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Blood, 1 November 2000, Vol. 96, No. 9, pp. 3215-3223
PHAGOCYTES
Identification and characterization of CKLiK, a novel granulocyte
Ca++/calmodulin-dependent kinase
Sandra Verploegen,
Jan-Willem J. Lammers,
Leo Koenderman, and
Paul J. Coffer
From the Department of Pulmonary Diseases, University
Medical Centre Utrecht, 3584 CX Utrecht, The Netherlands
Human granulocytes are characterized by a variety of specific
effector functions involved in host defense. Several widely expressed
protein kinases have been implicated in the regulation of these
effector functions. A polymerase chain reaction-based strategy was
used to identify novel granulocyte-specific kinases. A novel protein
kinase complementary DNA with an open reading frame of 357 amino acids
was identified with homology to calcium-calmodulin-dependent kinase I
(CaMKI). This has been termed CaMKI-like kinase (CKLiK). Analysis of
CKLiK messenger RNA (mRNA) expression in hematopoietic cells
demonstrated an almost exclusive expression in human polymorphonuclear leukocytes (PMN). Up-regulation of CKLiK mRNA occurs during
neutrophilic differentiation of CD34+ stem cells. CKLiK
kinase activity was dependent on Ca++ and calmodulin as
analyzed by in vitro phosphorylation of cyclic adenosine monophosphate
responsive element modulator (CREM). Furthermore, CKLiK- transfected
cells treated with ionomycin demonstrated an induction of
CRE- binding protein (CREB) transcriptional activity compared
to control cells. Additionally, CaMK-kinase enhanced CKLiK
activity. In vivo activation of CKLiK was shown by addition of
interleukin (IL)-8 to a myeloid cell line stably expressing CKLiK.
Furthermore inducible activation of CKLiK was sufficient to induce
extracellular signal-related kinase (ERK) mitogen-activated protein
(MAP) kinase activity. These data identify a novel
Ca++/calmodulin-dependent
PMN- specific kinase that may play a role in
Ca++-mediated regulation of human granulocyte functions.
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