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Blood, Vol. 92 No. 4 (August 15), 1998:
pp. 1206-1218
Expression of Protein Kinase C Isozymes in Human Basophils:
Regulation by Physiological and Nonphysiological Stimuli
Katsushi Miura and
Donald W. MacGlashan Jr
From the Johns Hopkins Asthma and Allergy Center, Baltimore, MD.
The expression of protein kinase C (PKC) isozymes in human basophils
and the regulation of PKC isozymes during basophil activation by
phorbol 12-myristate 13-acetate (PMA) ± ionomycin,
f-met-leu-phe (FMLP), and anti-IgE antibody were examined. In human
basophils (> 98% purity), PKC I, II,  , and  were
expressed, PKC was difficult to detect, and PKC and  were
undetectable. In unstimulated basophils, PKCI and II were found
primarily in the cytosol fraction (95% ± 3% of total and 98% ± 1%, respectively). Within 5 minutes of stimulation with PMA (100 ng/mL), both PKCI and II were translocated to the membrane
fraction (85% ± 4% and 83% ± 6%, respectively). In
resting cells, 48% ± 3% and 61% ± 10% of PKC and
, respectively, existed in the membrane fraction. Within 1 minute of
stimulation with PMA, 90% ± 6% of PKC was found in the membrane
fraction, however, no translocation of PKC was apparent. Stimulation
with FMLP caused modest translocation ( 20%) of all PKC isozymes by 1 minute, whereas stimulation with anti-IgE antibody led to no detectable changes in PKC location throughout a 15-minute period of
measurement. However, concentrations of PMA and ionomycin that alone
caused no PKC translocation and little histamine release, together
caused significant histamine release but no apparent PKC translocation.
Studies with bis-indolylmaleimide analogs showed inhibition of
PMA-induced, but not anti-IgE-induced, histamine release. These
pharmacological studies suggest that PKC does not play a
prodegranulatory role in human basophil IgE-mediated secretion.
© 1998 by The American Society of Hematology.
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