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(Received for publication, May 9, 1996, and in revised form, September 4, 1996)
From the Institute of Physiological Chemistry and
Pathobiochemistry, University of Münster, Waldeyerstrasse 15, D-48149 Münster, Federal Republic of Germany
Decorin, a member of a family of proteins with
leucine-rich repeat motifs, is a widely distributed extracellular
matrix proteoglycan that is thought to be responsible for the
structure, tissue organization, and surface properties of fibrils. In
mammals, decorin carries one chondroitin/dermatan sulfate chain as a
distinction from its homologue, biglycan, which contains two
glycosaminoglycan chains. With the aim to study decorin-collagen
interactions in chicken, where the fibrillar organization of cartilage
collagens is best understood, we have isolated decorin-related
proteoglycans from sternal cartilage of 40-day-old broiler chickens.
Small chondroitin/dermatan sulfate proteoglycans were resolved by
hydrophobic interaction chromatography into two fractions, DCN I and
DCN II. Both forms contained dermatan sulfate and, in addition, keratan
sulfate chains. Tryptic fingerprinting revealed that the core proteins
of DCN I and DCN II were identical. The protein was identified as
decorin by amino-terminal sequencing. DCN II was found to contain two dermatan sulfate chains, whereas DCN I had a single dermatan sulfate chain. The dermatan sulfate attachment sites are located near the
NH2 terminus of the core protein, i.e. at Ser-4
and Ser-16 in DCN II and at Ser-4 in DCN I. The keratan sulfate
attachment sites are located in the central portion of the core
protein, at Asn-179 and Asn-230.
The presence of two dermatan sulfate chains renders the chicken
proteoglycan DCN II structurally similar to mammalian biglycan. Interestingly, biglycan has not been detected in chicken. Therefore, in
birds, DCN II may function as a biglycan substitute.
Volume 271, Number 48,
Issue of November 29, 1996
pp. 30347-30353
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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