Protein kinase C plays a role in the induction of tyrosine phosphorylation of lymphoid microtubule-associated protein-2 kinase. Evidence for a CD3-associated cascade that includes pp56 super(lck) and that is defective in HPB-ALL

Ligation of the CD3 receptor induces multiple signal transduction events that modify the activation state of the T cell. We have compared two lines that express biologically active CD3 receptors but differ in their biochemical activation pathways during ligation of this receptor. Jurkat cells respon...

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Veröffentlicht in:The Journal of immunology (1950) 1991-01, Vol.147 (6), p.1933-1939
Hauptverfasser: Nel, A E, Hanekom, C, Hultin, L
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container_end_page 1939
container_issue 6
container_start_page 1933
container_title The Journal of immunology (1950)
container_volume 147
creator Nel, A E
Hanekom, C
Hultin, L
description Ligation of the CD3 receptor induces multiple signal transduction events that modify the activation state of the T cell. We have compared two lines that express biologically active CD3 receptors but differ in their biochemical activation pathways during ligation of this receptor. Jurkat cells respond to anti-CD3 with Ca super(2+) mobilization, PKC activation, induction of protein tyrosine phosphorylation, and activation of newly characterized lymphoid microtubule associated protein-2 kinase (MAP-2K). The results imply the existence of a kinase cascade that is initiated by PKC and, in the course of which, lck and MAP-2K may interact.
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ispartof The Journal of immunology (1950), 1991-01, Vol.147 (6), p.1933-1939
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source Alma/SFX Local Collection
subjects lck protein
lymphocytes
signal transduction
title Protein kinase C plays a role in the induction of tyrosine phosphorylation of lymphoid microtubule-associated protein-2 kinase. Evidence for a CD3-associated cascade that includes pp56 super(lck) and that is defective in HPB-ALL
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