A myristoylated pseudosubstrate peptide of PKC-ζ induces degranulation in HMC-1 cells independently of PKC-ζ activity
- Authors
- Lim S.; Choi J.W.; Kim H.S.; Kim Y.-H.; Yea K.; Heo K.; Kim J.H.; Kim S.-H.; Song M.; Kim J.I.; Ryu S.H.; Suh P.-G.
- Issue Date
- 2008
- Keywords
- ζ-PS; Calcium; Degranulation; IP3; Mast cells; Phospholipase C
- Citation
- Life Sciences, v.82, no.13-14, pp 733 - 740
- Pages
- 8
- Indexed
- SCOPUS
- Journal Title
- Life Sciences
- Volume
- 82
- Number
- 13-14
- Start Page
- 733
- End Page
- 740
- URI
- https://scholarworks.korea.ac.kr/kumedicine/handle/2020.sw.kumedicine/17472
- DOI
- 10.1016/j.lfs.2008.01.005
- ISSN
- 0024-3205
1879-0631
- Abstract
- Mast cells play a central role in allergic disease and host defense against several pathogens through the release of various bioactive compounds via degranulation. In this study, we found that a myristoylated pseudosubstrate of PKC-ζ (ζ-PS; myristoyl-SIYRRGARRWRKL, a PKC-ζ inhibitor) regulates mast cell degranulation. ζ-PS increased [Ca+2]i level at nanomolar concentrations in a PKC-ζ activity-independent manner in HMC-1 cells. Moreover, ζ-PS-induced [Ca+2]i generation was completely abrogated by phospholipase C (PLC), IP3 receptor or Gαi/o inhibitor and ζ-PS potently induced degranulation in HMC-1 cells which was significantly inhibited by pretreating PLC inhibitors or a calcium chelator. Therefore, our results suggest that ζ-PS can induce degranulation in HMC-1 cells by triggering the calcium signal via a PKC-ζ-independent but Gαi/o, PLC and IP3-dependent pathways. © 2008 Elsevier Inc. All rights reserved.
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Collections - 1. Basic Science > Department of Anatomy > 1. Journal Articles
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