Opposing effects of protein kinase A and C on capacitative calcium entry into HL-60 promyelocytes
SCIE
SCOPUS
- Title
- Opposing effects of protein kinase A and C on capacitative calcium entry into HL-60 promyelocytes
- Authors
- Song, SK; Choi, SY; Kim, KT
- Date Issued
- 1998-09-01
- Publisher
- PERGAMON-ELSEVIER SCIENCE LTD
- Abstract
- Treatment of HL-60 cells with thapsigargin, a microsomal Ca2+/ATPase inhibitor, led to depletion of intracellular calcium stores followed by capacitative calcium entry. Stimulation of adenylyl cyclase with forskolin enhanced thapsigargin-induced Ca2+ influx. The forskolin effect was confirmed by enhanced fluorescence quenching induced by Mn2+ entry into fura-2 loaded cells. 1,9-Dideoxy-forskolin, an inactive analog of forskolin, did not affect capacitative calcium entry. On the other hand, phorbol 12-myristate 13-acetate (PMA), an activator of protein kinase C, inhibited thapsigargin-induced Ca2+ entry. Histamine and prostaglandin E-2 (PGE(2)) elevated intracellular adenosine 3':5'-cyclic monophosphate (cAMP) levels and enhanced the thapsigargin-induced capacitative calcium entry. Incubation with N-[2-(p-bromocynnamyl-amino)ethyl]-5-isoquinolinesulfonamide (H89), an inhibitor of protein kinase A (PKA), blocked the forskolin effect, and GF109203X, an inhibitor of protein kinase C (PKC), blocked the phorbol 12-myristate 13-acetate effect. The results suggest that protein kinase A regulates capacitative calcium entry positively, but that protein kinase C regulates Ca2+ influx negatively. Furthermore, after differentiation of HL-60 promyelocytes with dimethylsulfoxide to granulocytes, the inhibitory effect of phorbol 12-myristate 13-acetate became more pronounced, whereas the stimulatory effect of prostaglandin E-2 did not change. This result suggests that the regulation of capacitative calcium entry by protein kinase C and protein kinase A develops differently during differentiation. (C) 1998 Elsevier Science Inc.
- Keywords
- protein kinase A; protein kinase C; capacitative calcium entry; HL-60 cells; HUMAN NEUTROPHILS; CA2+ INFLUX; CHEMOTACTIC PEPTIDE; XENOPUS OOCYTES; CELL-LINE; INHIBITION; DIFFERENTIATION; PATHWAY; STORES; PHOSPHATASE
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/20667
- DOI
- 10.1016/S0006-2952(97)00660-6
- ISSN
- 0006-2952
- Article Type
- Article
- Citation
- BIOCHEMICAL PHARMACOLOGY, vol. 56, no. 5, page. 561 - 567, 1998-09-01
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- There are no files associated with this item.
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