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Science 17 March 1989:
Vol. 243. no. 4897, pp. 1477 - 1479
DOI: 10.1126/science.2928781
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Articles

Science, Vol 243, Issue 4897, 1477-1479
Copyright © 1989 by American Association for the Advancement of Science

articles

The EGF receptor kinase substrate p35 in the floor plate of the embryonic rat CNS

JA McKanna and S Cohen

Department of Cell Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.

P35 is a calcium- and phospholipid-binding protein that was originally isolated as a substrate for the epidermal growth factor (EGF) receptor tyrosine kinase and later was found to be related to lipocortin I. Immunohistochemistry was used to localize p35 to a raphe of primitive glial ependymal cells in the median one-third of the floor plate in the central nervous system (CNS) of rat embryos. The p35 appears by embryonic day 12 before the arrival of pioneering ventral commissural axons. The unexpected, discrete distribution of this protein during development opens the question of its role in neural morphogenesis.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Origins of Growth Factors: NGF and EGF.
S. Cohen (2008)
J. Biol. Chem. 283, 33793-33797
   Full Text »    PDF »
Immunohistochemical Localization of Lipocortin 1 in Rat Brain Is Sensitive to pH, Freezing, and Dehydration.
J. A. McKanna and M.-Z. Zhang (1997)
J. Histochem. Cytochem. 45, 527-538
   Abstract »    Full Text »    PDF »
Expression of a lacZ transgene reveals floor plate cell morphology and macromolecular transfer to commissural axons.
R. M. Campbell and A. C. Peterson (1993)
Development 119, 1217-1228
   Abstract »    PDF »


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