Purification and properties of human serum carnosinase

Jackson, Mel C.; Kucera, Christine M.; Lenney, James F.

doi:10.1016/0009-8981(91)90073-l

Cited by 111 publications

(93 citation statements)

References 24 publications

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“…However, a possibility that l-carnosine improves the I/R-induced renal injury, at least in part, via its antioxidative activity cannot be ruled out, because oxidative stress is definitely involved in the pathogenesis of ischemic ARF (Chatterjee et al, 2000;Takaoka et al, 2002). l-Carnosine is decomposed to ␤-alanine and l-histidine by a carnosine-degrading enzyme, carnosinase, which is present in serum and several tissues (Lenney et al, 1985;Kunze et al, 1986;Jackson et al, 1991;Nagai et al, 2003). In rat brain, two types of carnosine-degrading enzymes are present: one enzyme is carnosinase, which preferentially hydrolyzes carnosine, and the other enzyme hydrolyzes ␤-alanyl-l-arginine considerably faster than carnosine, both of which do not degrade acetyl-l-carnosine (Kunze et al, 1986).…”

Section: Discussionmentioning

confidence: 99%

“…l-Carnosine is known to be hydrolyzed by a carnosinedegrading enzyme, carnosinase, which is present in several tissues and serum of humans or animals (Lenney et al, 1985;Kunze et al, 1986;Jackson et al, 1991;Nagai et al, 2003). These findings raise a possibility that enzymatic hydrolysis of exogenous l-carnosine by carnosinase may be involved in l-carnosine actions on ischemic ARF.…”

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confidence: 99%

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Renoprotective Effects of l-Carnosine on Ischemia/Reperfusion-Induced Renal Injury in Rats

Kurata¹,

Fujii²,

Tsutsui³

et al. 2006

J Pharmacol Exp Ther

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We examined the renoprotective effects of l-carnosine (␤-alanyl-l-histidine) on ischemia/reperfusion (I/R)-induced acute renal failure (ARF) in rats. Ischemic ARF was induced by occlusion of the left renal artery and vein for 45 min followed by reperfusion, 2 weeks after contralateral nephrectomy. In vehicle (0.9% saline)-treated rats, renal sympathetic nerve activity (RSNA) was significantly augmented during the renal ischemia, and renal function was markedly decreased at 24 h after reperfusion. Intracerebroventricular injection of l-carnosine (1.5 and 5 pmol/rat) to ischemic ARF rats dose-dependently suppressed the augmented RSNA during ischemia and the renal injury at 24 h after reperfusion. N-␣-Acetyl-l-carnosine [N-acetyl-␤-alanyl-l-histidine; 5 pmol/rat intracerebroventricular (i.c.v.)], which is resistant to enzymatic hydrolysis by carnosinase, did not affect the renal injury, and l-histidine (5 pmol/rat i.c.v.), a metabolite cleaved from l-carnosine by carnosinase, ameliorated the I/R-induced renal injury. Furthermore, a selective histamine H 3 receptor antagonist, thioperamide (30 nmol/rat i.c.v.) eliminated the preventing effects by l-carnosine (15 nmol/rat intravenously) on ischemic ARF. In contrast, a selective H 3 receptor agonist, R-␣-methylhistamine (5 pmol/rat i.c.v.), prevented the I/R-induced renal injury as well as l-carnosine (5 pmol/rat) did. These results indicate that l-carnosine prevents the development of I/R-induced renal injury, and the effect is accompanied by suppressing the enhanced RSNA during ischemia. In addition, the present findings suggest that the renoprotective effect of l-carnosine on ischemic ARF is induced by its conversion to l-histidine and l-histamine and is mediated through the activation of histamine H 3 receptors in the central nervous system.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Renoprotective Effects of l-Carnosine on Ischemia/Reperfusion-Induced Renal Injury in Rats

Kurata¹,

Fujii²,

Tsutsui³

et al. 2006

J Pharmacol Exp Ther

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“…At this point, it should also be noted that it is difficult to extrapolate from animal experiments on carnosine efficacy to humans, since many non-primate mammals (e.g. rat, mouse, rabbit and guinea pig) appear to possess little or no serum carnosinase activity (Jackson et al 1991). In addition to serum carnosinase, the cytosolic isoform of carnosinase (CN2, EC 3.4.13.3) should not be underestimated with regard to final bioavailability of carnosine in the tissue that is targeted [for a review see (Pegova et al 2000)].…”

Section: Carnosinase Activitymentioning

confidence: 99%

Carnosine and cancer: a perspective

Gaunitz

Hipkiss

2012

Amino Acids

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The application of carnosine in medicine has been discussed since several years, but many claims of therapeutic effects have not been substantiated by rigorous experimental examination. In the present perspective, a possible use of carnosine as an anti-neoplastic therapeutic, especially for the treatment of malignant brain tumours such as glioblastoma is discussed. Possible mechanisms by which carnosine may perform its anti-tumourigenic effects are outlined and its expected bioavailability and possible negative and positive side effects are considered. Finally, alternative strategies are examined such as treatment with other dipeptides or b-alanine.

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“…The latter findings have been confirmed and extended in several other animal models of metabolic diseases (3,23,25). Whether the protective effects of carnosine ingestion in rodents can be translated to humans is not known, because rodents, unlike humans, have no carnosinase in their plasma (18). However, it can be expected that the normal dietary intake of carnosine in humans is more protective in people with low carnosinase activity.…”

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confidence: 68%

Aerobic and resistance training do not influence plasma carnosinase content or activity in type 2 diabetes

Stegen

Sigal

Kenny

et al. 2015

American Journal of Physiology-Endocrinology and Metabolism

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A particular allele of the carnosinase gene (CNDP1) is associated with reduced plasma carnosinase activity and reduced risk for nephropathy in diabetic patients. On the one hand, animal and human data suggest that hyperglycemia increases plasma carnosinase activity. On the other hand, we recently reported lower carnosinase activity levels in elite athletes involved in high-intensity exercise compared with untrained controls. Therefore, this study investigates whether exercise training and the consequent reduction in hyperglycemia can suppress carnosinase activity and content in adults with type 2 diabetes. Plasma samples were taken from 243 males and females with type 2 diabetes (mean age = 54.3 yr, SD = 7.1) without major microvascular complications before and after a 6-mo exercise training program [4 groups: sedentary control ( n = 61), aerobic exercise ( n = 59), resistance exercise ( n = 63), and combined exercise training ( n = 60)]. Plasma carnosinase content and activity, hemoglobin (Hb) A1c, lipid profile, and blood pressure were measured. A 6-mo exercise training intervention, irrespective of training modality, did not decrease plasma carnosinase content or activity in type 2 diabetic patients. Plasma carnosinase content and activity showed a high interindividual but very low intraindividual variability over the 6-mo period. Age and sex, but not Hb A1c, were significantly related to the activity or content of this enzyme. It can be concluded that the beneficial effects of exercise training on the incidence of diabetic complications are probably not related to a lowering effect on plasma carnosinase content or activity.

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Purification and properties of human serum carnosinase

Cited by 111 publications

References 24 publications

Renoprotective Effects of l-Carnosine on Ischemia/Reperfusion-Induced Renal Injury in Rats

Renoprotective Effects of l-Carnosine on Ischemia/Reperfusion-Induced Renal Injury in Rats

Carnosine and cancer: a perspective

Aerobic and resistance training do not influence plasma carnosinase content or activity in type 2 diabetes

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