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Differentiation of immature oligodendrocytes is regulated by phosphorylation of cyclic AMP‐response element binding protein by a protein kinase C signaling cascade
Author(s) -
Shiga Hatsuki,
Yamane Yukako,
Kubo Minoru,
Sakurai Yoko,
Asou Hiroaki,
Ito Etsuro
Publication year - 2005
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.20513
Subject(s) - creb , phosphorylation , protein kinase a , microbiology and biotechnology , oligodendrocyte , protein kinase c , cyclic amp response element binding protein , biology , protein phosphorylation , kinase , transcription factor , signal transduction , chemistry , biochemistry , endocrinology , myelin , central nervous system , gene
Previous experiments showed that the expression and phosphorylation levels of cyclic AMP‐response element binding protein (CREB) are important factors that regulate oligodendrocyte differentiation. The present study was designed to determine whether CREB phosphorylation advances oligodendrocyte differentiation or vice versa and to identify the protein kinase that primarily regulates CREB phosphorylation. We examined the expression and phosphorylation levels of CREB in developing oligodendrocytes at a specific differentiation stage by double‐immunocytochemical staining with specific differentiation markers and antibody for phosphorylated CREB. We found that the CREB expression level increased along oligodendrocyte differentiation, and that its phosphorylated level was highest in immature oligodendrocytes. We also showed that CREB phosphorylation was regulated principally by protein kinase C (PKC) activity in immature oligodendrocytes. Our findings suggest that CREB phosphorylation is dependent on a PKC signaling cascade, and this phosphorylation activates CREB‐mediated transcription and advances the differentiation of immature to mature oligodendrocytes. © 2005 Wiley‐Liss, Inc.