn.edu.

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