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Open AccessJournal ArticleDOI

Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2.

TLDR
Two new cloned human cDNAs encode paralogs of the 85-kDa cytosolic phospholipase A2(cPLA2), giving the name cPLA2α to the well known 85-KDa enzyme, and residues activated by phosphorylation do not appear to be well conserved in either new enzyme.
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This article is published in Journal of Biological Chemistry.The article was published on 1999-03-26 and is currently open access. It has received 198 citations till now. The article focuses on the topics: Calmodulin & Binding site.

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The expanding superfamily of phospholipase A(2) enzymes: classification and characterization.

TL;DR: This review updates the classification of the various PLA(2)'s now described in the literature, and expands or realignment of Groups VI, VII and VIII, as well as the addition of Group XIPLA(2) from plants.
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Physiology of cell volume regulation in vertebrates.

TL;DR: Current knowledge regarding the molecular identity of these transport pathways and their regulation by, e.g., membrane deformation, ionic strength, Ca(2+), protein kinases and phosphatases, cytoskeletal elements, GTP binding proteins, lipid mediators, and reactive oxygen species are reviewed.
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JmjC-domain-containing proteins and histone demethylation.

TL;DR: The evolutionary relationship between Jumonji C (JmjC)-domain-containing proteins is analysed and their cellular functions in relation to their potential enzymatic activities are discussed.
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Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention.

TL;DR: The phospholipase A2 (PLA2) superfamily traces its roots to the identification of lytic actions of snake venom at the end of the 19th century and to the late 1980’s when PLA2-like activities were reported in mammalian cells in contrast to extracellular secreted activities from venom and pancreas.
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The phospholipase A2 superfamily and its group numbering system

TL;DR: The PLA(2) superfamily has grown continuously and over the intervening years has required several updates of this Group numbering system, so a number of new PLA( 2)s have been discovered and are now included in this update.
References
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Journal ArticleDOI

Basic Local Alignment Search Tool

TL;DR: A new approach to rapid sequence comparison, basic local alignment search tool (BLAST), directly approximates alignments that optimize a measure of local similarity, the maximal segment pair (MSP) score.
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Caspases: killer proteases

TL;DR: Caspases (cysteinyl aspartate-specific proteinases) mediate highly specific proteolytic cleavage events in dying cells, which collectively manifest the apoptotic phenotype.
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A novel arachidonic acid-selective cytosolic PLA2 contains a Ca2+-dependent translocation domain with homology to PKC and GAP

TL;DR: The cloning and expression of a cDNA encoding a high molecular weight cytosolic phospholipase A2 (cPLA2) that has no detectable sequence homology with the secreted forms of PLA2 is reported and it is demonstrated that cPLA2 selectively cleaves arachidonic acid from natural membrane vesicles and translocates to membrane vESicles in response to physiologically relevant changes in free calcium.
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Phosphatidylcholine breakdown and signal transduction

TL;DR: PC hydrolysis by PLA2, PLC or PLD is a widespread response elicited by most growth factors, cytokines, neurotransmitters, hormones and other extracellular signals and the mechanisms can involve G-proteins, PKC, Ca2+ and tyrosine kinase activities.
Journal ArticleDOI

Regulation of Phosphoinositide-specific Phospholipase C Isozymes

TL;DR: The hydrolysis of a minor membrane phospholipid, phosphatidylinositol 4,5-bisphosphate (PIP2), 1 by a specificospholipase C (PLC) is one of the earliest key events in the regulation of various cell functions by more than 100 extracellular signaling molecules.
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