Identification of a novel class of mammalian phosphoinosital-specific phospholipase C enzymes

Alan J. Stewart, Joy Mukherjee, Scott J. Robers, Douglas H. Lester, Colin Farquharson

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

Phosphoinositol (PhoIns)-specific phospholipase C enzymes (PLCs) are central to the inositol lipid signaling pathways and contribute to intracellular Ca2+ release and protein kinase C activation. Five distinct classes of PhoIns-specific PLCs are known to exist in mammals, which are activated by membrane receptor-mediated events. Here we have identified a sixth class of PhoIns-specific PLC with a novel domain structure, which we have termed PLC-η. Two putative PLC-η enzymes were identified in humans and in mice. Sequence analysis revealed that residues implicated in substrate binding and catalysis from other PhoIns-specific PLCs are conserved in the novel enzymes. PLC-η enzymes are most closely related to the PLC-δ class and share a close evolutionary relationship with other PLC isozymes. EST analysis and RT-PCR data suggest that PLC-η enzymes are expressed in several cell types and, by analogy with other mammalian PhoIns-specific PLCs, are likely to be involved in signal transduction pathways
Original languageEnglish
Pages (from-to)117-121
Number of pages5
JournalInternational Journal of Molecular Medicine
Volume15
Issue number1
DOIs
Publication statusPublished - 1 Jan 2005

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Type C Phospholipases
Enzymes
Phosphoinositide Phospholipase C
Expressed Sequence Tags
Inositol
Catalysis
Protein Kinase C
Isoenzymes
Sequence Analysis
Mammals
Signal Transduction
Lipids
Polymerase Chain Reaction
Membranes

Cite this

Stewart, Alan J. ; Mukherjee, Joy ; Robers, Scott J. ; Lester, Douglas H. ; Farquharson, Colin. / Identification of a novel class of mammalian phosphoinosital-specific phospholipase C enzymes. In: International Journal of Molecular Medicine. 2005 ; Vol. 15, No. 1. pp. 117-121.
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Identification of a novel class of mammalian phosphoinosital-specific phospholipase C enzymes. / Stewart, Alan J.; Mukherjee, Joy; Robers, Scott J.; Lester, Douglas H.; Farquharson, Colin.

In: International Journal of Molecular Medicine, Vol. 15, No. 1, 01.01.2005, p. 117-121.

Research output: Contribution to journalArticle

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AU - Stewart, Alan J.

AU - Mukherjee, Joy

AU - Robers, Scott J.

AU - Lester, Douglas H.

AU - Farquharson, Colin

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AB - Phosphoinositol (PhoIns)-specific phospholipase C enzymes (PLCs) are central to the inositol lipid signaling pathways and contribute to intracellular Ca2+ release and protein kinase C activation. Five distinct classes of PhoIns-specific PLCs are known to exist in mammals, which are activated by membrane receptor-mediated events. Here we have identified a sixth class of PhoIns-specific PLC with a novel domain structure, which we have termed PLC-η. Two putative PLC-η enzymes were identified in humans and in mice. Sequence analysis revealed that residues implicated in substrate binding and catalysis from other PhoIns-specific PLCs are conserved in the novel enzymes. PLC-η enzymes are most closely related to the PLC-δ class and share a close evolutionary relationship with other PLC isozymes. EST analysis and RT-PCR data suggest that PLC-η enzymes are expressed in several cell types and, by analogy with other mammalian PhoIns-specific PLCs, are likely to be involved in signal transduction pathways

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