Abstract

We have previously communicated that heparin co-solubilizes the asymmetric form of acetylcholinesterase (AChE) and a dermatan sulfate proteoglycan from the extracellular matrix (ECM) of rat skeletal muscles. In this report we unequivocally demonstrate by biochemical and immunological analyses that the proteoglycan that is solubilized by heparin from rat skeletal muscle ECM corresponds to decorin. These results support the concept for the role of decorin in the ECM organization.