Control of SHB gene expression by protein phosphorylation
1996 (English)In: Cellular Signalling, ISSN 0898-6568, E-ISSN 1873-3913, Vol. 8, no 1, 55-58 p.Article in journal (Refereed) Published
To increase our understanding of the role of the Src homology 2 (SH2) domain-containing protein Shb in the mitogenic signal transduction, Shb mRNA contents were determined in the fibroblast-like NIH3T3 cells and the insulin producing βTC-1 cells under various conditions. In NIH3T3 cells, the serine/ threonine phosphatase inhibitor okadaic acid and the tyrosine kinase inhibitor genistein increased Shb mRNA contents, the protein kinase C activating phorbol ester 12-O-tetradecanoyl 13-acetate (TPA) decreased the Shb mRNA content, whereas the tyrosine kinase inhibitor tyrphostin 25 and the mitogen platelet-derived growth factor (PDGF-BB) had no effect. In βTC-1 cells, okadaic acid and genistein increased the Shb mRNA content, whereas tyrphostin 25 and serum were without effect. Okadaic acid and genistein decreased the rates of βTC-1 cell DNA synthesis. It is concluded that expression of the SHB gene is under a complex mode of regulation involving at least three different protein kinases. As a consequence of this, it is likely that SHB gene expression is significantly modulated by conditions of specific activation of certain pathways, whereas its expression appears little influenced by serum and a mitogen.
Place, publisher, year, edition, pages
1996. Vol. 8, no 1, 55-58 p.
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-53021DOI: 10.1016/0898-6568(95)02019-5PubMedID: 8777141OAI: oai:DiVA.org:uu-53021DiVA: diva2:80931