Decorin binds myostatin and modulates its activity to muscle cells

Journal Article · Fri Feb 10 04:00:00 EST 2006 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2005.12.060· OSTI ID:20798799

Miura, Takayuki ^[1]; Kishioka, Yasuhiro ^[1]; Wakamatsu, Jun-ichi ^[1]; Hattori, Akihito ^[1]; Hennebry, Alex ^[2]; Berry, Carole J ^[2]; Sharma, Mridula ^[2]; Kambadur, Ravi ^[2]; Nishimura, Takanori ^[1]

---

1. Meat Science Laboratory, Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589 (Japan)
2. Animal Genomics, AgResearch, Hamilton 2015 (New Zealand)

Myostatin, a member of TGF-{beta} superfamily of growth factors, acts as a negative regulator of skeletal muscle mass. The mechanism whereby myostatin controls the proliferation and differentiation of myogenic cells is mostly clarified. However, the regulation of myostatin activity to myogenic cells after its secretion in the extracellular matrix (ECM) is still unknown. Decorin, a small leucine-rich proteoglycan, binds TGF-{beta} and regulates its activity in the ECM. Thus, we hypothesized that decorin could also bind to myostatin and participate in modulation of its activity to myogenic cells. In order to test the hypothesis, we investigated the interaction between myostatin and decorin by surface plasmon assay. Decorin interacted with mature myostatin in the presence of concentrations of Zn{sup 2+} greater than 10 {mu}M, but not in the absence of Zn{sup 2+}. Kinetic analysis with a 1:1 binding model resulted in dissociation constants (K {sub D}) of 2.02 x 10{sup -8} M and 9.36 x 10{sup -9} M for decorin and the core protein of decorin, respectively. Removal of the glycosaminoglycan chain by chondroitinase ABC digestion did not affect binding, suggesting that decorin could bind to myostatin with its core protein. Furthermore, we demonstrated that immobilized decorin could rescue the inhibitory effect of myostatin on myoblast proliferation in vitro. These results suggest that decorin could trap myostatin and modulate its activity to myogenic cells in the ECM.

• OSTI ID: 20798799
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 340; ISSN 0006-291X; ISSN BBRCA9
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
CELL PROLIFERATION
DIGESTION
GROWTH FACTORS
HYPOTHESIS
IN VITRO
LEUCINE
MODULATION
MUSCLES
SECRETION
ZINC IONS