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The Journal of Immunology, Vol 154, Issue 10 4965-4972, Copyright © 1995 by American Association of Immunologists

ARTICLES

Nerve growth factor induces activation of MAP-kinase and p90rsk in human B lymphocytes

RA Franklin, C Brodie, I Melamed, N Terada, JJ Lucas and EW Gelfand
Department of Pediatrics, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206, USA.

A previous report from this laboratory demonstrated that human B lymphocytes expressed nerve growth factor (NGF) receptors on their surface. On the basis of NGF enhancement of B cell proliferation these receptors are presumed to be functional. We have now characterized one of the signaling pathways that NGF may utilize in the functional activation of B lymphocytes. Stimulation of three different human B- lymphoblastoid cell lines with NGF induced the tyrosine phosphorylation and activation of the p42erk-2 isoform of MAP-kinase (MAPK). In addition, NGF induced shifts in the mobility of p90 ribosomal S6 kinase (p90rsk) on immunoblots and increased p90rsk kinase activity in immunoprecipitates. NGF-induced shifts in p90rsk mobility displayed similar dose and time kinetics as NGF-induced MAPK activation. Activation of both MAPK and p90rsk occurred with doses of NGF as low as 400 pg/ml. Preincubation of NGF with anti-NGF Ab inhibited NGF-induced activation of MAPK and p90rsk. These results demonstrate that the interaction of NGF with its receptor on human B cells results in the stimulation of major components of the signaling pathway also initiated by NGF-receptor ligation in cells of neuronal origin.


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