Effects of starvation and feeding on tissue Nα -acetylhistidine levels in Nile tilapia Oreochromis niloticus

Yamada, Shoji; Tanaka, Yoshito; Sameshima, Muneo; Furuichi, Masayuki

doi:10.1016/0300-9629(94)90130-9

Cited by 16 publications

(10 citation statements)

References 11 publications

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“…This is in accordance with our findings in Atlantic salmon muscle, as well as in lens tissue of this species. Both Ans and NAH are believed to keep His ‘trapped’ in the respective tissues and prevent this essential amino acid from being catabolized or used in protein synthesis (Yamada, Tanaka, Sameshima & Furuichi 1994; Baslow 1998).…”

Section: Discussionmentioning

confidence: 99%

Histidine nutrition and genotype affect cataract development in Atlantic salmon, Salmo salar L.

Breck¹,

Bjerkås

Campbell

et al. 2005

Journal of Fish Diseases

123

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The aim of this study was to investigate effects of dietary levels of histidine (His) and iron (Fe) on cataract development in two strains of Atlantic salmon monitored through parr-smolt transformation. Three experimental diets were fed: (i) a control diet (CD) with 110 mg kg )1 Fe and 11.7 g kg )1 His; (ii) CD supplemented with crystalline His to a level of 18 g kg )1 (HD); and (iii) HD with added iron up to 220 mg kg )1 (HID). A cross-over design, with two feeding periods was used. A 6-week freshwater (FW) period was followed by a 20-week period, of which the first three were in FW and the following 17 weeks in sea water (SW). Fish were sampled for weighing, cataract assessment and tissue analysis at five time points. Cataracts developed in all groups in SW, but scores were lower in those fed high His diets (P < 0.05). This effect was most pronounced when HD or HID was given in SW, but was also observed when these diets were given in FW only. Histidine supplementation had a positive effect on growth performance and feed conversion ratio (P < 0.05), whereas this did not occur when iron was added. Groups fed HD or HID had higher lens levels of His and N-acetyl histidine (NAH), the latter showing a marked increase post-smoltification (P < 0.05). The HD or HID groups also showed higher muscle concentrations of the His dipeptide anserine (P < 0.05). There was a strong genetic influence on cataract development in the CD groups (P < 0.001), not associated with tissue levels of His or NAH. The role of His and Hisrelated compounds in cataractogenesis is discussed in relation to tissue buffering, osmoregulation and antioxidation.

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Section: Discussionmentioning

confidence: 99%

Histidine nutrition and genotype affect cataract development in Atlantic salmon, Salmo salar L.

Breck¹,

Bjerkås

Campbell

et al. 2005

Journal of Fish Diseases

123

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“…NAH is also present in high concentration in the skeletal muscle of frogs (Tsunoo et al, 1972) and one fish species, the Nile tilapia (Yamada et al, 1992). It is found in the epithelial receptor cell layer of the trout inner ear (Drescher and Drescher, 1991), and very small amounts have been reported in the liver, spleen, kidney, and stomach of fish species (Yamada et al, 1994). In Nile tilapia, upon starvation, muscle NAH disappears, but NAN in brain and lens is spared.…”

Section: Comparative Analysis Of Naa and Nah Distribution In Organismmentioning

confidence: 99%

A Review of Phylogenetic and Metabolic Relationships Between the Acylamino Acids, N‐Acetyl‐l‐Aspartic Acid and N‐Acetyl‐l‐Histidine, in the Vertebrate Nervous System

Baslow

1997

Journal of Neurochemistry

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N-Acetyl-L-histidine (NAH) and N-acetyl-Laspartic acid (NAA) are major constituents of vertebrate brain and eye with distinct phylogenetic distributions. They are characterized by high tissue concentrations, high tissue/extracellularfluid gradients, and a continuous regulated efflux into the extracellular fluid. As a result of parallel investigations over the past three decades, evidence has accumulated that suggests that the metabolism of NAA in the CNS of both homeothermic and poikilothermic vertebrates and the metabolism of NAH in the CNS of poikilothermic vertebrates are related. Tissue distribution and concentrations are similar, as well as timing of appearance during embryological development and their synthetic and degradative biochemistry. Both amino acids appear to be involved in a rapid tissue-to-fluidspace cycling phenomenon across a membrane. Evidence accumulating for each amino acid suggests a dynamic and important role in the CNS and the eye of vertebrates. A genetic disease in humans, Canavan's disease, is associated with NAA aciduria and aspartoacylase deficiency with concomitant accumulation of NAA and a spongy degeneration of the brain. In this article, evidence linking NAA and NAH metabolism is reviewed, and the hypothesis that NAA and NAH complement each other and are metabolic analogues involved with membrane transport is developed. Their enzyme systems also appear to exhibit plasticity in relation to osmoregulatory forces on an evolutionary time scale, with an apparent interface at the fish-tetrapod boundary. Key Words: NAcetyl-L-aspartic acid-N-Acetyl-L-histidine-Phylogenetic distribution-Cycling phenomenon-EvolutionCanavan's disease-Osmoregulatory forces-Efflux. J. Neurochem. 68, 1335-1344 (1997).The vertebrate brain has been found to contain very high concentrations of two acetylated amino acids, Nacetyl-L-aspartic acid (NAA) and N-acetyl-L-histidine (NAH). NAA was first isolated in extracts of cat brain by Tallan et a!. (1956). Two years later, NAH was isolated as an unknown in an imidazole fraction (TM 1) in cold-blooded vertebrates by Correale (1958) and later identified as NAH from the IM~fraction of frog tissues by Anastasi et al. (1964). Baslow (1963Baslow ( , 1964 independently isolated an unknown imidazole compound from the brain of fish and frogs and named it neurosine. Later, neurosine was identified as NAH (Baslow, 1965). Kuroda and Ikoma (1966) independently isolated and identified NAH in frog heart. Since the identification of these acetylated amino acids in very high concentrations in the brain of vertebrates, they have been the subject of many investigations into their possible function in both cold-blooded (poikilothermic) and warm-blooded (homeothermic) vertebrates. The studies, for the most part, have treated these amino acids as separate entities, probably because high concentrations of NAH are only present in the brain of poikilothermic vertebrates and high concentrations of NAA are found primarily in the brain of homeothermic vertebrates. In only a single ...

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“…We could not detect the RT‐PCR products of the expected size for anserinase mRNA in any other tissues. According to our previous works [11,21], the enzymatic activity of anserinase was detected strongly in kidney, brain, liver and ocular fluid, and weakly in skeletal muscle and spleen of Nile tilapia. The mRNA expression in the brain and kidney obtained in this study are therefore consistent with the distribution of the enzyme activity.…”

Section: Resultsmentioning

confidence: 93%

“…Previously, we reported that this enzyme, purified from the brain of rainbow trout Oncorhynchus mykiss to apparent homogeneity, is a homodimeric protein with a subunit of 55 kDa [9]. It is commonly believed that anserinase is universally distributed in poikilothermic animals containing N α‐acetylhistidine in their tissues [5,6,9–11].…”

mentioning

confidence: 99%

Purification and sequence identification of anserinase

Yamada¹,

Tanaka²,

Ando³

2005

The FEBS Journal

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Anserinase (Xaa‐methyl‐His dipeptidase, EC 3.4.13.5) is a dipeptidase that mainly catalyzes the hydrolysis of Nα‐acetylhistidine in the brain, retina and vitreous body of all poikilothermic vertebrates. The gene encoding anserinase has not been previously identified. We report the molecular identification of anserinase, purified from brain of Nile tilapia Oreochromis niloticus. The determination of the N‐terminal sequence of the purified anserinase allowed the design of primers permitting the corresponding cDNA to be cloned by PCR. The anserinase cDNA has an ORF of 1485 nucleotides and encodes a signal peptide of 18 amino acids and a mature protein of 476 amino acids with a predicted molecular mass of 53.3 kDa. Sequence analysis showed that anserinase is a member of the M20A metallopeptidase subfamily in MEROPS peptidase database, to which ‘serum’ carnosinase (EC 3.4.13.20) and cytosolic nonspecific dipeptidase (EC 3.4.13.18, CNDP) belong. A cDNA encoding CNDP‐like protein was also isolated from tilapia brain. Whereas anserinase mRNA was detected only in brain, retina, kidney and skeletal muscle, CNDP‐like protein mRNA was detected in all tissues examined.

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Effects of starvation and feeding on tissue Nα -acetylhistidine levels in Nile tilapia Oreochromis niloticus

Cited by 16 publications

References 11 publications

Histidine nutrition and genotype affect cataract development in Atlantic salmon, Salmo salar L.

Histidine nutrition and genotype affect cataract development in Atlantic salmon, Salmo salar L.

A Review of Phylogenetic and Metabolic Relationships Between the Acylamino Acids, N‐Acetyl‐l‐Aspartic Acid and N‐Acetyl‐l‐Histidine, in the Vertebrate Nervous System

Purification and sequence identification of anserinase

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