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Gene Review

Got2  -  glutamatic-oxaloacetic transaminase 2,...

Mus musculus

Synonyms: AL022787, Aspartate aminotransferase, mitochondrial, FABP-1, FABP-pm, FABPpm, ...
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Disease relevance of Got2

  • Levels of mAspAT mRNA were higher in liver and intestine of mice treated with peroxisome proliferators, while levels in hepatoma cells were similar regardless of treatment [1].
  • Mouse mammary tumor viruses (MMTVs) contain distinct membrane glycoproteins of 52,000 daltons (gp52) and 36,000 daltons (gp36) [2].

High impact information on Got2


Biological context of Got2


Anatomical context of Got2


Associations of Got2 with chemical compounds


Physical interactions of Got2


Other interactions of Got2

  • Differentiation, induced by high calcium, did not affect FATP mRNA levels, but resulted in an approximately 50% increase in FACS mRNA, while decreasing FABP-pm mRNA by 50% [19].
  • The region coding for the mature mAspAT and that for the cAspAT show about 53% overall homology [7].
  • Thus, for mAAT the discrimination between native and non-native structures by Hsc70 may rely more on the level of structure of the binding sites than on their degree of exposure to the solvent in the native structure [18].
  • Three different nuclear loci for mitochondrial enzymes (Mod-2, Got-2, and Mor-1) have now been mapped in the mouse, all on different chromosomes [20].

Analytical, diagnostic and therapeutic context of Got2


  1. Expression of putative fatty acid transporter genes are regulated by peroxisome proliferator-activated receptor alpha and gamma activators in a tissue- and inducer-specific manner. Motojima, K., Passilly, P., Peters, J.M., Gonzalez, F.J., Latruffe, N. J. Biol. Chem. (1998) [Pubmed]
  2. Radioimmunoassays for the 36,000-dalton glycoprotein of murine mammary tumor viruses demonstrate type, group, and interspecies determinants. Teramoto, Y.A., Schlom, J. J. Virol. (1979) [Pubmed]
  3. 3T3 fibroblasts transfected with a cDNA for mitochondrial aspartate aminotransferase express plasma membrane fatty acid-binding protein and saturable fatty acid uptake. Isola, L.M., Zhou, S.L., Kiang, C.L., Stump, D.D., Bradbury, M.W., Berk, P.D. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  4. Selective up-regulation of fatty acid uptake by adipocytes characterizes both genetic and diet-induced obesity in rodents. Berk, P.D., Zhou, S., Kiang, C., Stump, D.D., Fan, X., Bradbury, M.W. J. Biol. Chem. (1999) [Pubmed]
  5. Regulation of putative fatty acid transporters and Acyl-CoA synthetase in liver and adipose tissue in ob/ob mice. Memon, R.A., Fuller, J., Moser, A.H., Smith, P.J., Grunfeld, C., Feingold, K.R. Diabetes (1999) [Pubmed]
  6. Adipocyte differentiation of 3T3-L1 cells involves augmented expression of a 43-kDa plasma membrane fatty acid-binding protein. Zhou, S.L., Stump, D., Sorrentino, D., Potter, B.J., Berk, P.D. J. Biol. Chem. (1992) [Pubmed]
  7. Cloning and sequence analysis of mRNA for mouse aspartate aminotransferase isoenzymes. Obaru, K., Nomiyama, H., Shimada, K., Nagashima, F., Morino, Y. J. Biol. Chem. (1986) [Pubmed]
  8. Structural organization of the mouse mitochondrial aspartate aminotransferase gene. Tsuzuki, T., Obaru, K., Setoyama, C., Shimada, K. J. Mol. Biol. (1987) [Pubmed]
  9. Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA. Bradbury, M.W., Berk, P.D. Biochem. J. (2000) [Pubmed]
  10. Regulatory regions of the mitochondrial and cytosolic isoenzyme genes participating in the malate-aspartate shuttle. Setoyama, C., Ding, S.H., Choudhury, B.K., Joh, T., Takeshima, H., Tsuzuki, T., Shimada, K. J. Biol. Chem. (1990) [Pubmed]
  11. Molecular structures and evolution of mouse isozyme genes functioning in the malate-aspartate shuttle. Shimada, K., Joh, T., Ding, S.H., Choudhury, B.K., Setoyama, C. Prog. Clin. Biol. Res. (1990) [Pubmed]
  12. Structure of the genes of two homologous intracellularly heterotopic isoenzymes. Cytosolic and mitochondrial aspartate aminotransferase of chicken. Juretić, N., Mattes, U., Ziak, M., Christen, P., Jaussi, R. Eur. J. Biochem. (1990) [Pubmed]
  13. Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake. Zhou, S.L., Stump, D., Kiang, C.L., Isola, L.M., Berk, P.D. Proc. Soc. Exp. Biol. Med. (1995) [Pubmed]
  14. Quantitation of plasma membrane fatty acid-binding protein by enzyme dilution and monoclonal antibody based immunoassay. Zhou, S.L., Potter, B.J., Stump, D., Sorrentino, D., Berk, P.D. Mol. Cell. Biochem. (1990) [Pubmed]
  15. Dietary restriction and triiodothyronine (T3) regulation of malate-aspartate shuttle enzymes in the liver and kidney of mice. Goyary, D., Sharma, R. Indian J. Biochem. Biophys. (2005) [Pubmed]
  16. Structural organization of the mouse mitochondrial malate dehydrogenase gene. Takeshima, H., Joh, T., Tsuzuki, T., Shimada, K., Matsukado, Y. J. Mol. Biol. (1988) [Pubmed]
  17. Cisplatin-induced toxicity is associated with platinum deposition in mouse kidney mitochondria in vivo and with selective inactivation of the alpha-ketoglutarate dehydrogenase complex in LLC-PK1 cells. Zhang, L., Cooper, A.J., Krasnikov, B.F., Xu, H., Bubber, P., Pinto, J.T., Gibson, G.E., Hanigan, M.H. Biochemistry (2006) [Pubmed]
  18. Identification of Hsc70 binding sites in mitochondrial aspartate aminotransferase. Artigues, A., Iriarte, A., Martinez-Carrion, M. Arch. Biochem. Biophys. (2006) [Pubmed]
  19. Expression and regulation of mRNA for putative fatty acid transport related proteins and fatty acyl CoA synthase in murine epidermis and cultured human keratinocytes. Harris, I.R., Farrell, A.M., Memon, R.A., Grunfeld, C., Elias, P.M., Feingold, K.R. J. Invest. Dermatol. (1998) [Pubmed]
  20. Mitochondrial malate dehydrogenase (Mor-1) in the mouse: linkage to chromosome 5 markers. Womack, J.E., Hawes, N.L., Soares, E.R., Roderick, T.H. Biochem. Genet. (1975) [Pubmed]
  21. Molecular cloning and in vivo expression of a precursor to rat mitochondrial aspartate aminotransferase. Mattingly, J.R., Rodriguez-Berrocal, F.J., Gordon, J., Iriarte, A., Martinez-Carrion, M. Biochem. Biophys. Res. Commun. (1987) [Pubmed]
  22. Monoclonal and polyclonal antibodies against porcine mitochondrial aspartate aminotransferase: their inhibition modes and application to enzyme immunoassay. Suzuki, T., Kishi, Y., Totani, M., Kagamiyama, H., Murachi, T. Biotechnol. Appl. Biochem. (1987) [Pubmed]
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