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Expression of phosphoinositide-specific phospholipase C isoforms in native endothelial cells

Phospholipase C (PLC) comprises a superfamily of enzymes that play a key role in a wide array of intracellular signalling pathways, including protein kinase C and intracellular calcium. Thirteen different mammalian PLC isoforms have been identified and classified into 6 families (PLC-β, γ, δ, ε, ζ a...

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Published in:PloS one 2015-04, Vol.10 (4), p.e0123769-e0123769
Main Authors: Béziau, Delphine M, Toussaint, Fanny, Blanchette, Alexandre, Dayeh, Nour R, Charbel, Chimène, Tardif, Jean-Claude, Dupuis, Jocelyn, Ledoux, Jonathan
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creator Béziau, Delphine M
Toussaint, Fanny
Blanchette, Alexandre
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Charbel, Chimène
Tardif, Jean-Claude
Dupuis, Jocelyn
Ledoux, Jonathan
description Phospholipase C (PLC) comprises a superfamily of enzymes that play a key role in a wide array of intracellular signalling pathways, including protein kinase C and intracellular calcium. Thirteen different mammalian PLC isoforms have been identified and classified into 6 families (PLC-β, γ, δ, ε, ζ and η) based on their biochemical properties. Although the expression of PLC isoforms is tissue-specific, concomitant expression of different PLC has been reported, suggesting that PLC family is involved in multiple cellular functions. Despite their critical role, the PLC isoforms expressed in native endothelial cells (ECs) remains undetermined. A conventional PCR approach was initially used to elucidate the mRNA expression pattern of PLC isoforms in 3 distinct murine vascular beds: mesenteric (MA), pulmonary (PA) and middle cerebral arteries (MCA). mRNA encoding for most PLC isoforms was detected in MA, MCA and PA with the exception of η2 and β2 (only expressed in PA), δ4 (only expressed in MCA), η1 (expressed in all but MA) and ζ (not detected in any vascular beds tested). The endothelial-specific PLC expression was then sought in freshly isolated ECs. Interestingly, the PLC expression profile appears to differ across the investigated arterial beds. While mRNA for 8 of the 13 PLC isoforms was detected in ECs from MA, two additional PLC isoforms were detected in ECs from PA and MCA. Co-expression of multiple PLC isoforms in ECs suggests an elaborate network of signalling pathways: PLC isoforms may contribute to the complexity or diversity of signalling by their selective localization in cellular microdomains. However in situ immunofluorescence revealed a homogeneous distribution for all PLC isoforms probed (β3, γ2 and δ1) in intact endothelium. Although PLC isoforms play a crucial role in endothelial signal transduction, subcellular localization alone does not appear to be sufficient to determine the role of PLC in the signalling microdomains found in the native endothelium.
doi_str_mv 10.1371/journal.pone.0123769
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Thirteen different mammalian PLC isoforms have been identified and classified into 6 families (PLC-β, γ, δ, ε, ζ and η) based on their biochemical properties. Although the expression of PLC isoforms is tissue-specific, concomitant expression of different PLC has been reported, suggesting that PLC family is involved in multiple cellular functions. Despite their critical role, the PLC isoforms expressed in native endothelial cells (ECs) remains undetermined. A conventional PCR approach was initially used to elucidate the mRNA expression pattern of PLC isoforms in 3 distinct murine vascular beds: mesenteric (MA), pulmonary (PA) and middle cerebral arteries (MCA). mRNA encoding for most PLC isoforms was detected in MA, MCA and PA with the exception of η2 and β2 (only expressed in PA), δ4 (only expressed in MCA), η1 (expressed in all but MA) and ζ (not detected in any vascular beds tested). The endothelial-specific PLC expression was then sought in freshly isolated ECs. Interestingly, the PLC expression profile appears to differ across the investigated arterial beds. While mRNA for 8 of the 13 PLC isoforms was detected in ECs from MA, two additional PLC isoforms were detected in ECs from PA and MCA. Co-expression of multiple PLC isoforms in ECs suggests an elaborate network of signalling pathways: PLC isoforms may contribute to the complexity or diversity of signalling by their selective localization in cellular microdomains. However in situ immunofluorescence revealed a homogeneous distribution for all PLC isoforms probed (β3, γ2 and δ1) in intact endothelium. Although PLC isoforms play a crucial role in endothelial signal transduction, subcellular localization alone does not appear to be sufficient to determine the role of PLC in the signalling microdomains found in the native endothelium.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25875657</pmid><doi>10.1371/journal.pone.0123769</doi><oa>free_for_read</oa></addata></record>
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subjects Animals
Arteries
Arteries - enzymology
Calcium
Calcium (intracellular)
Cellular signal transduction
Endothelial cells
Endothelial Cells - enzymology
Endothelium
Enzymes
Family
Gene expression
Gene Expression Regulation, Enzymologic
Heart
Immunofluorescence
Intracellular
Intracellular signalling
Isoenzymes - genetics
Isoenzymes - metabolism
Isoforms
Kinases
Localization
Medicine
Mice, Inbred C57BL
Phosphoinositide Phospholipase C - genetics
Phosphoinositide Phospholipase C - metabolism
Phospholipase
Phospholipase C
Phospholipases
Physiology
Protein kinase C
Proteins
Regulation
RNA
RNA, Messenger - genetics
RNA, Messenger - metabolism
Signal transduction
Subcellular Fractions - enzymology
Veins & arteries
title Expression of phosphoinositide-specific phospholipase C isoforms in native endothelial cells
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