The EGF Receptor Kinase Substrate p35 in the Floor Plate of the Embryonic Rat CNS
- 17 March 1989
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 243 (4897), 1477-1479
- https://doi.org/10.1126/science.2928781
Abstract
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.Keywords
This publication has 17 references indexed in Scilit:
- Diversity in the lipocortin/calpactin familyCell, 1988
- Calcium-dependent phospholipid- (and membrane-) binding proteinsBiochemistry, 1988
- Spatial regulation of axonal glycoprotein expression on subsets of embryonic spinal neuronsNeuron, 1988
- A thousand and one protein kinasesCell, 1987
- Annexins—New family of Ca2+-regulated-phospholipid binding proteinBioscience Reports, 1987
- Calpactins: two distinct Ca++-regulated phospholipid- and actin-binding proteins isolated from lung and placenta.The Journal of cell biology, 1987
- The
p 35p 36Cell, 1986 - Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinaseCell, 1986
- Somatostatinlike immunoreactive neurons in the hedgehog (Erinaceus europaeus) and the sheep (Ovis aries) central nervous systemJournal of Comparative Neurology, 1986
- Isolation of a calcium-dependent 35-kilodalton substrate for the epidermal growth factor receptor/kinase from A-431 cells.Journal of Biological Chemistry, 1984