Each of these chapters has a general section that describes the special needs for glycerolipid synthesis and the physiological context in which the regulation of phosphatidate phosphohydrolase activity can be understood.
| Title | : | Phosphatidate Phosphohydrolase (1988): Volume II |
| Author | : | David N Brindley |
| Language | : | en |
| Rating | : | 4.90 out of 5 stars |
| Type | : | PDF, ePub, Kindle |
| Uploaded | : | Apr 04, 2021 |
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Revival: Phosphatidate Phosphohydrolase (1988): Volume I - 1st
Phosphatidate Phosphohydrolase (1988): Volume II
Sphingosine inhibits phosphatidate phosphohydrolase in human neutrophils by protein kinase c-independent mechanism march 1991 journal of biological chemistry 266(4):2013-6.
Relationship between the displacement of phosphatidate phosphohydrolase from the membrane-associated compartment by chlorpromazine and the inhibition of the synthesis of triacylglycerol and phosphatidylcholine in rat hepatocytes.
Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/pa, lysophosphatidate/lpa, diacylglycerol pyrophosphate/dgpp, sphingosine 1-phosphate/s1p and ceramide 1-phosphate/c1p (pubmed:9705349, pubmed:9607309, pubmed:27694435).
Phosphatidylcholine hydrolysis by phospholipase d determines phosphatidate and diglyceride levels in chemotactic peptide-stimulated human neutrophils. Involvement of phosphatidate phosphohydrolase in signal transduction.
Phosphatidate phosphatase-1 (pap1) enzymes have a key role in glycerolipid synthesis through the conversion of phosphatidate to diacylglycerol, the immediate precursor of triacylglycerol, phosphatidylcholine, and phosphatidylethanolamine.
Phosphatidate phosphatase (pap) enzymes catalyze the dephosphorylation of phosphatidate, yielding diacylglycerol and inorganic phosphate. In eukaryotic cells, pap activity has a central role in the synthesis of phospholipids and triacylglycerol through its product diacylglycerol, and it also generates and/or degrades lipid-signaling molecules that are related to phosphatidate.
Each of these chapters has a general section that describes the special needs for glycerolipid synthesis and the physiological context in which the regulation of phosphatidate phosphohydrolase activity can be understood.
A novel ecto-phosphatidate phosphohydrolase activity mediates activation of neutrophil superoxide generation by exogenous phosphatidate january 1994 journal of biological chemistry 268(34):25302-10.
Phosphatidate phosphatase activity (pap) was first characterized in the mid 1950s as an enzyme mammalian lipid phosphate phosphohydrolases.
The later peak, containing both carbachol-stimulated [3h]cmp-phosphatidate and ptdins synthase activity, has a distribution in the gradient that is similar to nadph-cytochrome c reductase activity.
Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/pa, lysophosphatidate/lpa, diacylglycerol pyrophosphate/dgpp, sphingosine 1-phosphate/s1p and ceramide 1-phosphate/c1p (pubmed:9305923, pubmed:9705349, pubmed:9607309, pubmed:10962286, pubmed:17379599).
Phosphatidate phosphohydrolase: its role in glycerolipid synthesis.
The definition of the “ecto-phosphohydrolase” in work published so far relies on the assumption that the transmembrane movement of lipid phosphates is slow (unless specifically catalyzed by translocases). 32 p i from labeled pa and lyso-pa is also released quickly into the culture medium, whereas intracellular p i is not rapidly secreted.
Phosphatidate phosphohydrolase, tyrosine aminotransferase and glycerol kinase in isolated rat hepatocytes in relation to the control of triacylglycerol synthesis and gluconeogenesis.
Phosphatidic acid phosphohydrolase was initially described in plants by that this substrate is primarily supplied by activated sphingomyelinases (88, 237).
Converted to 1,2-sn-diacylglycerols by phosphatidate phosphohydrolase, which also was activated by il-1 via a separate mechanism involving a pertussis-sensi- tive g-protein. The activities of lyso-pa at and phos- phatidate phosphohydrolase were associated with plasma membrane enriched and refined microsomal fractions.
Propranolol, a beta-adrenergic receptor antagonist, also inhibits phosphatidate phosphohydrolase, the enzyme that converts phosphatidic acid into diacylglycerol.
Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/pa, lysophosphatidate/lpa, diacylglycerol pyrophosphate/dgpp, sphingosine 1-phosphate/s1p and ceramide 1-phosphate/c1p.
The oa-feeding significantly increased the activity of hepatic microsomal phosphatidate phosphohydrolase (pap), which is the rate-limiting enzyme for tg synthesis. Hepatic glucose-6-phosphate dehydrogenase (g6pdh) and malic enzyme activities were also increased.
4) is a key regulatory enzyme in lipid metabolism, catalyzing the conversion of phosphatidate to diacylglycerol. The two substrates of pap are phosphatidate and h 2 o, and its two products are diacylglycerol and phosphate, as shown here.
N‐ethylmaleimide–sensitive and –insensitive phosphatidate phosphohydrolase activities were measured in needle liver biopsy specimens from 42 alcoholic patients and 6 patients with primary biliary cirrhosis and in wedge biopsy specimens from 6 normal patients undergoing routine cholecystectomy.
Barrier disruption effected by dioctanoyl (di-c8) phosphatidate was markedly potentiated by the addition of propranolol, an inhibitor of endothelial cell ecto-phosphatidate phosphohydrolase (pap), a lipid phosphate phosphohydrolase (lpp) that efficiently hydrolyzes extracellular substrate.
4) catalyzes the hydrolysis of phosphatidate to yield sn-1,2-diacylglycerol and inorganic phosphate.
4) is a key regulatory enzyme in lipid metabolism, phosphatidate phosphohydrolase, and; lipid phosphate phosphohydrolase (lpp).
However, bel is also known to inhibit another key enzyme of phospholipid metabolism, namely the magnesium-dependent phosphatidate phosphohydrolase-1 (pap-1). In this work we report that bel is able to promote apoptosis in a variety of cell lines, including u937, thp-1, and monomac (human phagocyte), raw264.
Mg(2+)-dependent phosphatidate (pa) phosphatase which catalyzes the dephosphorylation of pa to yield diacylglycerol. Required for de novo lipid synthesis and formation of lipid droplets. Controles transcription of phospholipid biosynthetic genes and nuclear structure by regulating the amount of membrane present at the nuclear envelope.
Phosphatidate phosphohydrolase, measured with phosphatidate emulsion, was activated by 1m m-mg 2+ in all but the mitochondrial fraction of euthyroid rabbit hearts. The activation was more pronounced in subcellular fractions isolated from hyperthyroid hearts, so that the measured activities were significantly increased above those of the controls.
(1988) inhibition of apolipoprotein secretion and phosphatidate phosphohydrolase activity by eicosapentaenoic and docosahexaenoic acids in the perfused rat liver,metabolism 37, 1177–1181.
These generate diacylglycerol and phosphatidate, respectively, although the two lipids are also apparently interconvertable through the actions of phosphatidate phosphohydrolase and diacylglycerol kinase. Diacylglycerol activates protein kinase c while one role for phosphatidate is the activation of actin stress fiber formation.
A mg 2+-independent and n-ethylmaleimide-insensitive phosphatidate phosphohydrolase (pap-2) has been identified in the plasma membrane of cells and it has been purified. The enzyme is a multi-functional phosphohydrolase that can dephosphorylate phosphatidate, lysophosphatidate, sphingosine 1-phosphate and ceramide 1-phosphate and these substrates are competitive inhibitors of the reaction.
Characterization of phosphatidate phosphohydrolase activity associated with chloroplast envelope membranes.
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