Abstract
Cytosolic PLA2 (cPLA2) and Ca(2+)-independent PLA2 (iPLA2) play a significant role in insulin β-cells secretion. Bacterial infections may be responsible of the onset of diabetes. The mechanism by which Staphylococcus aureus infection of INS-1 cells alters glucose-induced insulin secretion has been examined. After acute infection, insulin secretion and PLA2 activities significantly increased. Moreover, increased expressions of phospho-cPLA2, phospho-PKCα and phospho-ERK 1/2 were observed. Chronic infection causes a decrease in insulin release and a significant increase of iPLA2 and COX-2 protein expression. Moreover, insulin secretion in infected cells could be restored using specific siRNAs against iPLA2 isoform and specific COX-2 inhibitor.
Keywords:
INS-1E cell; Insulin; Phospholipases A(2); Staphylococcus aureus; siRNA.
Copyright © 2015. Published by Elsevier B.V.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cell Line, Tumor
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Cyclooxygenase 2 / chemistry
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Cyclooxygenase 2 / metabolism
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Cyclooxygenase 2 Inhibitors / pharmacology
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Diabetes Mellitus, Type 1 / etiology
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Group IV Phospholipases A2 / metabolism*
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Group VI Phospholipases A2 / antagonists & inhibitors
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Group VI Phospholipases A2 / genetics
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Group VI Phospholipases A2 / metabolism*
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Host-Pathogen Interactions* / drug effects
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Insulin / metabolism*
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Insulin Secretion
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Insulin-Secreting Cells / drug effects
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Insulin-Secreting Cells / enzymology
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Insulin-Secreting Cells / metabolism*
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Insulin-Secreting Cells / microbiology
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Kinetics
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MAP Kinase Signaling System / drug effects
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Methicillin-Resistant Staphylococcus aureus / physiology*
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Pancreatitis / microbiology
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Pancreatitis / physiopathology
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Phosphorylation / drug effects
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Protein Kinase C-alpha / metabolism
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Protein Processing, Post-Translational / drug effects
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RNA Interference
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Rats
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Staphylococcal Infections / microbiology
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Staphylococcal Infections / physiopathology
Substances
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Cyclooxygenase 2 Inhibitors
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Insulin
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Cyclooxygenase 2
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Ptgs2 protein, rat
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Protein Kinase C-alpha
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Group IV Phospholipases A2
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Group VI Phospholipases A2
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Pla2g4a protein, rat
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Pla2g6 protein, rat