Co-solubilization of asymmetric acetylcholinesterase and dermatan sulfate proteoglycan from the extracellular matrix of rat skeletal muscles.
We have previously communicated that heparin released asymmetric acetylcholinesterase (AChE) from cholinergic synapses. Here we report studies showing that heparin, besides releasing asymmetric AChE from the skeletal muscle extracellular matrix (ECM), specifically solubilizes a dermatan sulfate proteoglycan (DSPG) which accounts for more than 95% of the 35S-released material. The co-solubilization of AChE and the proteoglycan opens up the possibility that both macromolecules could be involved in the formation of the soluble AChE complex observed after incubation of muscle homogenate with heparin. Our results suggest a possible association between asymmetric AChE and DSPG at the muscle ECM, moreover this work is the first report of the existence of DSPG at the skeletal muscle cell surface.
D000110:Acetylcholinesterase / Q000302:isolation & purification*; D000818:Animals; D002807:Chondroitin / Q000031:analogs & derivatives*; D011508:Chondroitin Sulfate Proteoglycans / Q000302:isolation & purification*; D002852:Chromatography, Ion Exchange; D003871:Dermatan Sulfate / Q000302:isolation & purification*; D005109:Extracellular Matrix / Q000032:analysis*; D006493:Heparin; D046911:Macromolecular Substances; D008297:Male; D009132:Muscles / Q000648:ultrastructure*; D011509:Proteoglycans / Q000302:isolation & purification*; D051381:Rats; D011919:Rats, Inbred Strains; D012995:Solubility; D013431:Sulfates / Q000378:metabolism
D011508:Chondroitin Sulfate Proteoglycans; D046911:Macromolecular Substances; D011509:Proteoglycans; D013431:Sulfates; C032649:dermatan sulfate proteoglycan; D003871:Dermatan Sulfate; D006493:Heparin; D002807:Chondroitin; D000110:Acetylcholinesterase