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Signal transduction mechanism in human neutrophil: comparative study between the ζ and β-protein kinase c isotypes

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Abstract

Role of protein kinase C (PKC) isotypes in the regulation of neutrophil function are not clearly known. In the present study we purified the β-PKC and ζ-PKC isotypes from human neutrophil. Both the isotypes are immunoreactive only to their respective antibodies. ζ-PKC was further confirmed by RT-PCR using specific primer. Co-factor requirements for both the kinases were found to be different when DG and ceramide were used as second messenger. Selective substrate specificities were determined for both β and ζ-PKC using isotype specific pseudosubstrates viz., [Ser25]PKC [19-31] and [Ser119]PKC[113-130] respectively. Endogenous protein phosphorylation by purified β-PKC and ζ-PKC showed their functional differences in neutrophil. β-PKC phosphorylated 13, 15, 19, 33, 36, 47, 80 and 92 kDa proteins and ζ-PKC phosphorylated 19, 22, 42, 47, 75 and 87 kDa proteins, only exception was the phosphorylation of 47 kDa protein which had been phosphorylated by both the kinases. Differences in phosphorylation between β-PKC and ζ-PKC clearly indicate the selective role for these PKC isotypes in the activation sequences of neutrophil.

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  1. Department of Microbiology, Bose Institute, P 1/12, CIT, Scheme VII M, Calcutta, India

    Sonali Das, Sandip Bhattacharyya, Sanjukta Ghosh & Subrata Majumdar

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  1. Sonali Das
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Das, S., Bhattacharyya, S., Ghosh, S. et al. Signal transduction mechanism in human neutrophil: comparative study between the ζ and β-protein kinase c isotypes. Mol Cell Biochem 203, 143–151 (2000). https://doi.org/10.1023/A:1007097220890

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