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Decorin is a Zn2+ metalloprotein
V W Yang1, S R LaBrenz, L C Rosenberg
1Graduate School of Biomedical Sciences, University of Texas, Houston Health Science Center, Houston, Texas 77030, USA.
The Journal of Biological Chemistry
|April 23, 1999
Summary
Decorin, a proteoglycan found in mammalian extracellular matrix, binds tightly to zinc ions (Zn2+). This zinc binding influences decorin's structure and is mediated by its N-terminal domain.
Area of Science:
- Biochemistry
- Proteoglycan research
- Extracellular matrix biology
Background:
- Decorin is a ubiquitously distributed mammalian proteoglycan.
- Its core protein features leucine-rich repeat motifs.
Purpose of the Study:
- To investigate the potential for decorin to bind zinc ions (Zn2+).
- To localize the Zn2+-binding sites within the decorin protein structure.
Main Methods:
- Equilibrium dialysis was used to assess Zn2+ binding affinity.
- Recombinant decorin N-terminal peptides were synthesized.
- Circular dichroism spectroscopy analyzed structural changes upon Zn2+ binding.
Main Results:
- Decorin exhibits high affinity for Zn2+.
- Zn2+-binding sites are located in the N-terminal domain, containing cysteine residues.
- A 41-amino acid peptide demonstrated full Zn2+ binding activity (KD of 3 x 10(-7) M).
- Zn2+ binding induced secondary structure alterations in the peptide.
Conclusions:
- Decorin's N-terminal domain possesses high-affinity Zn2+-binding capabilities.
- Structurally related proteoglycans like biglycan may also bind Zn2+, unlike epiphycan and osteoglycin.