메뉴 건너뛰기




Volumn 35, Issue 1, 2011, Pages 94-104

An ancient molecule with novel function: Alanine aminotransferase as a lipopolysaccharide binding protein with bacteriocidal activity

Author keywords

Alanine aminotransaminase (ALT); Amphioxus; Attern recognition receptor; Branchiostoma; Lancelet

Indexed keywords

ALANINE AMINOTRANSFERASE; AMPHIALT; LIPOPOLYSACCHARIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 77957865464     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2010.08.014     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 0022589710 scopus 로고
    • Aminotransferase activity in the liver and white muscle of Mugil capito fed diets containing different levels of proteins and carbohydrates
    • Alexin M.N., Papoutsoglou E.P. Aminotransferase activity in the liver and white muscle of Mugil capito fed diets containing different levels of proteins and carbohydrates. Comp. Biochem. Physiol. 1986, 83:245-249.
    • (1986) Comp. Biochem. Physiol. , vol.83 , pp. 245-249
    • Alexin, M.N.1    Papoutsoglou, E.P.2
  • 2
    • 84987592447 scopus 로고
    • Pathophysiology of experimental Aeromonas hydrophila infection in goldfish, Carassius auratus (L.)
    • Brenden R.A., Huizinga H.W. Pathophysiology of experimental Aeromonas hydrophila infection in goldfish, Carassius auratus (L.). J. Fish Dis. 1986, 9:163-167.
    • (1986) J. Fish Dis. , vol.9 , pp. 163-167
    • Brenden, R.A.1    Huizinga, H.W.2
  • 3
    • 34547964678 scopus 로고    scopus 로고
    • Prevalence and etiology of elevated serum alanine aminotransferase level in an adult population in Taiwan
    • Chen C.H., Huang M.H., Yang J.C., Nien C.K., Yang C.C., Yueh Y.H. Prevalence and etiology of elevated serum alanine aminotransferase level in an adult population in Taiwan. J. Gastroenterol. Hepatol. 2007, 22:1482-1489.
    • (2007) J. Gastroenterol. Hepatol. , vol.22 , pp. 1482-1489
    • Chen, C.H.1    Huang, M.H.2    Yang, J.C.3    Nien, C.K.4    Yang, C.C.5    Yueh, Y.H.6
  • 4
    • 0037429229 scopus 로고    scopus 로고
    • The resistance to physical stresses by Penaeus monodon juveniles fed diets supplemented with astaxanthin
    • Chien Y.H., Pan C.H., Hunter B. The resistance to physical stresses by Penaeus monodon juveniles fed diets supplemented with astaxanthin. Aquaculture 2003, 216:177-191.
    • (2003) Aquaculture , vol.216 , pp. 177-191
    • Chien, Y.H.1    Pan, C.H.2    Hunter, B.3
  • 5
    • 0038805259 scopus 로고    scopus 로고
    • The prevalence and etiology of elevated aminotransferase levels in the United States
    • Clark J.M., Brancati F.L., Diehl A.M. The prevalence and etiology of elevated aminotransferase levels in the United States. Am. J. Gastroenterol. 2003, 98:960-967.
    • (2003) Am. J. Gastroenterol. , vol.98 , pp. 960-967
    • Clark, J.M.1    Brancati, F.L.2    Diehl, A.M.3
  • 6
    • 33845202244 scopus 로고    scopus 로고
    • Identification and expression of a novel class of glutathione-S-transferase from amphioxus (Branchiostoma belcheri) with implications to the origin of vertebrate liver
    • Fan C.X., Zhang S.C., Liu Z.H., Li L., Luan J., Saren G. Identification and expression of a novel class of glutathione-S-transferase from amphioxus (Branchiostoma belcheri) with implications to the origin of vertebrate liver. Int. J. Biochem. Cell Biol. 2007, 39:450-461.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 450-461
    • Fan, C.X.1    Zhang, S.C.2    Liu, Z.H.3    Li, L.4    Luan, J.5    Saren, G.6
  • 7
    • 0015578098 scopus 로고
    • The glucose-alanine cycle
    • Felig P. The glucose-alanine cycle. Metabolism 1973, 22:179-207.
    • (1973) Metabolism , vol.22 , pp. 179-207
    • Felig, P.1
  • 8
    • 0025690501 scopus 로고
    • Partial characterization of the alanine aminotransferase isoenzymes from human liver
    • Gubern G., Imperial S., Busquets M., Cortes A. Partial characterization of the alanine aminotransferase isoenzymes from human liver. Biochem. Soc. Trans. 1990, 18:1288-1289.
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 1288-1289
    • Gubern, G.1    Imperial, S.2    Busquets, M.3    Cortes, A.4
  • 9
    • 70350017864 scopus 로고    scopus 로고
    • Expression, mitogenic activity and regulation by growth hormone of insulin-like growth factor in Branchiostoma belcheri
    • Guo B., Zhang S.C., Wang S.H., Liang Y.J. Expression, mitogenic activity and regulation by growth hormone of insulin-like growth factor in Branchiostoma belcheri. Cell Tissue Res. 2009, 338:67-77.
    • (2009) Cell Tissue Res. , vol.338 , pp. 67-77
    • Guo, B.1    Zhang, S.C.2    Wang, S.H.3    Liang, Y.J.4
  • 10
    • 32444440123 scopus 로고
    • Zur Kenntnis der Leberentwicklung bei Amphioxus
    • Hammar J.A. Zur Kenntnis der Leberentwicklung bei Amphioxus. Anatomischier Anzeiger 1898, 14:602-606.
    • (1898) Anatomischier Anzeiger , vol.14 , pp. 602-606
    • Hammar, J.A.1
  • 12
    • 0037353576 scopus 로고    scopus 로고
    • Identification of photorespiratory glutamate:glyoxylate aminotransferase (GGAT) gene in Arabidopsis
    • Igarashi D., Miwa T., Seki M., Kobayashi M., Kato T., Tabata S., Shinozaki K., Ohsumi C. Identification of photorespiratory glutamate:glyoxylate aminotransferase (GGAT) gene in Arabidopsis. Plant J. 2002, 33:975-983.
    • (2002) Plant J. , vol.33 , pp. 975-983
    • Igarashi, D.1    Miwa, T.2    Seki, M.3    Kobayashi, M.4    Kato, T.5    Tabata, S.6    Shinozaki, K.7    Ohsumi, C.8
  • 13
    • 2342627291 scopus 로고    scopus 로고
    • Murine alanine aminotransferase: cDNA cloning, functional expression, and differential gene regulation in mouse fatty liver
    • Jadaho S.B., Yang R.Z., Lin Q., Hu H., Anania F.A., Shuldiner A.R., Gong D.W. Murine alanine aminotransferase: cDNA cloning, functional expression, and differential gene regulation in mouse fatty liver. Hepatology 2004, 39:1297-1302.
    • (2004) Hepatology , vol.39 , pp. 1297-1302
    • Jadaho, S.B.1    Yang, R.Z.2    Lin, Q.3    Hu, H.4    Anania, F.A.5    Shuldiner, A.R.6    Gong, D.W.7
  • 14
    • 0033561303 scopus 로고    scopus 로고
    • Special considerations in interpreting liver function tests
    • Johnston D.E. Special considerations in interpreting liver function tests. Am. Fam. Physician 1999, 59:2223-2230.
    • (1999) Am. Fam. Physician , vol.59 , pp. 2223-2230
    • Johnston, D.E.1
  • 15
    • 60649109600 scopus 로고    scopus 로고
    • Identification, expression and antibacterial activity of a tachylectin-related homolog in amphioxus Branchiostoma belcheri with implications for involvement of the digestive system in acute phase response
    • Ju L.Y., Zhang S.C., Liang Y.J., Sun X.M. Identification, expression and antibacterial activity of a tachylectin-related homolog in amphioxus Branchiostoma belcheri with implications for involvement of the digestive system in acute phase response. Fish Shellfish Immunol. 2009, 26:235-242.
    • (2009) Fish Shellfish Immunol. , vol.26 , pp. 235-242
    • Ju, L.Y.1    Zhang, S.C.2    Liang, Y.J.3    Sun, X.M.4
  • 16
    • 0036125618 scopus 로고    scopus 로고
    • Attenuation of bacterial lipopolysaccharide-induced hepatotoxicity by betaine or taurine in rats
    • Kim S.K., Kim Y.C. Attenuation of bacterial lipopolysaccharide-induced hepatotoxicity by betaine or taurine in rats. Food Chem. Toxicol. 2002, 40:545-549.
    • (2002) Food Chem. Toxicol. , vol.40 , pp. 545-549
    • Kim, S.K.1    Kim, Y.C.2
  • 17
    • 0023665902 scopus 로고
    • An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak M. An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 1987, 15:8125-8148.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 18
    • 44849088161 scopus 로고    scopus 로고
    • Vitellogenin functions as a multivalent pattern recognition receptor with an opsonic activity
    • Li Z.J., Zhang S.C., Liu Z.H. Vitellogenin functions as a multivalent pattern recognition receptor with an opsonic activity. PLoS ONE 2008, 3(4):e1940.
    • (2008) PLoS ONE , vol.3 , Issue.4
    • Li, Z.J.1    Zhang, S.C.2    Liu, Z.H.3
  • 19
    • 70349449588 scopus 로고    scopus 로고
    • Vitellogenin is a cidal factor capable of killing bacteria via interaction with lipopolysaccharide and lipoteichoic acid
    • Li Z.J., Zhang S.C., Zhang J., Liu M., Liu Z.H. Vitellogenin is a cidal factor capable of killing bacteria via interaction with lipopolysaccharide and lipoteichoic acid. Mol. Immunol. 2009, 46:3232-3239.
    • (2009) Mol. Immunol. , vol.46 , pp. 3232-3239
    • Li, Z.J.1    Zhang, S.C.2    Zhang, J.3    Liu, M.4    Liu, Z.H.5
  • 20
    • 68749112924 scopus 로고    scopus 로고
    • A kringle-containing protease with plasminogen-like activity in the basal chordate Branchiostoma belcheri
    • Liu M.Y., Zhang S.C. A kringle-containing protease with plasminogen-like activity in the basal chordate Branchiostoma belcheri. Biosci. Rep. 2009, 29:385-395.
    • (2009) Biosci. Rep. , vol.29 , pp. 385-395
    • Liu, M.Y.1    Zhang, S.C.2
  • 21
    • 0031970627 scopus 로고    scopus 로고
    • Study of serum alanine-aminotransferase levels in blood donors in Spain
    • Lozano M., Cid J., Bedini J.L., Mazzara R., Gimenez N., Mas E. Study of serum alanine-aminotransferase levels in blood donors in Spain. Haematologica 1998, 83:237-239.
    • (1998) Haematologica , vol.83 , pp. 237-239
    • Lozano, M.1    Cid, J.2    Bedini, J.L.3    Mazzara, R.4    Gimenez, N.5    Mas, E.6
  • 22
    • 33750810209 scopus 로고    scopus 로고
    • Alanine aminotransferase in amphioxus: presence, localization and up-regulation after acute lipopolysaccharide exposure
    • Lun L.M., Zhang S.C., Liang Y.J. Alanine aminotransferase in amphioxus: presence, localization and up-regulation after acute lipopolysaccharide exposure. J. Biochem. Mol. Biol. 2006, 39:511-515.
    • (2006) J. Biochem. Mol. Biol. , vol.39 , pp. 511-515
    • Lun, L.M.1    Zhang, S.C.2    Liang, Y.J.3
  • 23
    • 0029972176 scopus 로고    scopus 로고
    • New insights into the compartmentation of glutamate and glutamine in cultured rat brain astrocytes
    • McKenna M.C., Tildon J.T., Stevenson J.H., Huang X. New insights into the compartmentation of glutamate and glutamine in cultured rat brain astrocytes. Dev. Neurosci. 1996, 18:380-390.
    • (1996) Dev. Neurosci. , vol.18 , pp. 380-390
    • McKenna, M.C.1    Tildon, J.T.2    Stevenson, J.H.3    Huang, X.4
  • 24
    • 0014197538 scopus 로고
    • Alanine aminotransferase: purification and properties
    • Milton H., Saeir J., Jenkins W.T. Alanine aminotransferase: purification and properties. J. Biol. Chem. 1967, 242:91-100.
    • (1967) J. Biol. Chem. , vol.242 , pp. 91-100
    • Milton, H.1    Saeir, J.2    Jenkins, W.T.3
  • 25
    • 0028371265 scopus 로고
    • Hypoxically inducible barley alanine aminotransferase: cDNA cloning and expression analysis
    • Muench D.G., Good A.G. Hypoxically inducible barley alanine aminotransferase: cDNA cloning and expression analysis. Plant Mol. Biol. 1994, 24:417-427.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 417-427
    • Muench, D.G.1    Good, A.G.2
  • 26
    • 0018394049 scopus 로고
    • Subcellular distribution and some properties of alanine aminotransferase in striated muscles of the crayfish, trout, carp, frog, pigeon and rabbit
    • Ruscák M., Orlický J. Subcellular distribution and some properties of alanine aminotransferase in striated muscles of the crayfish, trout, carp, frog, pigeon and rabbit. Physiol. Bohemoslov. 1979, 28:209-216.
    • (1979) Physiol. Bohemoslov. , vol.28 , pp. 209-216
    • Ruscák, M.1    Orlický, J.2
  • 27
    • 3843142721 scopus 로고    scopus 로고
    • Novel Archaeal alanine:glyoxylate aminotransferase from Thermococcus litoralis
    • Sakuraba H., Kawakami R., Takahashi H., Ohshima T. Novel Archaeal alanine:glyoxylate aminotransferase from Thermococcus litoralis. J. Bacteriol. 2004, 186:5513-5518.
    • (2004) J. Bacteriol. , vol.186 , pp. 5513-5518
    • Sakuraba, H.1    Kawakami, R.2    Takahashi, H.3    Ohshima, T.4
  • 28
    • 0024366671 scopus 로고
    • A review of donor alanine aminotransferase testing: implications for the blood donor and practitioner
    • Saxena S., Korula J., Shulman I.A. A review of donor alanine aminotransferase testing: implications for the blood donor and practitioner. Arch. Pathol. Lab. Med. 1989, 113:767-771.
    • (1989) Arch. Pathol. Lab. Med. , vol.113 , pp. 767-771
    • Saxena, S.1    Korula, J.2    Shulman, I.A.3
  • 29
    • 0010431140 scopus 로고
    • Purification and properties of liver glutamic-alanine transaminase from normal and corticoid treated rats
    • Segal H.L., Beattle D.S., Hopper S. Purification and properties of liver glutamic-alanine transaminase from normal and corticoid treated rats. J. Biol. Chem. 1962, 237:1914-1920.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1914-1920
    • Segal, H.L.1    Beattle, D.S.2    Hopper, S.3
  • 30
    • 1342342997 scopus 로고    scopus 로고
    • Purification and properties of cytosolic alanine aminotransferase from the liver of two freshwater fish, Clarias batrachus and Labeo rohita
    • Srivastava A.S., Oohara I., Suzuki T., Shenouda S., Singh S.N., Chauhan D.P., Carrier E. Purification and properties of cytosolic alanine aminotransferase from the liver of two freshwater fish, Clarias batrachus and Labeo rohita. Comp. Biochem. Physiol. B 2004, 137:197-207.
    • (2004) Comp. Biochem. Physiol. B , vol.137 , pp. 197-207
    • Srivastava, A.S.1    Oohara, I.2    Suzuki, T.3    Shenouda, S.4    Singh, S.N.5    Chauhan, D.P.6    Carrier, E.7
  • 31
    • 53549107487 scopus 로고    scopus 로고
    • Chordate phylogeny and evolution: a not so simple three-taxon problem
    • Stach T. Chordate phylogeny and evolution: a not so simple three-taxon problem. J. Zool. 2008, 276:117-141.
    • (2008) J. Zool. , vol.276 , pp. 117-141
    • Stach, T.1
  • 32
    • 0022382351 scopus 로고
    • Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates
    • Takada Y., Noguchi T. Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates. Biochem. J. 1985, 231:157-163.
    • (1985) Biochem. J. , vol.231 , pp. 157-163
    • Takada, Y.1    Noguchi, T.2
  • 33
    • 0035999613 scopus 로고    scopus 로고
    • Comparison of liver enzymes in osmerid fishes: key differences between a glycerol accumulating species, rainbow smelt (Osmerus mordax), and a species that does not accumulate glycerol, capelin (Mallotus villosus)
    • Treberg J.R., Lewis J.M., Driedzic W.R. Comparison of liver enzymes in osmerid fishes: key differences between a glycerol accumulating species, rainbow smelt (Osmerus mordax), and a species that does not accumulate glycerol, capelin (Mallotus villosus). Comp. Biochem. Physiol. A. 2003, 132:433-438.
    • (2003) Comp. Biochem. Physiol. A. , vol.132 , pp. 433-438
    • Treberg, J.R.1    Lewis, J.M.2    Driedzic, W.R.3
  • 34
    • 70349509954 scopus 로고    scopus 로고
    • Up-regulation of C/EBP by thyroid hormones: a case demonstrating the vertebrate-like thyroid hormone signaling pathway in amphioxus
    • Wang S.H., Zhang S.C., Zhao B.S., Lun L.M. Up-regulation of C/EBP by thyroid hormones: a case demonstrating the vertebrate-like thyroid hormone signaling pathway in amphioxus. Mol. Cell Endocrinol. 2009, 313:57-63.
    • (2009) Mol. Cell Endocrinol. , vol.313 , pp. 57-63
    • Wang, S.H.1    Zhang, S.C.2    Zhao, B.S.3    Lun, L.M.4
  • 35
    • 0011169845 scopus 로고
    • Quantitative differences between the human red cell glutamate-pyruvate transaminase phenotypes
    • Welch S.C. Quantitative differences between the human red cell glutamate-pyruvate transaminase phenotypes. Hum. Hered. 1972, 22:190-197.
    • (1972) Hum. Hered. , vol.22 , pp. 190-197
    • Welch, S.C.1
  • 36
    • 0002740651 scopus 로고
    • The fine structure of the pharynx, cyrtopodocytes and digestive caecum of Amphioxus (Branchiostoma lanceolatum)
    • Welsch U. The fine structure of the pharynx, cyrtopodocytes and digestive caecum of Amphioxus (Branchiostoma lanceolatum). Symp. Zool. Soc. Lond. 1975, 36:17-41.
    • (1975) Symp. Zool. Soc. Lond. , vol.36 , pp. 17-41
    • Welsch, U.1
  • 37
    • 0036195317 scopus 로고    scopus 로고
    • CDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase
    • Yang R.Z., Blaileanu G., Hansen B.C., Shuldiner A.R., Gong D.W. cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase. Genomics 2002, 79:445-450.
    • (2002) Genomics , vol.79 , pp. 445-450
    • Yang, R.Z.1    Blaileanu, G.2    Hansen, B.C.3    Shuldiner, A.R.4    Gong, D.W.5
  • 38
    • 61949403067 scopus 로고    scopus 로고
    • Alanine aminotransferase isoenzymes: molecular cloning and quantitative analysis of tissue expression in rats and serum elevation in liver toxicity
    • Yang R.Z., Park S., Reagan W.J., Goldstein R., Zhong S., Lawton M., Rajamohan F., Qian K., Liu L., Gong D.W. Alanine aminotransferase isoenzymes: molecular cloning and quantitative analysis of tissue expression in rats and serum elevation in liver toxicity. Hepatology 2009, 49:598-607.
    • (2009) Hepatology , vol.49 , pp. 598-607
    • Yang, R.Z.1    Park, S.2    Reagan, W.J.3    Goldstein, R.4    Zhong, S.5    Lawton, M.6    Rajamohan, F.7    Qian, K.8    Liu, L.9    Gong, D.W.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.