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J. Biol. Chem., Vol. 266, Issue 14, 8667-8670, 05, 1991
RK Cheung and HM Dosch
Epstein-Barr virus (EBV) exposure of human B lymphocytes induces rapid,
Ca(2+)-dependent tyrosine phosphorylation of two cytosolic proteins, one
likely the CD21 EBV receptor and another unknown species of 55-60 kDa. We
now identify the latter protein as the tyrosine kinase lck (p56lck). In T
cells many activation events reduce the high constitutive p56lck expression
levels typical for that lineage, and they induce the appearance of a 60-kDa
lck species. We now demonstrate that in B cells exposed to EBV the at best
low constitutive p56lck expression levels are rapidly and transiently
up-regulated without generation of 60-kDa lck. lck-specific antisense
oligonucleotides block p56lck induction and prevent subsequent B cell
activation and immortalization whereas B cell activation by nononcogenic
agents was unaffected. We propose that p56lck superinduction is a
transformation prerequisite which signals entry into the oncogenic growth
transformation process.
The tyrosine kinase lck is critically involved in the growth transformation of human B lymphocytes
Department of Pediatrics, University of Toronto, Ontario, Canada.
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