Endocannabinoids and diacylglycerol kinase activity

Gantayet, Arpita; Jegatheswaran, Januvi; Jayakumaran, Gowtham; Topham, Matthew K.; Epand, Richard M.

doi:10.1016/j.bbamem.2010.12.022

Cited by 7 publications

(5 citation statements)

References 21 publications

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“…3 and Table 1). This value is almost the same as that of a previous report by Gantayet et al (6.4% relative to DGK activity) [31].On the other hand, its 1-MGK activity was negligible (0.0 ± 0.0% DGK activity) (Fig. 3 and Table 1).…”

Section: -Mgk and 2-mgk Activities Of Type III Dgk ()supporting

confidence: 90%

“…30 years ago, Kanohet al demonstrated that purified DGKhad high 2-MGK activity (10-20% compared to DGK activity), whereas its 1-MGK activity was less than 4% [30]. DGKwas also reported to have 2-MGK activity (6.4% of DGK activity) by Gantayetet al [31]. In the present study, DGK and  exhibited approximately 12 and 8% 2-MGK activities compared to their DGK activities (Figs.…”

Section: Discussionsupporting

confidence: 58%

“…30 years ago, Kanohet al purified DGKfrom porcine liver and demonstrated that the enzyme had10-20% 2-monoacylglycerol (MG) kinase (MGK) activitycompared withits DGK activity [30]. However, its 1-MGK activity was less than 4% relative toits DGK activity.Gantayetet al reported that DGK also exhibited6.4% 2-MGK activity compared withits DGK activity [31]. However, because a comprehensive analysis has not been done,the MGK activities of the other isozymes are presently unknown.…”

Section: Introductionmentioning

confidence: 99%

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Distinct 1-monoacylglycerol and 2-monoacylglycerol kinase activities of diacylglycerol kinase isozymes

Satō

Murakami

Yamaki

et al. 2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Diacylglycerol kinase (DGK) consists of ten isozymes and is involved in a wide variety of patho-physiological events. However, the enzymological properties of DGKs have not been fully understood. In this study, we performed a comprehensive analysis on the 1-monoacylglycerol kinase (MGK) and 2-MGK activities of ten DGK isozymes. We revealed that type I (α, β and γ), type II (δ, η and κ) and type III (ε) DGKs have 7.9-19.2% 2-MGK activity compared to their DGK activities, whereas their 1-MGK activities were <3.0%. Both the 1-MGK and 2-MGK activities of the type IV DGKs (ζ and ι) were <1% relative to their DGK activities. Intriguingly, type V DGKθ has approximately 6% 1-MGK activity and <2% 2-MGK activity compared to its DGK activity. Purified DGKθ exhibited the same results, indicating that its 1-MGK activity is intrinsic. Therefore, DGK isozymes are categorized into three types with respect to their 1-MGK and 2-MGK activities: those having (1) 2-MGK activity relatively stronger than their 1-MGK activity (types I-III), (2) only negligible 1-MGK and 2-MGK activities (type IV), and (3) 1-MGK activity stronger than its 2-MGK activity (type V). The 1-MGK activity of DGKθ and the 2-MGK activity of DGKα were stronger than those of the acylglycerol kinase reported as 1-MGK and 2-MGK to date. The presence or absence of 1-MGK and 2-MGK activities may be essential to the patho-physiological functions of each DGK isozyme.

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Section: -Mgk and 2-mgk Activities Of Type III Dgk ()supporting

confidence: 90%

Section: Discussionsupporting

confidence: 58%

Section: Introductionmentioning

confidence: 99%

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Distinct 1-monoacylglycerol and 2-monoacylglycerol kinase activities of diacylglycerol kinase isozymes

Satō

Murakami

Yamaki

et al. 2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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“…Out of the 12 proteins that were exclusively detected in the IC of the GASH/Sal, there are four proteins that are particularly noteworthy. Diacylglycerol kinase (DGKZ) catalyzes the phosphorylation of diacylglycerol to produce phosphatidic acid [ 56 ] and remove 1-stearoyl-2-arachidonoylglycerol, the precursor of the endocannabinoid 2-arachidonoyl glycerol (2-AG) [ 57 ]. Interestingly, 2-AG itself is known to have anticonvulsive effects through activation of cannabinoid receptors [ 58 ], and mutant mice deficient in this enzyme had significantly fewer motor seizures and epileptic events compared with wild-type mice [ 59 ].…”

Section: Discussionmentioning

confidence: 99%

Proteomic and Bioinformatic Tools to Identify Potential Hub Proteins in the Audiogenic Seizure-Prone Hamster GASH/Sal

et al. 2023

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The GASH/Sal (Genetic Audiogenic Seizure Hamster, Salamanca) is a model of audiogenic seizures with the epileptogenic focus localized in the inferior colliculus (IC). The sound-induced seizures exhibit a short latency (7–9 s), which implies innate protein disturbances in the IC as a basis for seizure susceptibility and generation. Here, we aim to study the protein profile in the GASH/Sal IC in comparison to controls. Protein samples from the IC were processed for enzymatic digestion and then analyzed by mass spectrometry in Data-Independent Acquisition mode. After identifying the proteins using the UniProt database, we selected those with differential expression and performed ontological analyses, as well as gene-protein interaction studies using bioinformatics tools. We identified 5254 proteins; among them, 184 were differentially expressed proteins (DEPs), with 126 upregulated and 58 downregulated proteins, and 10 of the DEPs directly related to epilepsy. Moreover, 12 and 7 proteins were uniquely found in the GASH/Sal or the control. The results indicated a protein profile alteration in the epileptogenic nucleus that might underlie the inborn occurring audiogenic seizures in the GASH/Sal model. In summary, this study supports the use of bioinformatics methods in proteomics to delve into the relationship between molecular-level protein mechanisms and the pathobiology of rodent models of audiogenic seizures.

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“…While an arachidonoyl group at the sn-2 position is critical to DGKε activity by itself, it is not sufficient to make a good lipid substrate for DGKε. The monoglyceride 2-arachidonoyl-glycerol is a poor substrate for DGKε, and can even act as an inhibitor at higher concentrations (Gantayet et al, 2011 ). DGKε has essentially no activity in phosphorylating 1-monoacylglycerol substrates, but it does have 8% of the activity of SAG in phosphorylating 2-monoacylglycerol.…”

Section: Interaction With Diacylglycerolmentioning

confidence: 99%

Diacylglycerol Kinase-ε: Properties and Biological Roles

Epand

Jennings

et al. 2016

Front. Cell Dev. Biol.

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In mammals there are at least 10 isoforms of diacylglycerol kinases (DGK). All catalyze the phosphorylation of diacylglycerol (DAG) to phosphatidic acid (PA). Among DGK isoforms, DGKε has several unique features. It is the only DGK isoform with specificity for a particular species of DAG, i.e., 1-stearoyl-2-arachidonoyl glycerol. The smallest of all known DGK isoforms, DGKε, is also the only DGK devoid of a regulatory domain. DGKε is the only DGK isoform that has a hydrophobic segment that is predicted to form a transmembrane helix. As the only membrane-bound, constitutively active DGK isoform with exquisite specificity for particular molecular species of DAG, the functional overlap between DGKε and other DGKs is predicted to be minimal. DGKε exhibits specificity for DAG containing the same acyl chains as those found in the lipid intermediates of the phosphatidylinositol-cycle. It has also been shown that DGKε affects the acyl chain composition of phosphatidylinositol in whole cells. It is thus likely that DGKε is responsible for catalyzing one step in the phosphatidylinositol-cycle. Steps of this cycle take place in both the plasma membrane and the endoplasmic reticulum membrane. DGKε is likely present in both of these membranes. DGKε is the only DGK isoform that is associated with a human disease. Indeed, recessive loss-of-function mutations in DGKε cause atypical hemolytic-uremic syndrome (aHUS). This condition is characterized by thrombosis in the small vessels of the kidney. It causes acute renal insufficiency in infancy and most patients develop end-stage renal failure before adulthood. Disease pathophysiology is poorly understood and there is no therapy. There are also data suggesting that DGKε may play a role in epilepsy and Huntington disease. Thus, DGKε has many unique molecular and biochemical properties when compared to all other DGK isoforms. DGKε homologs also contain a number of conserved sequence features that are distinctive characteristics of either the rodents or specific groups of primate homologs. How cells, tissues and organisms harness DGKε's catalytic prowess remains unclear. The discovery of DGKε's role in causing aHUS will hopefully boost efforts to unravel the mechanisms by which DGKε dysfunction causes disease.

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Endocannabinoids and diacylglycerol kinase activity

Cited by 7 publications

References 21 publications

Distinct 1-monoacylglycerol and 2-monoacylglycerol kinase activities of diacylglycerol kinase isozymes

Distinct 1-monoacylglycerol and 2-monoacylglycerol kinase activities of diacylglycerol kinase isozymes

Proteomic and Bioinformatic Tools to Identify Potential Hub Proteins in the Audiogenic Seizure-Prone Hamster GASH/Sal

Diacylglycerol Kinase-ε: Properties and Biological Roles

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