Abstract
Protein phosphorylation is the most common form of post-translational modification used to regulate cellular functions (Edelman et al., 1987). CD5 provides accessory signals in T lymphocyte activation and proliferation (Weiss and Imboden, 1987). CD5 has been shown to undergo hyperphosphorylation after treatment with phorbol esters (Chatila and Geha, 1988) which are tumor promoter agents (TPA) capable to translocate and activate the serine/threonine protein kinase C (PKC) (Nishizuka, 1984). Here we show the rapid and PKC- dependent induction of a hyperphosphorylated and more slowly migrating subset of CD5 molecules after stimulation with TPA on normal and lymphoblastoid T and B cells.
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© 1991 Springer-Verlag Berlin Heidelberg
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Alberola-Ila, J., Places, L., Vives, J., Lozano, F. (1991). Changes on the Electrophoretic Mobility of CD5 Molecules Induced by PKC-Mediated Phosphorylation. In: Heilmeyer, L.M.G. (eds) Cellular Regulation by Protein Phosphorylation. NATO ASI Series, vol 56. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75142-4_24
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DOI: https://doi.org/10.1007/978-3-642-75142-4_24
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