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Altered Glycosaminoglycan Chain Structure in a Variant of the C2 Mouse Muscle Cell Line
Author(s) -
Bowen David C.,
Gordon Herman,
Hall Zach W.
Publication year - 1996
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1996.66062580.x
Subject(s) - proteoglycan , biochemistry , perlecan , dermatan sulfate , glycosaminoglycan , myogenesis , chemistry , microbiology and biotechnology , chondroitin sulfate , chondroitin sulfate proteoglycan , heparan sulfate , biology , extracellular matrix , in vitro
Abstract: Experiments on the S27 cell line, a variant of the C2 mouse muscle cell line that shows reduced incorporation of 35 SO 4 into proteoglycans, suggest that proteoglycans play a role in the clustering of acetylcholine receptors, an early step in synaptogenesis. Thus, unlike the C2 line, S27 myotubes do not form acetylcholine receptor clusters on their surface in aneural cultures and form few clusters in response to agrin. We have examined the proteoglycans synthesized by S27 myotubes to define further the biochemical defect in these cells. Gel filtration analysis of radiolabeled proteoglycans synthesized by C2 and S27 myotubes shows that both cell types express a similarly polydisperse complement of proteoglycans. Both radiolabeled heparan sulfate proteoglycans and chondroitin/dermatan sulfate proteoglycans are reduced in S27 myotubes, with the chondroitin/dermatan sulfate proteoglycans showing a distinct reduction in size. The core protein of perlecan, a major proteoglycan species in muscle, was present in S27 cells and unaltered in electrophoretic mobility. Thus a principal deficiency in S27 cells appears to be a defect in glycosaminoglycan chain elongation.