Studies with protein kinase C inhibitors presently available cannot elucidate the role of protein kinase C in the activation of NADPH oxidase |
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| Authors: | R Seifert C Sch?chtele |
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| Institution: | 1. Institut für Pharmakologie, Freie Universität Berlin, Thielallee 69/73, D-1000 Berlin 33, F.R.G.;2. Goedecke Forschungsinstitut, Biochemische Pharmakologie, Mooswaldallee 1/9, D-7800 Freiburg, F.R.G.;1. Institute of Ophthalmic Diseases, Guangxi Academy of Medical Sciences & Department of Ophthalmology, the People''s Hospital of Guangxi Zhuang Autonomous Region & Guangxi Key Laboratory of Eye Health & Guangxi Health Commission Key Laboratory of Ophthalmology and Related Systemic Diseases Artificial Intelligence Screening Technology, Nanning 530000, Guangxi, China;2. State Key Laboratory of Ophthalmology, Zhongshan Ophthalmic Center, Sun Yat-sen University, Guangdong Provincial Key Laboratory of Ophthalmology and Visual Science, 7 Jinsui Road, Guangzhou 510060, China;3. Life Science Institute, Guangxi Medical University, Nanning 530021, China;4. Laboratory Animal Center, Guangxi Medical University, Nanning 530021, China;5. School of Basic Medical Science, Guangxi Medical University, Nanning 530021, China;6. Guangxi Key Laboratory of Regenerative Medicine, Guangxi Medical University, Nanning 530021, China;1. Anatomy and Histology, Bosch Institute, The University of Sydney, Sydney, NSW, Australia;2. Glucox Biotech AB, Stockholm, Sweden;3. Save Sight Institute, The University of Sydney, Sydney, NSW, Australia |
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| Abstract: | The effects of various protein kinase C (PKC) inhibitors on NADPH oxidase (NO) activation by the phorbol ester PMA and by the chemotactic peptide FMLP were studied. H-7 reduced the effects of both stimuli in human neutrophils (HN) and HL-60 cells by 13-63%. Polymyxin B did not inhibit NO activation by PMA and FMLP in HN and reduced the effects of both stimuli in HL-60 cells by 27-55%. Retinal and retinoic acid enhanced the effects of PMA and FMLP in HL-60 cells and of FMLP in HN up to 4.5-fold. In contrast, retinoic acid inhibited the effect of PMA in HN. In the presence of cytochalasin B, retinal inhibited the effect of FMLP in HN, whereas retinoic acid inhibited NO activation by FMLP in both cell types. The dual PKC/calmodulin inhibitors trifluoperazine and W-7 abolished NO activation by PMA and FMLP in HN and HL-60 cells. Thus, the effects of PKC inhibitors on NO activation exhibit (1) cell type specificity, (2) stimulus dependency and (3) no correlation with in vitro inhibition of PKC. Our results suggest that studies with PKC inhibitors presently available cannot clarify the role of PKC in NO activation. |
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