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Decorin is a member of the small leucine-rich proteoglycan family and it is a component of the extracellular matrix. Decorin was previously shown to bind different molecules, including myostatin, in a zinc-dependent manner. Here, we investigated in detail the anti-myostatin activity of decorin and fragments thereof. We show that this protein displays in vitro anti-myostatin activities with an IC(50) of 2.3 × 10(-8)M. After intramuscular injection of decorin in dystrophic mdx and γ-sarcoglycan(-/-) mice, we observed a significant increase of the muscle mass and this effect was maximal 18 days after administration. Further, we show that the myostatin-binding site is located in the N-terminal domain of decorin. In fact, a peptide encompassing the 31-71 sequence retains full myostatin binding capacity and intramuscular injection of the peptide induces muscle hypertrophy. The evaluation of three additional peptides suggests a crucial role of the four cysteines within the conserved CX3CXCX6C motif of class I of the small leucine-rich proteoglycans. Altogether, our results show that the N-terminal domain of decorin is sufficient for the binding to myostatin and they underscore the crucial role for this interaction of zinc and the cysteine cluster.

Original publication




Journal article


Neuromuscul Disord

Publication Date





1057 - 1068


Animals, Decorin, Extracellular Matrix Proteins, Mice, Mice, Inbred mdx, Mice, Knockout, Muscle, Skeletal, Muscular Diseases, Myostatin, Peptides, Protein Binding, Proteoglycans, Zinc