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Inhibition of H₂ Histamine Receptor-Mediated Cation Channel Opening by Protein Kinase C in Human Promyelocytic Cells¹

Byung-Chang Suh^*, Hyun Lee^*, Dong-Jae Jun^*, Jang-Soo Chun, Jong-Hee Lee^* and Kyong-Tai Kim^2,*

^* Department of Life Science, Division of Molecular and Life Science, Pohang University of Science and Technology, Pohang, Republic of Korea; and Department of Life Science, Kwangju Institute of Science and Technology, Kwangju, Republic of Korea

Histamine, through H₂ receptors, triggers a prominent rise in intracellular free Ca²⁺ concentration ([Ca²⁺]_i) in addition to an elevation of cAMP level in HL-60 promyelocytes. Here we show that the histamine-induced [Ca²⁺]_i rise was due to influx of Ca²⁺ from the extracellular space, probably through nonselective cation channels, as incubation of the cells with SKF 96365 abolished the histamine-induced [Ca²⁺]_i rise, Na⁺ influx, and membrane depolarization. The Ca²⁺ influx was specifically inhibited by pretreatment of the cells with PMA or extracellular ATP with 50% inhibitory concentrations of 0.12 ± 0.03 nM and 185 ± 17 µM, respectively. Western blot analysis of protein kinase C (PKC) isoforms revealed that PMA (1 nM) and ATP (300 µM) caused selective translocation of PKC- to the particulate/membrane fraction. Costimulation of the cells with histamine and SKF 96365 partially reduced histamine-induced granulocytic differentiation, which was evaluated by looking at the extent of fMet-Leu-Phe-induced [Ca²⁺]_i rise and superoxide generation. In conclusion, nonselective cation channels are opened by stimulation of the H₂ receptor, and the channels are at least in part involved in the induction of histamine-mediated differentiation processes. Both effects of histamine were selectively inhibited probably by the isoform of PKC in HL-60 cells.

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