DIFFERENTIAL BASAL PROTEIN-TYROSINE PHOSPHORYLATION IN NATURAL-KILLER(NK) AND T-CELLS - A BIOCHEMICAL CORRELATE OF LYMPHOID FUNCTIONAL-ACTIVITY

Citation
Dw. Mcvicar et al., DIFFERENTIAL BASAL PROTEIN-TYROSINE PHOSPHORYLATION IN NATURAL-KILLER(NK) AND T-CELLS - A BIOCHEMICAL CORRELATE OF LYMPHOID FUNCTIONAL-ACTIVITY, Cellular immunology, 169(2), 1996, pp. 302-308
Citations number
40
Categorie Soggetti
Cell Biology",Immunology
Journal title
ISSN journal
00088749
Volume
169
Issue
2
Year of publication
1996
Pages
302 - 308
Database
ISI
SICI code
0008-8749(1996)169:2<302:DBPPIN>2.0.ZU;2-J
Abstract
Despite the similarities between natural killer (NK) and T cells, thes e lymphocytes have dramatically different functional phenotypes. To id entify potential biochemical parameters that correlate with the ''prim ed'' NK phenotype, we have investigated protein tyrosine phosphorylati on in NK and T cells. Examination of tyrosyl phosphorylation in NK cel ls showed that they have higher levels of phosphorylation than resting T cells. Consistent with this, the concentrations of the tyrosine kin ase inhibitor, herbimycin A, required to inhibit FcR-mediated Ca2+ flu x in NK cells were much higher than those required for inhibition of T cell receptor-mediated Ca2+ mobilization. Differences in phosphorylat ion were not due to purification artifact or explained by differential expression of the prominent lymphocyte src-family kinase, p56(lck) or the protein tyrosine phosphatase CD45. Thus, we have identified high basal tyrosyl phosphorylation as a striking biochemical feature of NR cells that correlates with the unique functions of this subset. (C) 19 96 Academic Press, Inc.