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Methods in Enzymology 1991
Topics: Indicators and Reagents; Kinetics; Phospholipases; Phospholipases A; Phospholipids; Spectrophotometry; Sulfhydryl Compounds
PubMed: 2051946
DOI: 10.1016/0076-6879(91)97133-j -
Biochimica Et Biophysica Acta Dec 1998A large number of extracellular signals stimulate hydrolysis of phosphatidylinositol 4,5-bisphosphate by phosphoinositide-specific phospholipase C (PI-PLC). PI-PLC... (Review)
Review
A large number of extracellular signals stimulate hydrolysis of phosphatidylinositol 4,5-bisphosphate by phosphoinositide-specific phospholipase C (PI-PLC). PI-PLC isozymes have been found in a broad spectrum of organisms and although they have common catalytic properties, their regulation involves different signalling pathways. A number of recent studies provided an insight into domain organisation of PI-PLC isozymes and contributed towards better understanding of the structural basis for catalysis, cellular localisation and molecular changes that could underlie the process of their activation.
Topics: Animals; Hydrolysis; Isoenzymes; Models, Molecular; Phosphatidylinositol Diacylglycerol-Lyase; Phosphatidylinositols; Phosphoinositide Phospholipase C; Phospholipase C beta; Phospholipase C gamma; Phosphoric Diester Hydrolases; Type C Phospholipases
PubMed: 9838022
DOI: 10.1016/s0005-2760(98)00125-8 -
Zeitschrift Fur... Nov 1975Phospholipase D (phosphatidylcholine-phosphatidohydrolase, EC 3.1.4.4) hydrolyses lecithin into phosphatidic acid and choline. A review is given on the properties of... (Review)
Review
Phospholipase D (phosphatidylcholine-phosphatidohydrolase, EC 3.1.4.4) hydrolyses lecithin into phosphatidic acid and choline. A review is given on the properties of phospholipase D described in the literature; it deals with the occurrence and distribution of phospholipase D in higher plants, with it's pH and temperature, substrate specifity, activators, inhibitors and with occurrence and properties of bacterial phospholipase D.
Topics: Choline; Enzyme Activation; Hydrogen-Ion Concentration; Hydrolysis; Phosphatidic Acids; Phosphatidylcholines; Phospholipases; Plants
PubMed: 4933
DOI: 10.1007/BF01460064 -
Progress in Lipid Research Apr 2011Mammalian genomes encode genes for more than 30 phospholipase A₂s (PLA₂s) or related enzymes, which are subdivided into several classes including... (Review)
Review
Mammalian genomes encode genes for more than 30 phospholipase A₂s (PLA₂s) or related enzymes, which are subdivided into several classes including low-molecular-weight secreted PLA₂s (sPLA₂s), Ca²+-dependent cytosolic PLA₂s (cPLA₂s), Ca²+-independent PLA₂s (iPLA₂s), platelet-activating factor acetylhydrolases (PAF-AHs), lysosomal PLA₂s, and a recently identified adipose-specific PLA. Of these, the intracellular cPLA₂ and iPLA₂ families and the extracellular sPLA₂ family are recognized as the "big three". From a general viewpoint, cPLA₂α (the prototypic cPLA₂ plays a major role in the initiation of arachidonic acid metabolism, the iPLA₂ family contributes to membrane homeostasis and energy metabolism, and the sPLA₂ family affects various biological events by modulating the extracellular phospholipid milieus. The cPLA₂ family evolved along with eicosanoid receptors when vertebrates first appeared, whereas the diverse branching of the iPLA₂ and sPLA₂ families during earlier eukaryote development suggests that they play fundamental roles in life-related processes. During the past decade, data concerning the unexplored roles of various PLA₂ enzymes in pathophysiology have emerged on the basis of studies using knockout and transgenic mice, the use of specific inhibitors, and information obtained from analysis of human diseases caused by mutations in PLA₂ genes. This review focuses on current understanding of the emerging biological functions of PLA₂s and related enzymes.
Topics: Animals; Humans; Lipid Metabolism; Mice; Mice, Knockout; Mice, Transgenic; Phospholipases A2, Calcium-Independent; Phospholipases A2, Cytosolic; Phospholipases A2, Secretory
PubMed: 21185866
DOI: 10.1016/j.plipres.2010.12.001 -
Advances in Enzyme Regulation 2003
Review
Topics: Animals; Enzyme Inhibitors; Gene Expression Regulation, Enzymologic; Humans; Hydrolysis; Models, Biological; Models, Chemical; Phospholipase C gamma; Signal Transduction; Time Factors; Type C Phospholipases
PubMed: 12791384
DOI: 10.1016/s0065-2571(02)00027-4 -
Annals of the Rheumatic Diseases Apr 1989The activation of phospholipase A2 is believed to have an important role in the inflammatory process owing to its induction of eicosanoids, platelet activating factor,... (Review)
Review
The activation of phospholipase A2 is believed to have an important role in the inflammatory process owing to its induction of eicosanoids, platelet activating factor, and other mediators. Soluble phospholipase A2 has been associated with exudates in different inflammatory conditions. In this review the general physiology and control of this enzyme and, in particular, the most recent findings on human synovial fluid phospholipase A2s are discussed.
Topics: Enzyme Activation; Humans; Inflammation; Phospholipases; Phospholipases A; Phospholipases A2; Synovial Fluid
PubMed: 2653242
DOI: 10.1136/ard.48.4.267 -
Methods in Molecular Biology (Clifton,... 2018Phospholipases are lipolytic enzymes that hydrolyze phospholipid substrates at specific ester bonds. Phospholipases are widespread in nature and play very diverse roles... (Review)
Review
Phospholipases are lipolytic enzymes that hydrolyze phospholipid substrates at specific ester bonds. Phospholipases are widespread in nature and play very diverse roles from aggression in snake venom to signal transduction, lipid mediator production, and metabolite digestion in humans. Phospholipases vary considerably in structure, function, regulation, and mode of action. Tremendous advances in understanding the structure and function of phospholipases have occurred in the last decades. This introductory chapter is aimed at providing a general framework of the current understanding of phospholipases and a discussion of their mechanisms of action and emerging biological functions.
Topics: Animals; Humans; Hydrolysis; Intracellular Space; Lipid Metabolism; Multigene Family; Phospholipases; Phospholipids
PubMed: 30109646
DOI: 10.1007/978-1-4939-8672-9_3 -
Ryoikibetsu Shokogun Shirizu 1998
Review
Topics: Arachidonic Acid; Blood Platelet Disorders; Blood Platelets; Humans; Phospholipases
PubMed: 9833519
DOI: No ID Found -
Current Opinion in Pharmacology Apr 2006Despite substantial progress in preventing adverse cardiovascular events with current therapeutic strategies, there remains an extensive residual risk of clinical... (Review)
Review
Despite substantial progress in preventing adverse cardiovascular events with current therapeutic strategies, there remains an extensive residual risk of clinical events, particularly in high-risk patients. Because of the evidence implicating inflammation in the pathogenesis of atherosclerosis, identifying and targeting inflammatory pathways could help further reduce cardiovascular risk. There has been controversy regarding the role of lipoprotein-associated phospholipase A2 (Lp-PLA2) in atherosclerosis, partly because of the lack of simple animal models with a human-like pattern of Lp-PLA2 lipoprotein distribution. However, accumulating evidence from pathology, biology and epidemiology studies favors a pro-atherogenic rather than an atheroprotective role for the enzyme. In particular, Lp-PLA2 might play an important role in plaque vulnerability. As a result, additional studies are warranted to determine whether Lp-PLA2 inhibition improves plaque stability and ultimately clinical outcomes for high-risk patients.
Topics: 1-Alkyl-2-acetylglycerophosphocholine Esterase; Atherosclerosis; Cardiovascular Diseases; Enzyme Inhibitors; Humans; Phospholipases A; Phospholipases A2
PubMed: 16495153
DOI: 10.1016/j.coph.2005.11.008 -
Life Sciences 1991Phospholipases C and D are phosphodiesterases which act on phospholipid head groups. Although the presence of these enzymes in living organisms has long been known, it... (Comparative Study)
Comparative Study Review
Phospholipases C and D are phosphodiesterases which act on phospholipid head groups. Although the presence of these enzymes in living organisms has long been known, it is only recently that their role in cell signal transduction has been appreciated. The new developments on phospholipases D (PLD) are especially noteworthy, since these enzymes catalyze a novel pathway for second messenger generation. In a variety of mammalian cell systems, several biological or chemical agents have recently been shown to stimulate PLD activity. Depending on the system, activation of PLD has been suggested to be either dependent on, or independent of, Ca2+ and protein kinase C. PLD primarily hydrolyses phosphatidylcholine (PC) but phosphatidylinositol and phosphatidylethanolamine have also been reported as substrates. Different forms of endogenous PLD may also exist in cells. Exogenous addition of PLD causes alterations in cellular functions. In many instances, Ca2+ mobilizing agonists may stimulate both PLC and PLD pathways. Interestingly, several metabolites of these two enzymes are second messengers and are common to both pathways (e.g. phosphatidic acid, diglyceride). This has raised the issue of the interrelationship between these pathways. The regulation of either PLC or PLD by cellular components, e.g. guanine nucleotide binding proteins or protein kinases, is under intense investigation. These recent advances are providing novel information on the significance of phospholipase C and D mediated phospholipid turnover in cellular signalling. This review highlights some of these new discoveries and emerging issues, as well as challenges for future research on phospholipases.
Topics: Animals; Cell Communication; Humans; Phospholipase D; Second Messenger Systems; Type C Phospholipases
PubMed: 1997787
DOI: 10.1016/0024-3205(91)90031-6