Stimulation of fatty acid methylation in human red cell membranes by phospholipase A2 activation

Engelsen, S.; Zatz, Martin

doi:10.1016/0005-2760(82)90067-4

Cited by 12 publications

(4 citation statements)

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“…The natural occurrence of fatty acid methyl esters was reported only in few publications since, in most cases, fatty acid composition is analyzed after transmethylation of the organic extracts. However, there are confirmed reports in the literature of the isolation of fatty acid methyl esters from various human and animal cells and tissues (20)(21)(22)(23)(24)(25)(26)(27). Moreover, the biochemical pathway for methyl-ester formation was determined to be the carboxyl methylation of fatty acids by S-adenosylmethionine (24)(25)(26).…”

Section: Discussionmentioning

confidence: 80%

“…However, there are confirmed reports in the literature of the isolation of fatty acid methyl esters from various human and animal cells and tissues (20)(21)(22)(23)(24)(25)(26)(27). Moreover, the biochemical pathway for methyl-ester formation was determined to be the carboxyl methylation of fatty acids by S-adenosylmethionine (24)(25)(26). The formation of methyl esters of fatty acids was demonstrated in both cells and tissues, as well as membrane preparations incubated with a radioactive methyl group on methionine or S-adenosylmethionine.…”

Section: Discussionmentioning

confidence: 80%

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Identification of fatty acid methyl ester as naturally occurring transcriptional regulators of the members of the peroxisome proliferator‐activated receptor family

Schmidt

Vogel

Witherup

et al. 1996

Lipids

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The nuclear hormone receptors NUC-1 (PPAR delta) and PPAR alpha are members of the peroxisome proliferator-activated receptor (PPAR) family. The members of this receptor family are activated by agents that stimulate peroxisome proliferation, free fatty acids, prostaglandin 12 metabolites, and agents considered for the therapy of insulin-independent diabetes mellitus. To identify putative physiological agents that activate NUC-1, we tested the ability of acetone extracts of various rat tissues to activate the transcription of an MMTV-luciferase reporter gene, via a GR/NUC-1 hybrid receptor. GR/NUC-1 contains the ligand binding region of the NUC-1 receptor and the DNA binding domain of the glucocorticoid receptor. Using this assay, we found stimulatory activity in the pancreas, which upon purification and characterization was identified as methyl-palmitate, known to be enriched in pancreatic lipids. In addition, we determined that ethyl esters of palmitic and oleic acids are also potent activators of this receptor. Thus, fatty acid ester formation may control the cellular concentrations of fatty acids, and acyl-ester formation may play a role in the control of metabolic pathways and the activation of the PPAR.

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Section: Discussionmentioning

confidence: 80%

Section: Discussionmentioning

confidence: 80%

Identification of fatty acid methyl ester as naturally occurring transcriptional regulators of the members of the peroxisome proliferator‐activated receptor family

Schmidt

Vogel

Witherup

et al. 1996

Lipids

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“…Gabexate mesilate, chlorproma zine and p-bromophenacyl bromide inhib ited the enzyme activity, but the enzyme was not inhibited by cytidine diphosphate cho line at the concentration of 5 mmol/1. vous tissues [25], rat lung [26], mouse mam mary gland [27], human gallbladder epithe lium [28], human amniotic fluid [29], human polymorphonuclear leukocytes [30], rabbit inflammatory exudates [31], bovine thyroid [32], human red cells [33], rat testis [34], mouse sperm [35] and human rheumatoid fluids [36]. But, only a few reports have appeared on the purification and the proper ties of the enzymes, because the specific ac tivity and the content of the enzymes are very low.…”

Section: Properties Of Phospholipase A2mentioning

confidence: 99%

Purification and Some Properties of Membrane-Associated Phospholipase A(2) of Human Spleen

Nakaguchi¹,

Nishijima²,

Ogawa³

et al. 1986

Enzyme

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Membrane-associated phospholipase A(2) was purified to homogeneity from human spleen. The enzyme was solubilized from the particulate fraction by the addition of KBr, and purified by reverse-phase high-performance liquid chromatography. The estimated molecular weight of the enzyme was 14,000. The enzyme had a pH optimum around 9.5, required the presence of Ca^2+ for its activity, and hydrolyzed phosphatidylethanolamine more efficiently than phosphatidylcholine.

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“…; and (c) methylation of endogenous fatty acids by fatty acid carboxymethylases (FACM) in several tissues(8,(12)(13)(14)(15) (Figure 2B). Metabolic pathways for enzymatic methylation: Stepwise methylation of phosphatidylethanolamine (PE) to phosphatidylcholine (PC).…”

mentioning

confidence: 99%

S-Adenosyl-L-Methionine–Mediated Enzymatic Methylations in the Rat Retinal Membranes

Ps²,

Ve³

et al. 1994

Journal of Ocular Pharmacology and Therapeutics

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Enzymatic step-wise methylation of membrane phosphatidylethanolamine (PE) to phosphatidyl-N-methylethanolamine (PME) and then phosphatidyl-choline (PC) has been known to alter membrane properties and responsiveness of cells for activation of receptors by chemical transmitters. Conversion of PE to PME and PME to PC in the presence of S-adenosyl-Lmethionine (SAM) are catalyzed by two phospholipid N-methyltransferases, PMT I and PMT II, of which PMT I is the rate limiting enzyme. Retina is a good neuronal model for chemical transmission. However, retina was not studied for PMT activity. Therefore, we studied the rat retina for PMT I activity. Methylation of PE in the rat retinal sonicates was assayed using 3H-SAM (2 ßM) at 37°C in Tris-glycylglycine buffer (50 mM, pH 8.0) and methylated phospholipids were extracted with chloroform/methanol/HCl (2/1/0.02, v/v) and separated by thin layer chromatography on Silica Gel G plates. Chromatograms were developed in a solvent system of propionic acid/n-propyl alcohol/chloroform/water (2/2/1/1, v/v). This study gave the following results: (a) the total methylated phospholipids were (M + SE, N=5) 19.90 + 4.03 fmol/mg protein/min; (b) the major methylated phospholipid was PME (4.21 + 0.68 fmol/mg protein/min; (c) the fatty acid methylesters formed by fatty acid carboxymethylase (FACM) which accumulated in the solvent front amounted to 18.82 + 2.84 fmol/mg protein/min. Both PMT I and FACM were inhibited by S-adenosyl-L-homocysteine (150, 1.2 -5 ßM). These observations indicate that rat retina contains both PMTs and FACM.

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Stimulation of fatty acid methylation in human red cell membranes by phospholipase A2 activation

Cited by 12 publications

References 11 publications

Identification of fatty acid methyl ester as naturally occurring transcriptional regulators of the members of the peroxisome proliferator‐activated receptor family

Identification of fatty acid methyl ester as naturally occurring transcriptional regulators of the members of the peroxisome proliferator‐activated receptor family

Purification and Some Properties of Membrane-Associated Phospholipase A(2) of Human Spleen

S-Adenosyl-L-Methionine–Mediated Enzymatic Methylations in the Rat Retinal Membranes

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