| First Author | Carballo E | Year | 1996 |
| Journal | J Immunol | Volume | 156 |
| Issue | 5 | Pages | 1709-13 |
| PubMed ID | 8596017 | Mgi Jnum | J:31455 |
| Mgi Id | MGI:78963 | Doi | 10.4049/jimmunol.156.5.1709 |
| Citation | Carballo E, et al. (1996) Characterization and purification of a protein kinase C substrate in human B cells. Identification as lymphocyte-specific protein 1 (LSP1). J Immunol 156(5):1709-13 |
| abstractText | 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. |
