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Identification of a collagen potentiated neurite promoting factor isolated from C6 glioma cells
Author(s) -
Coyle D. E.
Publication year - 1993
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.490350406
Subject(s) - neurite , chondroitin sulfate proteoglycan , microbiology and biotechnology , cell culture , nerve growth factor , glycoprotein , chemistry , neurotrophic factors , chondroitin sulfate , neuron , proteoglycan , biochemistry , biology , neuroscience , extracellular matrix , in vitro , glycosaminoglycan , receptor , genetics
Abstract The C6 glial cell line has been used as a model cell system for the investigation of new glial produced neurotrophic and neurotropic molecules. By using the C6 cell line grown in a defined medium on collagen, this laboratory has isolated a distinct neurite promoting factor (NPF) that is potentiated by the presence of collagen (CPNPF). We have observed that C6 cells cultured in a defined medium on collagen (rat type‐I) slowed their growth rate and expressed an astrocytic‐ or oligodendrocytic‐like morphology. CPNPF, at this state of purity, appears to be a distinct NPF which induces neurite outgrowth (neurites of 1 or more somal diameters) in PC12 cells. These neurite promotion effects, however, appear to support the neuron morphology for only a short period (4 days) of time without the presence of neurotrophic factor (NTF). The neurite promoting activity is ineffective in inducing neurite outgrowth using mouse neuroblastoma cells (neuro‐2a). CPNPF appears to be a heat stable protein whose activity does not depend on the presence of intact collagen, heparin sulfate proteoglycan (HSPG), or chondroitin sulfate proteoglycan (CSPG). Exposure to dissociative conditions results in a loss of neurite promoting activity. CPNPF is not a glycoprotein that contains an accessible α‐D‐mannopyranosyl, α‐D‐glucopyranosyl, or a sterically related residue (hydroxyl groups in the C‐3,4, and 5 positions). Although these residues are not present on all glycoproteins, it does indicate that CPNPF is most likely not a glycoprotein. CPNPF activity is not blocked by neutralizing antibodies directed toward NGF, β‐FGF, IL‐1β, IL‐6, TGF‐β2, TGF‐β1.2, TGF‐β3, TGF‐β5, or EGF. CPNPF appears to either be oligomeric protein or a complex of proteins. On the basis of indirect evidence, it does not appear to be glial derived protease nexin‐I. The alteration in morphology of the C6 glial cell line by serum‐free conditions in the presence of collagen may have induced the production of a potentially new NPF not seen by previous investigators. © 1993 Wiley‐Liss, Inc.