ATP-independent Fatty Acyl-Coenzyme A Synthesis from Phospholipid

Yamashita, Atsushi; Kawagishi, Norikazu; Miyashita, Tomoyuki; Nagatsuka, Tomonari; Sugiura, Takayuki; Kume, Kazuhiko; Shimizu, Takao; Waku, Keizo

doi:10.1074/jbc.m101795200

Cited by 29 publications

(28 citation statements)

References 46 publications

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“…Assay of Acyl-CoA:Lysophospholipid Acyltransferases-Acyl-CoA:lysophospholipid acyltransferase activities were estimated from the incorporation of radiolabeled acyl-CoA into the corresponding phospholipid in the presence of lysophospholipid (11,15). Stocks of LPI (12 mM), LPA (11 mM), and acyl-CoA (1 mM) were in aqueous solution, and aliquots were added into assays directly.…”

Section: Methodsmentioning

confidence: 99%

“…The resulting membrane pellet was washed with the same buffer, and the final pellet was suspended in the same buffer and used for enzyme assays. The expression of mLPAAT in E. coli was confirmed by Western blotting using a monoclonal antibody against the penta-histidine epitope (Qiagen) (15).…”

Section: Effects Of Various Reagents On Lpiat Activity and Coa-dependmentioning

confidence: 99%

“…Fractions containing LPIAT activity, eluting at around 0.2 M potassium phosphate (see Fig. 2B, fractions [15][16][17][18][19][20], were pooled, diluted with 3 volumes of Buffer A, and applied to an Econo-Pac Q cartridge pre-equilibrated in Buffer A. The column was washed with Buffer A until the effluent absorbance neared base-line values and then eluted with Buffer A in which the NaCl concentration increased linearly from 0 to 500 mM.…”

Section: Solubilization Of Liver Microsomes By Chaps-mentioning

confidence: 99%

“…In each case, the treated fractions were assayed for LPIAT activity and for CoA-dependent transacylation activity toward [ 3 H]LPI. Expression of mLPAAT in Escherichia coli-mLPAAT tagged at the N terminus with His 6 was expressed under control of tac (trc-lac) promoter in JC201 E. coli cells that lack endogenous LPAAT activity (pls C mutant) (15,16,27). JC201 cells harboring pTrc/mLPAAT were cultured in LB medium at 30°C until the A 600 reached ϳ0.6 and then cultured for an additional 3 h with 1 mM isopropyl-␤-D-thiogalactopyranoside.…”

Section: Effects Of Various Reagents On Lpiat Activity and Coa-dependmentioning

confidence: 99%

“…To evaluate the model, we previously examined the detailed enzymology of recombinant acyltransferase (15). We used the mouse lysophosphatidic acid (LPA) acyltransferase (mLPAAT) (16), because LPAAT was the first to be cloned and is currently the only available acyltransferase active toward lysophospholipids, although this enzyme is involved in de novo synthesis of glycerolipids rather than fatty acid remodeling of phospholipids.…”

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Reverse Reaction of Lysophosphatidylinositol Acyltransferase

Yamashita

Watanabe

Sato

et al. 2003

Journal of Biological Chemistry

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CoA-dependent transacylation activity in microsomes catalyzes the transfer of fatty acid between phospholipids and lysophospholipids in the presence of CoA without the generation of free fatty acid. We examined the mechanism of the transacylation system using partially purified acyl-CoA:lysophosphatidylinositol (LPI) acyltransferase (LPIAT) from rat liver microsomes to test our hypothesis that both the reverse and forward reactions of acyl-CoA:lysophospholipid acyltransferases are involved in the CoA-dependent transacylation process. The purified LPIAT fraction exhibited ATP-independent acyl-CoA synthetic activity and CoA-dependent LPI generation from PI, suggesting that LPIAT could operate in reverse to form acyl-CoA and LPI. CoA-dependent acylation of LPI by the purified LPIAT fraction required PI as the acyl donor. In addition, the combination of purified LPIAT and recombinant lysophosphatidic acid acyltransferase could reconstitute CoA-dependent transacylation between PI and phosphatidic acid. These results suggest that the CoA-dependent transacylation system consists of the following: 1) acyl-CoA synthesis from phospholipid through the reverse action of acylCoA:lysophospholipid acyltransferases; and 2) transfer of fatty acyl moiety from the newly formed acyl-CoA to lysophospholipid through the forward action of acylCoA:lysophospholipid acyltransferases.The fatty acyl moieties of phospholipids are not static but instead are dynamically turned over. Acyltransferases and transacylases catalyze the acylation of lysophospholipids and are involved in the biosynthesis and fatty acid remodeling of phospholipids (1-4). A CoA-dependent transacylation system (or CoA-dependent transacylase) catalyzes the transfer of fatty acids from phospholipids to lysophospholipids in the presence of CoA without generation of free fatty acids (5-11). In rabbit liver microsomes, arachidonic acid (20:4n-6), linoleic acid (18: 2n-6), and stearic acid (18:0), esterified in phospholipids, are the main species transferred to lysophospholipids in the presence of CoA, indicating that this system shows some fatty acid specificity (11). Phosphatidylcholine (PC), 1 phosphatidylethanolamine (PE), and phosphatidylinositol (PI) have been shown to serve as donor phospholipids, PI being the preferred acyl donor (10, 11). Despite the importance of CoA-dependent transacylation system in fatty acid remodeling of phospholipids, the mechanism underlying the transacylation system is not fully understood yet. In fact, the identities of the enzymes responsible for CoA-dependent transacylation reactions have not been established. Although we and other investigators (5,6,11,(12)(13)(14) considered previously that acyl-CoA:lysophospholipid acyltransferases may be involved in CoA-dependent transacylation reactions, direct and conclusive evidence has not been obtained because of the lack of success in purification and cloning of membrane-bound lysophospholipid acyltransferases and transacylases, including the CoA-dependent transacylation system.Previously, we de...

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Section: Methodsmentioning

confidence: 99%

Section: Effects Of Various Reagents On Lpiat Activity and Coa-dependmentioning

confidence: 99%

Section: Solubilization Of Liver Microsomes By Chaps-mentioning

confidence: 99%

Section: Effects Of Various Reagents On Lpiat Activity and Coa-dependmentioning

confidence: 99%

mentioning

confidence: 99%

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Reverse Reaction of Lysophosphatidylinositol Acyltransferase

Yamashita

Watanabe

Sato

et al. 2003

Journal of Biological Chemistry

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Lysophosphatidic acid LPA₁ receptor close‐up

Avendaño‐Vázquez¹,

Cabrera-Wrooman²,

Colín-Santana³

et al. 2007

Signal Transduction

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Lysophosphatidic acid is a local hormone / autacoid / growth factor, which induces a plethora of actions in the majority of cells in our organism. These actions include, among many others, the following: cell migration, proliferation and surviving, induction of gene transcription, platelet aggregation, smooth muscle contraction, myelinization, neurotransmitter release, cytoskeletal reorganization during the stress fiber formation, establishment of focal adhesions, neurite retraction, and cell rounding. The actions of lysophosphatidic acid are mediated through a family of G protein coupled receptors that includes five receptor subtypes, i.e. LPA 1, -5 receptors. These receptors couple to different G proteins, mainly Gi, Gq and G12/13 and their signaling pathways, besides there is evidence that they can transactivate EGF receptors to mediate some of their actions. The LPA 1 receptor was the first subtype to be cloned for this lysophospholipid. It plays an important role in development, is expressed in many cells and tissues and has been the most extensively studied. The present review presents current knowledge on the structure, function and regulation of this receptor subtype, its possible involvement in pathological conditions and suggests certain areas in which current knowledge is insufficient and further research is required.

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1-Acylglycerol-3-phosphate O-acyltransferase

Springer Handbook of Enzymes

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ATP-independent Fatty Acyl-Coenzyme A Synthesis from Phospholipid

Cited by 29 publications

References 46 publications

Reverse Reaction of Lysophosphatidylinositol Acyltransferase

Reverse Reaction of Lysophosphatidylinositol Acyltransferase

Lysophosphatidic acid LPA₁ receptor close‐up

1-Acylglycerol-3-phosphate O-acyltransferase

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ATP-independent Fatty Acyl-Coenzyme A Synthesis from Phospholipid

Cited by 29 publications

References 46 publications

Reverse Reaction of Lysophosphatidylinositol Acyltransferase

Reverse Reaction of Lysophosphatidylinositol Acyltransferase

Lysophosphatidic acid LPA1 receptor close‐up

1-Acylglycerol-3-phosphate O-acyltransferase

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Lysophosphatidic acid LPA₁ receptor close‐up