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Evidence that the axolemmal mitogen for cultured schwann cells is a positively charged, heparan sulfate proteoglycan‐bound, heparin‐displaceable molecule
Author(s) -
Decoster M. A.,
Devries G. H.
Publication year - 1989
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490220308
Subject(s) - axolemma , proteoglycan , heparin , mitogen activated protein kinase , sulfation , heparan sulfate , chemistry , microbiology and biotechnology , schwann cell , biochemistry , perlecan , biophysics , biology , signal transduction , endocrinology , myelin , extracellular matrix , central nervous system
Treatment of axolemma with pH 9 buffer results in a pellet enriched two‐fold in the mitogen for cultured Schwann cells. Heparitinase treatment releases 8% of the mitogen into solution, while heparin selectively solubilizes the mitogen, resulting in an extract which has a specific mitogenic activity approximately 2.5 times greater than the mitogenicity of the starting axolemma membrane. These data support a model in which the axolemmal mitogen is a positively charged molecule associated with negatively charged sulfated proteoglycans.
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