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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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A myristoylated pseudosubstrate peptide of PKC-zeta induces degranulation in HMC-1 cells independently of PKC-zeta activity

Cited 14 times inthomson ciCited 14 times inthomson ci
Title
A myristoylated pseudosubstrate peptide of PKC-zeta induces degranulation in HMC-1 cells independently of PKC-zeta activity
Author
Lim, SeyoungChoi, Jung WoongKim, Hyeon SooKim, Yun-HeeYea, KyungmooHeo, KyanKim, Jong HyunKim, Sun-HeeSong, MinseokIl Kim, JaeRyu, Sung HoSuh, Pann-Ghill
Issue Date
2008-03
Publisher
PERGAMON-ELSEVIER SCIENCE LTD
Citation
LIFE SCIENCES, v.82, no.13-14, pp.733 - 740
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-zeta (zeta-PS; myristoyl-SIYRRGARRWRKL, a PKC-zeta inhibitor) regulates mast cell degranulation. zeta-PS increased [Ca+2](i) level at nanomolar concentrations in a PKC-zeta activity-independent manner in HMC-1 cells. Moreover, zeta-PS-induced [Ca+2](i) generation was completely abrogated by phospholipase C (PLC), IP3 receptor or G alpha(i/o). inhibitor and zeta-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 zeta-PS can induce degranulation in HMC-1 cells by triggering the calcium signal via a PKC-zeta-independent but G alpha(i/o), PLC and IP3-dependent pathways. (c) 2008 Elsevier Inc. All rights reserved.
URI
https://scholarworks.unist.ac.kr/handle/201301/10098
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=40849094196
DOI
10.1016/j.lfs.2008.01.005
ISSN
0024-3205
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BIO_Journal Papers
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