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Phospholipase D

(Synonyms: 磷脂酶D) 目录号 : GC20127

Phospholipase D Chemical Structure

Cas No.:9001-87-0

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Chemical Properties

Cas No. 9001-87-0 SDF
别名 磷脂酶D
分子式 C9H14N4O3 分子量 226.232
溶解度 储存条件 -20℃
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储备液的保存方式和期限:-80°C 储存时,请在 6 个月内使用,-20°C 储存时,请在 1 个月内使用。
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 4.4202 mL 22.1012 mL 44.2024 mL
5 mM 0.884 mL 4.4202 mL 8.8405 mL
10 mM 0.442 mL 2.2101 mL 4.4202 mL
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Research Update

Phospholipase D

Biochem Cell Biol 2004 Feb;82(1):225-53.PMID:15052340DOI:10.1139/o03-079.

Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals. Although enzymes with broader selectivity are found in some of the lower organisms, the plant, yeast, and mammalian enzymes are selective for phosphatidylcholine. The two mammalian Phospholipase D isoforms are regulated by protein kinases and GTP binding proteins of the ADP-ribosylation and Rho families. Mammalian and yeast phospholipases D are also potently stimulated by phosphatidylinositol 4,5-bisphosphate. This review discusses the identification, characterization, structure, and regulation of Phospholipase D. Genetic and pharmacological approaches implicate Phospholipase D in a diverse range of cellular processes that include receptor signaling, control of intracellular membrane transport, and reorganization of the actin cytoskeleton. Most ideas about Phospholipase D function consider that the phosphatidic acid product is an intracellular lipid messenger. Candidate targets for phospholipase-D-generated phosphatidic acid include phosphatidylinositol 4-phosphate 5-kinases and the raf protein kinase. Phosphatidic acid can also be converted to two other lipid mediators, diacylglycerol and lyso phosphatidic acid. Coordinated activation of these phospholipase-D-dependent pathways likely accounts for the pleitropic roles for these enzymes in many aspects of cell regulation.

Mammalian Phospholipase D: Function, and therapeutics

Prog Lipid Res 2020 Apr;78:101018.PMID:31830503DOI:10.1016/j.plipres.2019.101018.

Despite being discovered over 60 years ago, the precise role of Phospholipase D (PLD) is still being elucidated. PLD enzymes catalyze the hydrolysis of the phosphodiester bond of glycerophospholipids producing phosphatidic acid and the free headgroup. PLD family members are found in organisms ranging from viruses, and bacteria to plants, and mammals. They display a range of substrate specificities, are regulated by a diverse range of molecules, and have been implicated in a broad range of cellular processes including receptor signaling, cytoskeletal regulation and membrane trafficking. Recent technological advances including: the development of PLD knockout mice, isoform-specific antibodies, and specific inhibitors are finally permitting a thorough analysis of the in vivo role of mammalian PLDs. These studies are facilitating increased recognition of PLD's role in disease states including cancers and Alzheimer's disease, offering potential as a target for therapeutic intervention.

Phospholipase D

Ann N Y Acad Sci 2000 Apr;905:61-8.PMID:10818442DOI:10.1111/j.1749-6632.2000.tb06538.x.

Phospholipase D is an ubiquitous enzyme that hydrolyzes phosphatidylcholine to phosphatidic acid and choline. Its cellular actions are related to the production of phosphatidic acid and include alterations to cell growth, shape, and secretion. There are two mammalian Phospholipase D genes whose products (PLD1 and PLD2) are alternatively spliced. Both forms have two highly conserved HKD motifs that are essential for catalysis and dimerization. PLD1 is regulated in vitro and in vivo by protein kinase C and small GTPases of the Rho and ARF families, whereas PLD2 shows a higher basal activity with little or no response to these proteins. The cellular locations and specific functions of the two PLD isoforms remain to be established.

Phospholipase D and phosphatidic acid in plant immunity

Plant Sci 2019 Feb;279:45-50.PMID:30709492DOI:10.1016/j.plantsci.2018.05.021.

Phospholipase D (PLD) hydrolyzes membrane phospholipids to generate phosphatidic acid (PA). Both PLD and its lipid product PA are involved in various physiological processes, including plant response to pathogens. The PLD family is comprised of multiple members in higher plants, and PLDs have been reported to play positive and/or negative roles in plant immunity, depending on the types of pathogens and specific PLDs involved. Individual PLDs have distinguishable biochemical properties, such as Ca2+ and phosphatidylinositide requirements. In addition, PLDs and PA are found to interact with various proteins in hormone and stress signaling. The different biochemical and regulatory properties of PLDs and PA shed light on the mechanisms for the functional diversity of PLDs in plant defense signaling and response.

Phospholipase D as a Potential Modulator of Metabolic Syndrome: Impact of Functional Foods

Antioxid Redox Signal 2021 Jan 20;34(3):252-278.PMID:32586106DOI:10.1089/ars.2020.8081.

Significance: Cardiometabolic disorders (CMD) are composed of a plethora of metabolic dysfunctions such as dyslipidemia, nonalcoholic fatty liver disease, insulin resistance, and hypertension. The development of these disorders is highly linked to inflammation and oxidative stress (OxS), two metabolic states closely related to physiological and pathological conditions. Given the drastically rising CMD prevalence, the discovery of new therapeutic targets/novel nutritional approaches is of utmost importance. Recent Advances: The tremendous progress in methods/technologies and animal modeling has allowed the clarification of Phospholipase D (PLD) critical roles in multiple cellular processes, whether directly or indirectly via phosphatidic acid, the lipid product mediating signaling functions. In view of its multiple features and implications in various diseases, PLD has emerged as a drug target. Critical Issues: Although insulin stimulates PLD activity and, in turn, PLD regulates insulin signaling, the impact of the two important PLD isoforms on the metabolic syndrome components remains vague. Therefore, after outlining PLD1/PLD2 characteristics and functions, their role in inflammation, OxS, and CMD has been analyzed and critically reported in the present exhaustive review. The influence of functional foods and nutrients in the regulation of PLD has also been examined. Future Directions: Available evidence supports the implication of PLD in CMD, but only few studies emphasize its mechanisms of action and specific regulation by nutraceutical compounds. Therefore, additional investigations are first needed to clarify the functional role of nutraceutics and, second, to elucidate whether targeting PLDs with food compounds represents an appropriate therapeutic strategy to treat CMD. Antioxid. Redox Signal. 34, 252-278.