Pretreatment of starved rats with ornithine α-ketoglutarate: effects on hepatic mRNA levels and plasma concentrations of three liver-secreted proteins

Segaud, Frédéric; Lardeux, Bernard; Alexandre-Gouabau, Marie Cécile; Bleiberg-Daniel, Fanny; Nakib, Samir; Cynober, Luc; Moinard, Christophe

doi:10.1016/j.nut.2004.11.008

Cited by 2 publications

(1 citation statement)

References 25 publications

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“…Also, many studies on animals with induced muscle catabolism (Jeevanandam et al 1996 ; Le Boucher et al 1997 ; Ségaud et al 2005 ; Vaubourdolle et al 1988 , 1991 ) showed that OKG modulated protein metabolism by decreasing urea excretion, increasing protein synthesis in the liver and the intestine, and by inhibiting the degradation of myofibrils, reducing total proteolysis, and loss of glutamine from muscle tissue. In addition, OKG exerted a positive effect on the functioning of the intestinal mucosa and contributed to its recovery after surgery (Czernichow et al 1997 ; Dumas et al 1988 ; Raul et al 1995 ).…”

Section: Akg As a Complementary Factor In States Of Protein Deficiencmentioning

confidence: 99%

Alpha-Ketoglutarate as a Molecule with Pleiotropic Activity: Well-Known and Novel Possibilities of Therapeutic Use

Zdzisińska

Żurek

Kandefer‐Szerszeń

2016

Arch. Immunol. Ther. Exp.

167

133

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Alpha-ketoglutarate (AKG), an endogenous intermediary metabolite in the Krebs cycle, is a molecule involved in multiple metabolic and cellular pathways. It functions as an energy donor, a precursor in the amino acid biosynthesis, a signalling molecule, as well as a regulator of epigenetic processes and cellular signalling via protein binding. AKG is an obligatory co-substrate for 2-oxoglutarate-dependent dioxygenases, which catalyse hydroxylation reactions on various types of substrates. It regulates the activity of prolyl-4 hydroxylase, which controls the biosynthesis of collagen, a component of bone tissue. AKG also affects the functioning of prolyl hydroxylases, which, in turn, influences the function of the hypoxia-inducible factor, an important transcription factor in cancer development and progression. Additionally, it affects the functioning of enzymes that influence epigenetic modifications of chromatin: ten–eleven translocation hydroxylases involved in DNA demethylation and the Jumonji C domain containing lysine demethylases, which are the major histone demethylases. Thus, it regulates gene expression. The metabolic and extrametabolic function of AKG in cells and the organism open many different fields for therapeutic interventions for treatment of diseases. This review presents the results of studies conducted with the use of AKG in states of protein deficiency and oxidative stress conditions. It also discusses current knowledge about AKG as an immunomodulatory agent and a bone anabolic factor. Additionally, the regulatory role of AKG and its structural analogues in carcinogenesis as well as the results of studies of AKG as an anticancer agent are discussed.

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Section: Akg As a Complementary Factor In States Of Protein Deficiencmentioning

confidence: 99%

Alpha-Ketoglutarate as a Molecule with Pleiotropic Activity: Well-Known and Novel Possibilities of Therapeutic Use

Zdzisińska

Żurek

Kandefer‐Szerszeń

2016

Arch. Immunol. Ther. Exp.

167

133

View full text Add to dashboard Cite

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Effects of ornithine α-ketoglutarate on growth performance and gut microbiota in a chronic oxidative stress pig model induced byd-galactose

Wang

Yin

et al. 2020

Food Funct.

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Pretreatment of starved rats with ornithine α-ketoglutarate: effects on hepatic mRNA levels and plasma concentrations of three liver-secreted proteins

Cited by 2 publications

References 25 publications

Alpha-Ketoglutarate as a Molecule with Pleiotropic Activity: Well-Known and Novel Possibilities of Therapeutic Use

Alpha-Ketoglutarate as a Molecule with Pleiotropic Activity: Well-Known and Novel Possibilities of Therapeutic Use

Effects of ornithine α-ketoglutarate on growth performance and gut microbiota in a chronic oxidative stress pig model induced byd-galactose

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