The Journal of Immunology, Vol 156, Issue 5 1709-1713, Copyright © 1996 by American Association of Immunologists

ARTICLES

Characterization and purification of a protein kinase C substrate in human B cells. Identification as lymphocyte-specific protein 1 (LSP1)

E Carballo, D Colomer, JL Vives-Corrons, PJ Blackshear and J Gil
Biological Hematology Service, University of Barcelona, Spain.

Incubation of B-chronic lymphocytic leukemia (B-CLL) cells with phorbol esters resulted in the phosphorylation of two major PKC substrates, MARCKS (myristoylated, alanine-rich C kinase substrate) and MRP (MARCKS- related protein), and of a third protein, with an apparent m.w. of 60,000 that was the most prominent protein kinase C substrate in these cells. p60 phosphorylation was time and PMA dose dependent, and was induced by cell-permeable diacylglycerol, but not by inactive phorbol esters. Two-dimensional electrophoretic analysis of the protein phosphorylation pattern from the B cell line CESS demonstrated the identity between the p60 protein expressed in this cell line and that expressed in B-CLL cells. p60 was purified from CESS cells and peptide microsequencing of this protein revealed that it was lymphocyte- specific protein 1 (LSP1), that is here characterized as the most prominent protein kinase C substrate in B cells.

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