Science, Vol 247, Issue 4946, 1079-1082
Copyright © 1990 by American Association for the Advancement of Science
Tyrosine kinase activity and transformation potency of bcr-abl oncogene products
TG Lugo,
AM Pendergast,
AJ Muller,
and
ON Witte
Department of Microbiology, University of California, Los Angeles 90024.
Oncogenic activation of the proto-oncogene c-abl in human leukemias occurs as a result of the addition of exons from the gene bcr and truncation of the first abl exon. Analysis of tyrosine kinase activity and quantitative measurement of transformation potency in a single-step assay indicate that variation in bcr exon contribution results in a functional difference between p210bcr-abl and p185bcr-abl proteins. Thus, foreign upstream sequences are important in the deregulation of the kinase activity of the abl product, and the extent of deregulation correlates with the pathological effects of the bcr-abl proteins.
