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
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.