Decorin is a Zn2+ metalloprotein

Vivian W C Yang, Steven R. LaBrenz, Lawrence C. Rosenberg, David McQuillan, Magnus Höök

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)

Abstract

Decorin is ubiquitously distributed in the extracellular matrix of mammals and a member of the proteoglycan family characterized by a core protein dominated by leucine-rich repeat motifs. We show here that decorin extracted from bovine tissues under denaturing conditions or produced in recombinant 'native' form by cultured mammalian cells has a high affinity for Zn2+ as demonstrated by equilibrium dialyses. The Zn2+-binding sites are localized to the N-terminal domain of the core protein that contains 4 Cys residues in a spacing reminiscent of a zinc finger. A recombinant 41-amino acid long peptide representing the N-terminal domain of decorin has full Zn2+ binding activity and binds two Zn2+ ions with an average K(D) of 3 x 10-7 M. Binding of Zn2+ to this peptide results in a change in secondary structure as shown by circular dichroism spectroscopy. Biglycan, a proteoglycan that is structurally closely related to decorin contains a similar high affinity Zn2+-binding segment, whereas the structurally more distantly related proteoglycans, epiphycan and osteoglycin, do not bind Zn2+ with high affinity.

Original languageEnglish
Pages (from-to)12454-12460
Number of pages7
JournalJournal of Biological Chemistry
Volume274
Issue number18
DOIs
Publication statusPublished - Apr 30 1999
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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