Purification and characterization of a novel imidazole dipeptide synthase from the muscle of the Japanese eel Anguilla japonica

Tsubone, Shiori; Yoshikawa, Norishige; Okada, Shigeru; Abe, Hiroki

doi:10.1016/j.cbpb.2006.12.002

Cited by 15 publications

(5 citation statements)

References 37 publications

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“…This is also confirmed in the present study as baseline carnosine content is significantly higher (ϳ20%) in the fast-twitch gastrocnemius than the more slow-twitch tibialis anterior and soleus. It could be hypothesized that fast-twitch muscles have higher carnosine content because they display a higher expression of transporters for ␤-alanine (2) or carnosine (3) or of carnosine synthase (15,32). If this were the case, then a larger effect of ␤-alanine supplementation would be expected in gastrocnemius than in the other muscles.…”

Section: Discussionmentioning

confidence: 99%

Carnosine loading and washout in human skeletal muscles

Baguet¹,

Reyngoudt²,

Pottier³

et al. 2009

Journal of Applied Physiology

160

166

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Carnosine (beta-alanyl-L-histidine) is present in high concentrations in human skeletal muscles. The oral ingestion of beta-alanine, the rate-limiting precursor in carnosine synthesis, has been shown to elevate the muscle carnosine content both in trained and untrained humans. Little human data exist about the dynamics of the muscle carnosine content, its metabolic regulation, and its dependence on muscle fiber type. The present study aimed to investigate in three skeletal muscle types the supplementation-induced amplitude of carnosine synthesis and its subsequent elimination on cessation of supplementation (washout). Fifteen untrained males participated in a placebo-controlled double-blind study. They were supplemented for 5-6 wk with either 4.8 g/day beta-alanine or placebo. Muscle carnosine was quantified in soleus, tibialis anterior, and medial head of the gastrocnemius by proton magnetic resonance spectroscopy (MRS), before and after supplementation and 3 and 9 wk into washout. The beta-alanine supplementation significantly increased the carnosine content in soleus by 39%, in tibialis by 27%, and in gastrocnemius by 23% and declined post-supplementation at a rate of 2-4%/wk. Average muscle carnosine remained increased compared with baseline at 3 wk of washout (only one-third of the supplementation-induced increase had disappeared) and returned to baseline values within 9 wk at group level. Following subdivision into high responders (+55%) and low responders (+15%), washout period was 15 and 6 wk, respectively. In the placebo group, carnosine remained relatively constant with variation coefficients of 9-15% over a 3-mo period. It can be concluded that carnosine is a stable compound in human skeletal muscle, confirming the absence of carnosinase in myocytes. The present study shows that washout periods for crossover designs in supplementation studies for muscle metabolites may sometimes require months rather than weeks.

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Section: Discussionmentioning

confidence: 99%

Carnosine loading and washout in human skeletal muscles

Baguet¹,

Reyngoudt²,

Pottier³

et al. 2009

Journal of Applied Physiology

160

166

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“…Recently, Tsubone et al (375) reported a potential novel imidazole dipeptide synthase, which they purified from eel muscle. They propose that this enzyme is different from the above-mentioned CS (EC 6.3.2.11), as the synthesis would not require ATP.…”

Section: A Carnosine Synthasementioning

confidence: 99%

Physiology and Pathophysiology of Carnosine

Boldyrev

Aldini

Derave

2013

Physiological Reviews

906

1,023

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Carnosine (β-alanyl-l-histidine) was discovered in 1900 as an abundant non-protein nitrogen-containing compound of meat. The dipeptide is not only found in skeletal muscle, but also in other excitable tissues. Most animals, except humans, also possess a methylated variant of carnosine, either anserine or ophidine/balenine, collectively called the histidine-containing dipeptides. This review aims to decipher the physiological roles of carnosine, based on its biochemical properties. The latter include pH-buffering, metal-ion chelation, and antioxidant capacity as well as the capacity to protect against formation of advanced glycation and lipoxidation end-products. For these reasons, the therapeutic potential of carnosine supplementation has been tested in numerous diseases in which ischemic or oxidative stress are involved. For several pathologies, such as diabetes and its complications, ocular disease, aging, and neurological disorders, promising preclinical and clinical results have been obtained. Also the pathophysiological relevance of serum carnosinase, the enzyme actively degrading carnosine into l-histidine and β-alanine, is discussed. The carnosine system has evolved as a pluripotent solution to a number of homeostatic challenges. l-Histidine, and more specifically its imidazole moiety, appears to be the prime bioactive component, whereas β-alanine is mainly regulating the synthesis of the dipeptide. This paper summarizes a century of scientific exploration on the (patho)physiological role of carnosine and related compounds. However, far more experiments in the fields of physiology and related disciplines (biology, pharmacology, genetics, molecular biology, etc.) are required to gain a full understanding of the function and applications of this intriguing molecule.

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“…Moreover, a recent study clarified a partial sequence of imidazole dipeptide synthase from the Japanese eel (Tsubone et al, 2007). That information is important for elucidating the biosynthetic pathway and the constituent enzymes that catalyze formation of carnosine.…”

Section: Discussionmentioning

confidence: 99%