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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13-14
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pubmed:dateCreated |
2008-3-14
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pubmed:abstractText |
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 Galpha 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 Galpha i/o, PLC and IP3-dependent pathways.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/beta-N-Acetylhexosaminidases,
http://linkedlifedata.com/resource/pubmed/chemical/protein kinase C zeta
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0024-3205
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pubmed:author |
pubmed-author:ChoiJung WoongJW,
pubmed-author:HWEIC CCC,
pubmed-author:KimHyeon SooHS,
pubmed-author:KimJae IlJI,
pubmed-author:KimJong HyunJH,
pubmed-author:KimSun-HeeSH,
pubmed-author:KimYun-HeeYH,
pubmed-author:LimSeyoungS,
pubmed-author:RyuSung HoSH,
pubmed-author:SongMinseokM,
pubmed-author:SuhPann-GhillPG,
pubmed-author:YeaKyungmooK
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
82
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
733-40
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:18289606-Calcium,
pubmed-meshheading:18289606-Calcium Signaling,
pubmed-meshheading:18289606-Cell Degranulation,
pubmed-meshheading:18289606-Cell Line,
pubmed-meshheading:18289606-Enzyme Inhibitors,
pubmed-meshheading:18289606-GTP-Binding Protein alpha Subunits, Gi-Go,
pubmed-meshheading:18289606-Humans,
pubmed-meshheading:18289606-Inositol 1,4,5-Trisphosphate Receptors,
pubmed-meshheading:18289606-Ligands,
pubmed-meshheading:18289606-Mast Cells,
pubmed-meshheading:18289606-Microscopy, Confocal,
pubmed-meshheading:18289606-Oligopeptides,
pubmed-meshheading:18289606-Peptide Library,
pubmed-meshheading:18289606-Protein Kinase C,
pubmed-meshheading:18289606-Receptors, G-Protein-Coupled,
pubmed-meshheading:18289606-Substrate Specificity,
pubmed-meshheading:18289606-Type C Phospholipases,
pubmed-meshheading:18289606-beta-N-Acetylhexosaminidases
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pubmed:year |
2008
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pubmed:articleTitle |
A myristoylated pseudosubstrate peptide of PKC-zeta induces degranulation in HMC-1 cells independently of PKC-zeta activity.
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pubmed:affiliation |
Department of Life Science, Division of Molecular and Life Science, Biotech Center, Pohang University of Science and Technology, San 31 Hyoja-Dong, Nam-Gu, Pohang, Kyungbuk 790-784, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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