Purification and sequence identification of anserinase

Yamada, Shoji; Tanaka, Yoshito; Ando, Seiichi

doi:10.1111/j.1742-4658.2005.04991.x

Cited by 17 publications

(6 citation statements)

References 27 publications

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“…Other predictive transcripts are indicative of an oxidative stress response in polluted environments, including an aldo-keto reductase and copper/zinc superoxide dismutase. The glutamate carboxypeptidase-like clone, which is associated with folate and homocysteine levels and is similar to anserinase (Yamada et al, 2005) also contributed to prediction, warranting further study on its function and regulation. The well documented biomarkers CYP1A, choriogenin and metallothionein were also strong predictors.…”

Section: Class Predictionmentioning

confidence: 97%

Hepatic transcriptomic profiles of European flounder (Platichthys flesus) from field sites and computational approaches to predict site from stress gene responses following exposure to model toxicants

et al. 2008

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Genomic technologies offer opportunities to gain a more global assessment of the health status of an organism through an understanding of the functional pathways that are responding to pollutant exposure. We have developed a 13,000 clone cDNA toxicogenomics microarray for Platichthys flesus, the European flounder (EU-GENIPOL Project). We aimed to distinguish the origins of flounder taken from six sampling sites of different pollution status in Northern Europe according to their hepatic gene expression profile using bioinformatic approaches. To determine which gene expression differences may relate to pollutant impact, we have completed complementary laboratory exposures of flounder to selected toxicants and determined the associated gene expression profiles. Using multivariate variable selection coupled with a statistical modelling procedure (GALGO) we can predict geographical site but the accuracy is limited to specific sites. The search space for a combination of genes that effectively predicts class membership is very large, however, by combining the signatures derived from acute laboratory exposure to individual chemicals to limit the search space, a very accurate model for classification of all the different environmental sites was achieved. The final model utilised the expression profiles of 16 clones and validation with a qPCR array comprising these genes correctly assigned the site of origin for fish obtained from three of the sites in an independent sampling. These data would imply that the gene expression fingerprints obtained with these arrays are primarily attributable to variations in chemical pollutant responses at the different sites, indicating their potential utility in environmental impact assessment.

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Section: Class Predictionmentioning

confidence: 97%

Hepatic transcriptomic profiles of European flounder (Platichthys flesus) from field sites and computational approaches to predict site from stress gene responses following exposure to model toxicants

et al. 2008

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“…It was named anserinase because it was first described in codling muscle (203), which uniquely contains anserine as HCD. Yamada et al (394) recently identified anserinase molecularly and proposed a phylogenetic tree with three separate families of carnosinase-like enzymes, being serum carnosinase like (CN1), cytosolic nonspecific dipeptidaselike (CN2), and anserinase-like. Other carnosinases have been described within the EC 3.4.13 family of dipeptidases, but their enzyme classification (such as EC 3.4.13.3) is now deleted because its activity is covered by CN1 and CN2.…”

Section: Other Dipeptidases With Carnosinase Activitymentioning

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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“…3h). These catabolic enzymes and their anserine/carnosine substrates have been associated with cognitive functioning, neurovascular activity and physiological homeostasis of histidine-containing dipeptides [45][46][47] . This further supports the specific activity of OXT in homeostatic regulation of tilapia's metabolic response to cold stress.…”

Section: Oxt Signaling Reduces Metabolism In Poikilotherms Under Extreme Cold Conditionsmentioning

confidence: 99%

Oxytocin Signaling Regulates the Homeostatic Response to Cold Stress in Poikilothermic Vertebrates

Segev

Krispin

Olthof

et al. 2021

Preprint

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When exposed to low temperature, homeothermic vertebrates maintain internal body temperature by activating thermogenesis and by altered metabolism, synchronized by neuroendocrine responses. Although such physiological responses also occur in poikilothermic vertebrates, the prevailing notion is that their reactions are passive. Here, we explored molecular hypothalamic and physiological responses to cold stress in the tropical poikilotherm Nile tilapia (Oreochromis niloticus). We show that cold exposed tilapia exhibit complex homeostatic responses, including increased hypothalamic oxytocin, plasma glucose and cortisol concomitant with reduced plasma lactate and metabolic rate. Pharmacological or genetic blockage of oxytocin signaling further affected metabolic rate in two cold-exposed poikilothermic models. This indicates that oxytocin, a known thermoregulator in homeotherms, actively regulates temperature-related homeostasis in poikilotherms. Overall, our findings show that the brain of poikilotherms actively responds to cold temperature by regulating metabolic physiology. Moreover, we identify oxytocin signaling as an adaptive and evolutionarily conserved metabolic regulator of temperature-related homeostasis.

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Purification and sequence identification of anserinase

Cited by 17 publications

References 27 publications

Hepatic transcriptomic profiles of European flounder (Platichthys flesus) from field sites and computational approaches to predict site from stress gene responses following exposure to model toxicants

Hepatic transcriptomic profiles of European flounder (Platichthys flesus) from field sites and computational approaches to predict site from stress gene responses following exposure to model toxicants

Physiology and Pathophysiology of Carnosine

Oxytocin Signaling Regulates the Homeostatic Response to Cold Stress in Poikilothermic Vertebrates

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