Decorin is specifically solubilized by heparin from the extracellular matrix of rat skeletal muscles.
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.
Melo
F
F
Department of Cell and Molecular Biology, Faculty of Biologycal Sciences, Catholic University of Chile, Santiago.
Brandan
E
E
D000110:Acetylcholinesterase / Q000737:chemistry; D000818:Animals; D058575:Decorin; D005109:Extracellular Matrix / Q000737:chemistry*; D016326:Extracellular Matrix Proteins; D006493:Heparin / Q000737:chemistry*; D008297:Male; D008970:Molecular Weight; D009132:Muscles / Q000648:ultrastructure*; D011509:Proteoglycans / Q000737:chemistry*; D051381:Rats; D017207:Rats, Sprague-Dawley; D012995:Solubility
C546880:Dcn protein, rat; D058575:Decorin; D016326:Extracellular Matrix Proteins; D011509:Proteoglycans; D006493:Heparin; D000110:Acetylcholinesterase