Seiichi Ando

Nayoro City University, Nayoru, Hokkaidō, Japan

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Publications (26)34.57 Total impact

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    ABSTRACT: Three enzymes, carnosine dipeptidase I (EC 3.4.13.20, CNDP1), carnosine dipeptidase II (EC 3.4.13.18, CNDP2), and Xaa-methyl-His dipeptidase (or anserinase: EC 3.4.13.5, ANSN), are known to be capable of catalyzing the hydrolysis of carnosine (β-alanyl-l-histidine), in vertebrates. Here we report the purification and identification of two unidentified carnosine-cleaving enzymes from Japanese eel (Anguilla japonica). Two different dipeptidases were successfully purified to homogeneity from the skeletal muscle; one exhibited a broad substrate specificity, while the other a narrow specificity. N-terminal amino-acid sequencing, deglycosylation analysis, and genetic analysis clearly revealed that the former is a homodimer of glycosylated subunits, encoded by ANSN, and the latter is another homodimer of glycosylated subunits, encoded by CNDP1; that is, Xaa-methyl-His dipeptidase, and carnosine dipeptidase I respectively. This is the first report on the identification of carnosine dipeptidase I from a non-mammal. Database search revealed presence of a CNDP1 ortholog only from salmonid fishes, including Atlantic salmon and rainbow trout, but not from other ray-finned fish species, such as zebrafish, fugu, and medaka whose genomes have been completely sequenced. The mRNAs of CNDP1 and ANSN are strongly expressed in the liver of Japanese eel, compared with other tissues, while that of CNDP2 is widely distributed in all tissues tested.
    Biochimie 02/2012; 94(6):1281-90. · 3.14 Impact Factor
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    ABSTRACT: Complementary DNA clones encoding trypsins were isolated from pyloric ceca of cold-adapted fish, walleye pollock (Theragra chalcogramma) (WP-T) and Arctic cod (Boreogadus saida) (AC-T). The isolated full-length cDNA clones of WP-T and AC-T were 852 and 860 bp, respectively, and both cDNAs were contained an open reading frame of 726 bp. WP-T and AC-T seemed to be synthesized as preproenzyme that contains a signal peptide, an activation peptide, and a mature trypsin. Although the amino acid sequence identities of WP-T and AC-T to that of bovine trypsin were 64 and 63%, respectively, they completely conserved the structural features for catalytic function of trypsin. On the other hand, WP-T and AC-T possessed the four Met residues (Met135, Met145, Met175 and Met242) in their molecules and the deletion of Tyr151 and substitution of Pro152 for Gly in their autolysis loops when aligned with the sequences of tropical-zone fish and bovine trypsins. In addition, the contents of charged amino acid residues at the N-terminal regions (positions 20–50) of WP-T and AC-T were extremely higher than those of other fish and bovine trypsins. Moreover, one amino acid (Asn72) and two amino acids (Asn72 and Val75) coordinating with Ca2+ in bovine trypsin were exchanged for another amino acids in WP-T (His) and AC-T (His and Glu), respectively, and the contents of negative charged amino acids at their Ca2+-binding regions were lower than those of tropical-zone fish and bovine trypsins. Therefore, it was considered that these structural characteristics of WP-T and AC-T are closely related to their lower thermostability.
    European Food Research and Technology 12/2011; 233(6). · 1.39 Impact Factor
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    ABSTRACT: Imidazole-related dipeptides, such as carnosine and anserine, occur widely in skeletal muscles of jawed vertebrates. All of the known enzymes that catalyze the hydrolysis of these dipeptides belong to the M20A metallopeptidase subfamily; two secretory enzymes, serum carnosinase (EC 3.4.13.20) and anserinase (EC 3.4.13.5), and one non-secretory enzyme, cytosolic nonspecific dipeptidase (EC 3.4.13.18). Here we report the enzymatic characterization and molecular identification of an unidentified enzyme, which catalyzes the hydrolysis of these dipeptides, from the skeletal muscle of Far Eastern brook lamprey (Lethenteron reissneri). A 60-kDa subunit protein of the enzyme was purified to near homogeneity. We cloned two M20A genes from the skeletal muscle of Far Eastern brook lamprey; one was a secretory-type gene encoding for the 60-kD protein, and another was a non-secretory-type gene presumably encoding for cytosolic nonspecific dipeptidase. Our findings indicate that the purified enzyme is a N-glycosylated secretory M20A dipeptidase distributed specifically in the jawless vertebrate group, and may be derived from a common ancestor gene between serum carnosinase and anserinase. We propose that this dipeptidase is a novel secretory M20A enzyme and is classified as neither serum carnosinase nor anserinase.
    Peptides 04/2011; 32(4):648-55. · 2.52 Impact Factor
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    ABSTRACT: A cDNA clone encoding trypsin (AG-T) was isolated from the pyloric ceca of cold-adapted fish, arabesque greenling (Pleurogrammus azonus). The cDNA was composed of 892 bp with an open reading frame of 729 bp at nucleotide positions 25–753. Similar to all the known trypsin, the AG-T seemed to be synthesized as preproenzyme that contains a hydrophobic signal peptide, an activation pentapeptide and a mature trypsin of 222 amino acid residues. The AG-T also completely conserved the major structural features common to trypsin such as the catalytic triad (His57, Asp102, and Ser195), the obligatory Asp189 and twelve Cys residues. On the other hand, the AG-T possessed the deletion of Tyr151 and substitution of Pro152 for Gly in the autolysis loop when aligned with the sequence of tropical-zone fish and bovine trypsins. In addition, Val75 concerned in a combination with calcium ion was exchanged for Ala in the AG-T, and the content of positively charged amino acid residues at the calcium-binding site of the AG-T was three times higher than those of tropical-zone fish trypsins. Moreover, the ratio between charged and hydrophobic amino acid residues in the N-terminal region of the AG-T was also higher than those of temperate-zone fish and tropical-zone fish trypsins. Such structural properties of the AG-T would contribute to its low thermostability.
    European Food Research and Technology 01/2011; 232:381-388. · 1.39 Impact Factor
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    ABSTRACT: Apolipoproteins such as apolipoprotein (apo) A-I, apoA-IV, and apoE are lipid binding proteins synthesized mainly in the liver and the intestine and play an important role in the transfer of exogenous or endogenous lipids through the circulatory system. To investigate the mechanism of lipid transport in fish, we have isolated some novel genes of the apoA-I family, apoIA-I (apoA-I isoform) 1–11, from Japanese eel by PCR amplification. Some of the isolated genes of apoIA-I corresponded to 28kDa-1 cDNAs which had already been deposited into the database and encoded an apolipoprotein with molecular weight of 28 kDa in the LDL, whereas others seemed to be novel genes. The structural organization of all apoIA-Is consisted of four exons separated by three introns. ApoIA-I10 had a total length of 3232 bp, whereas other genes except for apoIA-I9 ranged from 1280 to 1441 bp. The sequences of apoIA-Is at the exon-intron junctions were mostly consistent with the consensus sequence (GT/AG) at exon-intron boundaries, whereas the sequences of 3′ splice acceptor in intron 1 of apoIA-I1-7 were (AC) but not (AG). The deduced amino acid sequences of all apoIA-Is contained a putative signal peptide and a propeptide of 17 and 5 amino acid residues, respectively. The mature proteins of apoIA-I1-3, 7, and 8 consisted of 237 amino acids, whereas those of apoIA-I4-6 consisted of 239 amino acids. The mature apoIA-I10 sequence showed 65% identity to amino acid sequence of apoIA-I11 which was associated with an apolipoprotein with molecular weight of 23 kDa in the VLDL. All these mature apoIA-I sequences satisfied the common structural features depicted for the exchangeable apolipoproteins such as apoA-I, apoA-IV, and apoE but apoIA-I11 lacked internal repeats 7, 8, and 9 when compared with other members of apoA-I family. Phylogenetic analysis showed that these novel apoIA-Is isolated from Japanese eel were much closer to apoA-I than apoA-IV and apoE, suggesting new members of the apoA-I family.
    Central European Journal of Biology 01/2011; 6(4):545-557. · 0.82 Impact Factor
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    ABSTRACT: Microcystin-LR, a cyclic heptapeptide, possesses the ability to inhibit the serine/threonine protein phosphatases PP1 and PP2A and, consequently, exhibits acute hepatocytotoxicity. Moreover, microcystin-LR induces cellular proliferation, resulting in tumor-promoting activity in hepatocytes. However, mechanisms that regulate the balance between cell death and proliferation after microcystin-LR treatment remain unclear. We examined the contribution of the transcription factor p53, as well as that of the hepatic uptake transporter for microcystin-LR, organic anion transporting polypeptide 1B3 (OATP1B3), to the cellular response to microcystin-LR exposure. We analyzed intracellular signaling responses to microcystin-LR by immunoblotting and real-time reverse-transcriptase polymerase chain reaction techniques using HEK293 human embryonic kidney cells stably transfected with SLCO1B3 (HEK293-OATP1B3). In addition, we analyzed the effect of attenuation of p53 function, via the p53 inhibitor pifithrin-alpha, and knockdown of p53 mRNA on the cytotoxicity of microcystin-LR using a 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. Microcystin-LR induced the phosphorylation and accumulation of p53 in HEK293-OATP1B3 cells, which resulted in up-regulation of the expression of p53 transcript targets, including p21 and seven in absentia homolog 1 (siah-1). In addition, microcystin-LR activated Akt signaling through the phosphorylation of Akt and glycogen synthase kinase 3beta. Although Akt signaling was activated, the accumulation of p53 led cells to apoptosis after treatment with 50 nM microcystin-LR for 24 hr. Both pharmacological inhibition of transcription factor activity of p53 by pifithrin-alpha and knockdown of p53 with small hairpin RNA attenuated the susceptibility of HEK293-OATP1B3 cells to microcystin-LR. This study demonstrates the importance of p53 in the regulation of cell fate after exposure to microcystin-LR. Our results suggest that, under conditions of p53 inactivation (including p53 mutation), chronic exposure to low doses of microcystin-LR may lead to cell proliferation through activation of Akt signaling. Results of this study may contribute to the development of chemoprevention and chemotherapeutic approaches to microcystin-LR poisoning.
    Environmental Health Perspectives 09/2010; 118(9):1292-8. · 7.26 Impact Factor
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    ABSTRACT: Pyloric ceca of starfish (Asterina pectinifera) were treated by supercritical carbon dioxide (SCO2) to remove the lipids. Then, phospholipase A2 (SC-PLA2) was extracted from the defatted powder and purified by a series of chromatographies including Sephacryl S-200, DEAE-cellulose, and Sephadex G-50. The purified SC-PLA2 was nearly homogeneous in SDS–PAGE and native-PAGE. The molecular weight of the SC-PLA2 was estimated as approximately 20,000. N-terminal amino acid sequence of the SC-PLA2 was SVYQF. Temperature and pH optimums of the SC-PLA2 were at around 50 °C and pH 9.0, respectively, and the enzyme activity was enhanced by sodium deoxycholate and 1 mM or higher concentration of Ca2+. The SC-PLA2 was stimulated most by adding Ca2+ followed by Mg2+ and Co2+, while it was strongly inhibited by adding Zn2+ and EDTA. The SC-PLA2 hydrolyzed phosphatidylcholine more effectively than phosphatidylethanolamine. These characteristics of the SC-PLA2 were the same as those of the starfish PLA2 (CM-PLA2) purified from the pyloric ceca defatted by chloroform–methanol (2:1, v/v) solution. Therefore, we concluded the SCO2 defatting process is useful as a substitute for organic solvent defatting process.
    Process Biochemistry. 05/2010;
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    ABSTRACT: Although apolipoprotein with molecular weight 14 kDa (apo-14 kDa) is associated with fish plasma high-density lipoproteins (HDLs), it remains to be determined whether apo-14 kDa is the homologue of mammalian apoA-II. We have obtained the full cDNA sequences that encode Japanese eel and rainbow trout apo-14 kDa. Homologues of Japanese eel apo-14 kDa sequence could be found in 14 fish species deposited in the DDBJ/EMBL/GenBank or TGI database. Fish apo-14 kDa lacks propeptide and contains more internal repeats than mammalian apoA-II. Nevertheless, phylogenetic analysis allowed fish apo-14 kDa to be the homologue of mammalian apoA-II. In addition, in silico cloning of the TGI, Ensembl, or NCBI database revealed apoA-IIs in dog, chicken, green anole lizard, and African clawed frog whose sequences had not so far been available, suggesting both apoA-I and apoA-II as fundamental constituents of vertebrate HDLs.
    Acta Biochimica et Biophysica Sinica 06/2009; 41(5):370-8. · 1.81 Impact Factor
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    ABSTRACT: The occurrence of Nα-acetylhistidine (NAH) in skeletal muscle of 91 species of freshwater fish and 9 species of other ectothermic vertebrates was investigated, with consideration of phylogenetic relationships. Of the 91 freshwater fish species examined, 13 species (7 cichlids, 5 anabantids, and 1 catfish) contained considerable amounts (> 1 µmol/g) of NAH in their skeletal muscles. The highest level (10.37 µmol/g) of NAH was found in the tissue of Betta splendens (Siamese fighting fish). Moreover, the NAH contents in the tissues of Trichogaster trichopterus (three spot gourami), Kryptopterus bicirrhis (glass catfish), Oreochromis niloticus (Nile tilapia), Mikrogeophagus ramirezi (ram cichlid) and Parachromis managuensis (Guapote tigre) were 3.17–6.16 µmol/g. The skeletal muscle of amphibians (5 species) and reptiles (4 species) had a low level (< 0.25 µmol/g) of NAH. The present findings clearly demonstrate NAH as the fifth imidazole-related compound, in addition to histidine, carnosine, anserine and ophidine (balenine), recognized as a major non-protein nitrogenous constituent in the skeletal muscle of vertebrate animals.
    Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology 03/2009; · 2.07 Impact Factor
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    Acta Biochimica Et Biophysica Sinica - ACTA BIOCHIM BIOPHYS SINICA. 01/2009; 41(5):370-378.
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    ABSTRACT: The lipid profile and fatty acid composition of muscle, liver, and plasma lipoprotein were examined in wild and cultured Japanese eel (Anguilla japonica). Although, the muscle lipid levels of wild eels (11.6%) were less than those of cultured eels (13.1%), both eels were classified as typical fatty fish. Compared with the liver lipid composition of cultured eels, triacylglycerol (TG) level of the liver decreased in wild eels, whilst phosphatidylcholine and phosphatidylethanolamine levels of the liver increased in wild eels, reflecting the difference of liver lipid levels in both eels. Wild eels contained more cholesteryl ester (CE) and less TG, phospholipid, and free cholesterol in their plasma than cultured eels. The ratio of TG to CE decreased, whilst that of CE to total cholesterol increased in the plasma of wild eels. Different fatty acid compositions were found between wild and cultured eels. Compared with the fatty acid compositions of cultured eels, wild eels contained high percentages of 18:2, 18:3, and 20:4 and low percentages of 22:6, 20:1, and 20:5 in their muscle, liver, and plasma lipoprotein. The lipid profile and fatty acid composition seemed to be useful criteria for distinguishing between wild and cultured eels.
    Food Chemistry. 01/2009;
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    Hideki Kishimura, Seiichi Ando
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    ABSTRACT: Site-directed mutagenesis study of phospholipase A2 (PLA2) from the pyloric ceca of starfish Asterina pectinifera was used to probe the relationship between polar-group specificity and structure of the pancreatic loop region. The sequence of the cDNA encoding the starfish PLA2 was exchanged by the oligonucleotide-directed dual amber-long and accurate polymerase chain reaction method to insert Lys residue between Cys-62 and Gly-63. The modified cDNA was inserted into the expression plasmid pET-16b, and PLA2 mutant was expressed in Escherichia coli Origami™ B (DE3) by induction with isopropyl-beta-d(−)-thiogalactopyranoside. The starfish PLA2 mutant showed essentially the same properties as the starfish native PLA2 with respect to substrate positional specificity, optimum pH, optimum temperature, Ca2+ requirement, and sodium deoxycholate requirement. However, the specific activity of the starfish PLA2 mutant for egg yolk PC (950 U/mg) was extremely lower than that of native PLA2 (119,000 U/mg), but close to that of porcine pancreatic PLA2 (4300 U/mg). Moreover, the ratio of specific activity of the PLA2 mutant for phosphatidylcholine to phosphatidylethanolamine (98 times) was highly lower than that of native PLA2 (2650 times), but similar to that of porcine pancreatic PLA2 (25 times). Therefore, it was suggested that the charge and structure of pancreatic loop region of the starfish PLA2 might carry out important role on polar-group specificity.
    01/2007;
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    ABSTRACT: Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii), TR-J, and elkhorn sculpin (Alcichthys alcicornis), TR-E, were purified by gel filtration on Sephacryl S-200 and Sephadex G-50. The molecular weights of TR-J and TR-E were estimated to be 24,000 Da by sodium dodecyl sulfate–polyacrylamide gel electrophoresis. TR-J and TR-E revealed optimum temperatures of 60 and 50 °C, respectively, and showed the same optimum pH (pH 8.0) for hydrolysis of Nα-p-tosyl-l-arginine methyl ester. TR-J and TR-E were unstable at above 50 and 40 °C, respectively, and were more stable at alkaline pH than at acidic pH. Thermal stabilities of TR-J and TR-E were highly calcium dependent. These purified trypsin enzymes were inhibited by serine protease inhibitors, such as TLCK and soybean trypsin inhibitor. The N-terminal amino acid sequences of TR-J and TR-E were also investigated. The N-terminal amino acid sequences of TR-J, IVGGYECKPYSQPHQVSLNS, and TR-E, IVGGYECTPHSQAHQVSLNS, were found, and these sequences showed highly homology to other fish trypsins.
    Food Chemistry. 01/2007;
  • Takashi Maoka, Seiichi Ando
    Fisheries Science 01/2007; 73(4):967-968. · 0.90 Impact Factor
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    ABSTRACT: Trypsin was purified from the pyloric ceca of spotted mackerel (Scomber australasicus) by gel filtration on Sephacryl S-200 and Sephadex G-50. The purification and yield were 20-fold and 81%, respectively, as compared to those in the starting crude extract. Final enzyme preparation was nearly homogeneous in sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) and the molecular weight of the enzyme was estimated to be 24,000 Da by SDS–PAGE. The trypsin was stable at pH 5–11 for 30 min at 30C, and its maximal activity against Nα-p-tosyl-L-arginine methyl ester was pH 8.0. Trypsin was heat-stable up to about 50C for 15 min at pH 8.0. Optimum temperature of the trypsin enzyme was 60C. The enzyme was stabilized by calcium ion. The purified trypsin was strongly inhibited by serine protease inhibitors such as N-p-tosyl-L-lysine chloromethyl ketone and soybean trypsin inhibitor, suggesting that it is a trypsin-like serine protease. N-Terminal amino acid sequence of spotted mackerel trypsin was IVGGYECTAHSQPHQVSLNS.
    Journal of Food Biochemistry 07/2006; 30(4):466 - 477. · 0.76 Impact Factor
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    ABSTRACT: Carboxypeptidase B was purified from the pyloric ceca of the starfish, Asterina pectinifera. The final enzyme preparation was nearly homogeneous in sodium dodecyl sulfate–polyacrylamide gel electrophoresis and its molecular weight was estimated as approximately 34,000. The value of the specificity constant (kcat/Km) for hydrolysis of benzoyl-glycyl-l-arginine by the purified enzyme was 1.72 × 105 M−1 s−1. The optimal pH and the optimal temperature of the enzyme were pH 7.5 and 55 °C, respectively. The enzyme was unstable above 50 °C and below pH 5.0. The enzyme was activated by Co2+, and inhibited by EDTA. The N-terminal amino acid sequence of the enzyme was determined as ATFDYNKYHSYQEIMDWVTN.
    Food Chemistry. 01/2006;
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    ABSTRACT: Trypsins from the pyloric ceca of two fish species, yellow tail (Seriola quinqueradiata) and brown hakeling (Physiculus japonicus) were purified by a series of chromatographic separations. Purity increased 62- and 106-fold with approximately 55 and 10% yield for yellow tail trypsin and brown hakeling trypsin, respectively. Final enzyme preparations were homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and the molecular weights of both enzymes were estimated to be 24 kDa by SDS-PAGE. Yellow tail and brown hakeling trypsins had maximal activity at pH 8.0 for hydrolysis of Nα-p-tosyl-L-arginine methyl ester hydrochloride and was unstable at acidic pH. The optimum temperatures for yellow tail and brown hakeling trypsins were 60 and 50C, respectively. Yellow tail trypsin was stable up to 50C, whereas brown hakeling was stable up to 40C. Both trypsins were stabilized by calcium ions. The activities of both trypsins were strongly inhibited by soybean trypsin inhibitor and N -p-tosyl-L-lysine chloromethyl ketone hydrochloride, and were partially inhibited by ethylenediaminetetraacetic acid. The N-terminal amino acid sequences of yellow tail trypsin and brown hakeling trypsin were determined as IVGGYECTPYSQPHQVSLNS and IVGGYECPKHSQPHQVSLNS, respectively.
    Journal of Food Biochemistry 01/2006; · 0.76 Impact Factor
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    Shoji Yamada, Yoshito Tanaka, Seiichi Ando
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    ABSTRACT: Anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5) is a dipeptidase that mainly catalyzes the hydrolysis of Nalpha-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.
    FEBS Journal 01/2006; 272(23):6001-13. · 4.25 Impact Factor
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    ABSTRACT: A truncated apolipoprotein (apo) A-I with a molecular weight (M(r)) of 26 kDa was first isolated from the plasma high density lipoproteins of an atypical Japanese eel (Anguilla japonica). Interestingly, this eel contained a very small amount of intact apoA-I (M(r)28 kDa) in the plasma, although serine protease inhibitors were present throughout the plasma preparation. The N-terminal sequence of 20 amino acids in truncated apoA-I was completely identical with that of intact apoA-I. Another apolipoprotein with M(r)28 kDa, whose N-terminal amino acid sequence differed from apoA-I, was also found in high density lipoprotein and low density lipoprotein. The apolipoprotein profiles of Japanese eel plasma appear to be complicated.
    Bioscience Biotechnology and Biochemistry 12/2005; 69(11):2258-62. · 1.27 Impact Factor
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    ABSTRACT: We investigated whether habitual exercise (HE) modulates levels of oxidative DNA damage and responsiveness to oxidative stress induced by renal carcinogen Fe-nitrilotriacetic acid (Fe-NTA). During a ten week protocol, two groups of rats either remained sedentary or underwent swimming for 15--60 min per day, 5 days per week, with or without a weight equivalent to 5% of their body weight. Then we injected Fe-NTA and sacrificed the rats 1 h after the injection. We determined the activity of superoxide dismutase (SOD) in diaphragm and kidney, evaluated levels of 8-hydroxydeoxyguanosine (8OHdG), catalase, and glutathione peroxidase, and assayed OGG1 protein levels in kidney. SOD activity in the diaphragm and kidney was increased in HE rats. By itself, HE had no effect on the level of 8OHdG, but it did significantly suppress induction of 8OHdG by Fe-NTA, and the amount of suppression correlated with intensity of exercise. These results suggest that HE induces resistance to oxidative stress and, at least at the initiation stage, inhibits carcinogenesis.
    Free Radical Research 10/2005; 39(9):905-11. · 3.28 Impact Factor

Publication Stats

172 Citations
34.57 Total Impact Points

Institutions

  • 2011–2012
    • Nayoro City University
      • Department of Nutritional Sciences
      Nayoru, Hokkaidō, Japan
  • 1992–2009
    • Kagoshima University
      • • United Graduate School of Agricultural Sciences
      • • Faculty of Fisheries
      Kagosima, Kagoshima, Japan
  • 2007
    • Prince of Songkla University
      • Department of Food Technology
      Songkhla, Changwat Songkhla, Thailand