Evidence for an essential role of long chain acyl-CoA synthetase in animal cell proliferation

Carnitine is a simple, vitamin-like compound that transports long-chain fatty acids into mitochondria. Despite its essential role in human nutrition and metabolism, carnitine engendered relatively little medical interest until the description in the 1970s of human disorders in which muscle or systemic levels of carnitine were markedly depressed and in which clinical improvement followed treatment with carnitine. Since then, carnitine has enjoyed a remarkable rise in popularity as an aid to everything from common muscle fatigue to treatment of specific inborn errors of metabolism. Nowhere has the popularity of carnitine been more evident than in the treatment of children taking valproic acid, which causes in some children a depression of free carnitine levels.

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Long-Chain acyl-CoA Synthetase LACS2 Contributes to Submergence Tolerance by Modulating Cuticle Permeability in Arabidopsis

Plants ◽

10.3390/plants9020262 ◽

2020 ◽

Vol 9 (2) ◽

pp. 262 ◽

Cited By ~ 1

Author(s):

Li-Juan Xie ◽

Wei-Juan Tan ◽

Yi-Cong Yang ◽

Yi-Fang Tan ◽

Ying Zhou ◽

...

Keyword(s):

Biological Processes ◽

Submergence Tolerance ◽

Ethylene Response ◽

Chain Acyl ◽

Surface Permeability ◽

And Function ◽

Wax Crystals ◽

Long Chain ◽

Arabidopsis Cells

In Arabidopsis thaliana, LONG-CHAIN ACYL-COA SYNTHETASEs (LACSs) catalyze the synthesis of long-chain acyl-CoAs and function in diverse biological processes. We have recently revealed that LACS2 is primarily involved in the production of polyunsaturated linolenoyl-CoA, essential for the activation of ethylene response transcription factors-mediated hypoxia signaling. Here, we further reported the dual role of LACS2 in the regulation of submergence tolerance by modulating cuticle permeability in Arabidopsis cells. LACS2-overexpressors (LACS2-OEs) showed improved tolerance to submergence, with higher accumulation of cuticular wax and cutin in their rosettes. In contrast, knockout of LACS2 in the lacs2-3 mutant resulted in hypersensitivity to submergence with reduced wax crystals and thinner cutin layer. By analyses of plant surface permeability, we observed that the hypoxic sensitivities in the LACS2-OEs and lacs2-3 mutant were physiologically correlated with chlorophyll leaching, water loss rates, ionic leakage, and gas exchange. Thus, our findings suggest the role of LACS2 in plant response to submergence by modulating cuticle permeability in plant cells.

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Role of long-chain acyl-coenzyme A synthetases in the regulation of arachidonic acid metabolism in interleukin 1β-stimulated rat fibroblasts

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids ◽

10.1016/j.bbalip.2013.09.015 ◽

2014 ◽

Vol 1841 (1) ◽

pp. 44-53 ◽

Cited By ~ 27

Author(s):

Hiroshi Kuwata ◽

Makiko Yoshimura ◽

Yuka Sasaki ◽

Emiko Yoda ◽

Yoshihito Nakatani ◽

...

Keyword(s):

Arachidonic Acid ◽

Acid Metabolism ◽

Coenzyme A ◽

Arachidonic Acid Metabolism ◽

Interleukin 1Β ◽

Chain Acyl ◽

Rat Fibroblasts ◽

Acyl Coenzyme A ◽

Long Chain

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2,6-Dimethylheptanoyl-CoA is a specific substrate for long-chain acyl-CoA dehydrogenase (LCAD): evidence for a major role of LCAD in branched-chain fatty acid oxidation

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism ◽

10.1016/s0005-2760(98)00053-8 ◽

1998 ◽

Vol 1393 (1) ◽

pp. 35-40 ◽

Cited By ~ 32

Author(s):

Ronald J.A. Wanders ◽

Simone Denis ◽

Jos P.N. Ruiter ◽

Lodewijk IJlst ◽

Georges Dacremont

Keyword(s):

Fatty Acid ◽

Fatty Acid Oxidation ◽

Chain Fatty Acid ◽

Acid Oxidation ◽

Specific Substrate ◽

Chain Acyl ◽

Branched Chain ◽

Long Chain

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Role of very-long-chain acyl-coenzyme A synthetase in X-linked adrenoleukodystrophy

Annals of Neurology ◽

10.1002/1531-8249(199909)46:3<409::aid-ana18>3.0.co;2-9 ◽

1999 ◽

Vol 46 (3) ◽

pp. 409-412 ◽

Cited By ~ 30

Author(s):

Steven J. Steinberg ◽

Stephan Kemp ◽

Lelita T. Braiterman ◽

Paul A. Watkins

Keyword(s):

Coenzyme A ◽

Chain Acyl ◽

Acyl Coenzyme A ◽

Long Chain

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The role of long-chain acyl-CoA in the damage of oxidative phosphorylation in heart mitochondria

FEBS Letters ◽

10.1016/0014-5793(89)80141-3 ◽

1989 ◽

Vol 243 (2) ◽

pp. 264-266 ◽

Cited By ~ 4

Author(s):

V. Borutait≐ ◽

V. Mildaz̆ien≐ ◽

L. Ivanovien≐ ◽

B. Kholodenko ◽

A. Toleikis ◽

...

Keyword(s):

Oxidative Phosphorylation ◽

Heart Mitochondria ◽

Chain Acyl ◽

Long Chain

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The Multiple Faces of MNT and Its Role as a MYC Modulator

Cancers ◽

10.3390/cancers13184682 ◽

2021 ◽

Vol 13 (18) ◽

pp. 4682

Author(s):

Judit Liaño-Pons ◽

Marie Arsenian-Henriksson ◽

Javier León

Keyword(s):

Cell Proliferation ◽

Transcriptional Repression ◽

Cell Biology ◽

Essential Role ◽

Present Knowledge ◽

Special Focus ◽

Cellular Functions ◽

Cellular Processes ◽

Tumor Cell Survival

MNT is a crucial modulator of MYC, controls several cellular functions, and is activated in most human cancers. It is the largest, most divergent, and most ubiquitously expressed protein of the MXD family. MNT was first described as a MYC antagonist and tumor suppressor. Indeed, 10% of human tumors present deletions of one MNT allele. However, some reports show that MNT functions in cooperation with MYC by maintaining cell proliferation, promoting tumor cell survival, and supporting MYC-driven tumorigenesis in cellular and animal models. Although MAX was originally considered MNT’s obligate partner, our recent findings demonstrate that MNT also works independently. MNT forms homodimers and interacts with proteins both outside and inside of the proximal MYC network. These complexes are involved in a wide array of cellular processes, from transcriptional repression via SIN3 to the modulation of metabolism through MLX as well as immunity and apoptosis via REL. In this review, we discuss the present knowledge of MNT with a special focus on its interactome, which sheds light on the complex and essential role of MNT in cell biology.

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