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Regulation of pp60 c‐ src synthesis in rat hippocampal slices by in vitro ischemia and glucocorticoid administration
Author(s) -
Barr Christina S.,
Dokas Linda A.
Publication year - 2001
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.1159
Subject(s) - glucocorticoid , hippocampal formation , medicine , glucocorticoid receptor , endocrinology , proto oncogene tyrosine protein kinase src , immunoprecipitation , corticosterone , protein biosynthesis , in vivo , biology , microbiology and biotechnology , chemistry , receptor , biochemistry , gene , hormone
Corticosteroids, released from the adrenal gland in response to stress, bind to receptors that act as transcription factors to alter gene expression and, subsequently, protein synthesis. Using [ 35 S]‐methionine‐cysteine incorporation to measure protein synthesis in hippocampal slices incubated under ischemic conditions, synthesis of 60 kDa and 78 kDa proteins decreases 4 hr after in vivo administration of corticosterone to rats. The former protein has been identified by immunoblotting and immunoprecipitation to be the proto‐oncogene, pp60 c‐ src . In the absence of prior glucocorticoid administration, ischemic conditions increase the amount of immunoreactive pp60 c‐ src in membranes of hippocampal slices. Chronic exposure to elevated titers of glucocorticoids has been demonstrated to result in cell loss as well as in reduced neuronal plasticity and regeneration. Given the involvement of pp60 c‐ src in synaptic plasticity and cell growth, glucocorticoid‐mediated reduction in its synthesis is a potential molecular marker for stress‐induced alterations in brain function. J. Neurosci. Res. 65:340–345, 2001. © 2001 Wiley‐Liss, Inc.