A Retinal Ganglion Cell Neurotrophic Factor Purified from the Superior Colliculus

A Retinal Ganglion Cell Neurotrophic Factor Purified from the Superior Colliculus Abstract: Dissociated neonatal rat retinal ganglion cells can be maintained by the addition of an extract from the neonatal superior colliculus. This extract can support 95% of ganglion cells over 24 h in culture; in addition it promotes the expression of neurites from these cells. This report describes the purification of a neurotrophic factor from the superior colliculus which supports the survival of 80% of retinal ganglion cells over 24 h in vitro. The purification procedure involves a combination of dye‐ligand, anion‐exchange, and molecular sieve chromatography. The purified neurotrophic factor has a Stokes radius of approximately 200 Å using molecular sieve chromatography in the presence of a chaotropic agent. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis of the purified factor indicates that it is a glycoprotein that migrates with a molecular mass >400 kDa. Further characterization of this high‐molecular‐mass glycoprotein by enzymatic digestion demonstrated that it is a chondroitin sulfate pro‐teoglycan. This factor is clearly distinguishable from other neurotrophic factors that have an effect on retinal ganglion cells such as brain‐derived neurotrophic factor and fibroblast growth factor. The chondroitin sulfate proteoglycan from the neonatal superior colliculus is the first proteoglycan to be identified as a neurotrophic factor. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Neurochemistry Wiley

A Retinal Ganglion Cell Neurotrophic Factor Purified from the Superior Colliculus

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Publisher
Wiley
Copyright
Copyright © 1990 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-3042
eISSN
1471-4159
D.O.I.
10.1111/j.1471-4159.1990.tb04567.x
Publisher site
See Article on Publisher Site

Abstract

Abstract: Dissociated neonatal rat retinal ganglion cells can be maintained by the addition of an extract from the neonatal superior colliculus. This extract can support 95% of ganglion cells over 24 h in culture; in addition it promotes the expression of neurites from these cells. This report describes the purification of a neurotrophic factor from the superior colliculus which supports the survival of 80% of retinal ganglion cells over 24 h in vitro. The purification procedure involves a combination of dye‐ligand, anion‐exchange, and molecular sieve chromatography. The purified neurotrophic factor has a Stokes radius of approximately 200 Å using molecular sieve chromatography in the presence of a chaotropic agent. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis of the purified factor indicates that it is a glycoprotein that migrates with a molecular mass >400 kDa. Further characterization of this high‐molecular‐mass glycoprotein by enzymatic digestion demonstrated that it is a chondroitin sulfate pro‐teoglycan. This factor is clearly distinguishable from other neurotrophic factors that have an effect on retinal ganglion cells such as brain‐derived neurotrophic factor and fibroblast growth factor. The chondroitin sulfate proteoglycan from the neonatal superior colliculus is the first proteoglycan to be identified as a neurotrophic factor.

Journal

Journal of NeurochemistryWiley

Published: Sep 1, 1990

References

  • Immunocytochemical localization of a chondroitin sulfate proteoglycan in nervous tissue II. Studies in developing brain
    Aquino, Aquino; Margolis, Margolis; Margolis, Margolis
  • The survival of neonatal rat retinal ganglion cells is enhanced in the presence of appropriate parts of the brain
    McCaffery, McCaffery; Bennett, Bennett; Dreher, Dreher
  • Isolation of an adhesion‐mediating protein from chick neural retina adherons
    Schubert, Schubert; LaCorbiere, LaCorbiere

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