2-Benzyloxybenzaldehyde inhibits formyl peptide-stimulated increase in intracellular Ca2+ in neutrophils mainly by blocking Ca2+ entry |
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Authors: | Jih-Pyang Wang Ling-Chu Chang Yu-Hsiang Kuan Lo-Ti Tsao Li-Jiau Huang Sheng-Chu Kuo |
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Institution: | (1) Department of Education and Research, Taichung Veterans General Hospital, Taichung, Taiwan; Graduate Institute of Pharmaceutical Chemistry, China Medical University, Taichung, Taiwan, ROC;(2) Department of Education and Research, Taichung Veterans General Hospital, Taichung, Taiwan, ROC;(3) Institute of Medicine, Chung Shan Medical University, Taichung, Taiwan, ROC;(4) Graduate Institute of Pharmaceutical Chemistry, China Medical University, Taichung, Taiwan, ROC |
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Abstract: | 2-Benzyloxybenzaldehyde (CCY1a) inhibited the formyl-Met-Leu-Phe (fMLP)-induced elevation of cytosolic Ca2+] (Ca2+]i) in rat neutrophils. The late plateau phase, but not the initial Ca2+ spike, of the fMLP-induced Ca2+]i change was inhibited by CCY1a. In the absence of external Ca2+, CCY1a had no appreciable effect on either the fMLP- or cyclopiazonic acid (CPA)-induced Ca2+]i elevation. CCY1a failed to inhibit Ca2+]i changes induced by N-ethylmaleimide, GEA3162, ionomycin or sphingosine, but slightly inhibited the Ca2+ signals elicited by ATP or interleukin-8 (IL-8). In a classical Ca2+ readdition protocol, addition of CCY1a after cell activation strongly inhibited the Ca2+]i response to fMLP, whilst that to CPA was only slightly reduced. CCY1a nearly abrogated the fMLP-stimulated Mn2+ influx but was less effective on the CPA-induced response. CCY1a attenuated the levels of tyrosine-phosphorylated bands in the 70–85 kDa molecular mass range. CCY1a had no effect on the basal Ca2+]i level, the pharmacologically isolated plasma membrane Ca2+-ATPase activity or on the mitochondrial membrane potential. Thus, CCY1a blocks fMLP-induced Ca2+ entry into neutrophils probably by blocking the relevant Ca2+ channel directly or, alternatively, indirectly through the attenuation of tyrosine phosphorylation of some cellular proteins. |
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Keywords: | CCY1a Rat neutrophils Intracellular free Ca2+ concentration Ca2+ entry Protein tyrosine phosphorylation |
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