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Tyrosine kinase and phosphotyrosine phosphatase activity in human
promyelocytic leukemia cells and human polymorphonuclear leukocytes
AS Kraft and RL Berkow
Although an increase in protein phosphorylation on tyrosine was first noted
as a result of cell transformation or the application of growth factors to
cells, recent reports have shown high levels of tyrosine kinases in
nondividing tissues. For that reason, we have investigated whether normal
human polymorphonuclear leukocytes (PMN) contain tyrosine kinase and
phosphatase activity. Using a copolymer of glutamine: tyrosine as a
substrate for the phosphotransferase reaction, we have demonstrated that
PMN contain a cytosolic tyrosine kinase activity that elutes as a single
peak from Sephacryl S-200 chromatography and has a molecular weight of 70
kilodaltons. Human promyelocytic leukemia cells (HL-60), contain a similar
activity (as demonstrated by column chromatography), with only 25% of the
activity found in PMN. This cytosolic tyrosine kinase can phosphorylate
angiotensin II and a fragment of the src protein containing tyrosine 416,
which suggests a similar substrate specificity to other tyrosine-
phosphorylating protein kinases. In addition, we have demonstrated that PMN
have double the amount of phosphotyrosine phosphatase (PTPase) activity of
that found in HL-60 cells. This enzyme has a Km of 0.932 mmol/L and a Vmax
of 0.355 mumol inorganic phosphate released/mg protein/min, which is
similar to other cellular PTPase. Activation of PMN with f-Met-Leu-Phe and
phorbol esters causes a slight but statistically significant drop in PMN
PTPase activity. These results suggest that terminally differentiated
myeloid cells have high tyrosine kinase and phosphatase activity, which may
play a role in stimulus response coupling in the mature PMN.
Volume 70,
Issue 2,
pp. 356-362,
08/01/1987
Copyright © 1987 by The American Society of Hematology
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