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GSTM5  -  glutathione S-transferase mu 5

Homo sapiens

Synonyms: GST class-mu 5, GSTM5-5, GTM5, Glutathione S-transferase Mu 5
 
 
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High impact information on GSTM5

  • Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13 [1].
  • The open reading frame of GSTM5 shared a high degree of homology with the sequences of other Mu-class glutathione S-transferases, but its 846-nucleotide 3'-noncoding region was unique and considerably larger than that of any of the other Mu forms [2].
  • A form designated GSTM5, was cloned from a human brain cDNA library and its sequence determined [2].
  • To determine a structural basis for the catalytic differences between hGSTM3-3 and other mu class enzymes, chimeric proteins were designed by modular interchange of the divergent C-terminal domains of hGSTM3 and hGSTM5 subunits [3].
  • GSTM4 and GSTM5 subunits, here identified for the first time in human tissue extracts, were minor components, with GSTM5 found only in brain, lung and testis [4].
 

Biological context of GSTM5

 

Anatomical context of GSTM5

 

Associations of GSTM5 with chemical compounds

  • Cytosolic GST subunits were resolved by reverse-phase HPLC methods, individual components were assigned to Alpha, Mu and Pi classes on the basis of their immunoreactivities, and peptide-sequence-specific antisera were used to distinguish among five different Mu-class subunits (GSTM1-GSTM5) [4].
 

Regulatory relationships of GSTM5

  • GSTM2 transcript was expressed in all patients in contradistinction to GSTM5, which was not detected in any sample [7].
 

Analytical, diagnostic and therapeutic context of GSTM5

  • A basis for differentiating among the multiple human Mu-glutathione S-transferases and molecular cloning of brain GSTM5 [2].
  • PCR primers developed from sequences 3'-downstream from the GSTM5 gene were used to identify clones containing the GSTM3 gene [5].

References

  1. Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13. Pearson, W.R., Vorachek, W.R., Xu, S.J., Berger, R., Hart, I., Vannais, D., Patterson, D. Am. J. Hum. Genet. (1993) [Pubmed]
  2. A basis for differentiating among the multiple human Mu-glutathione S-transferases and molecular cloning of brain GSTM5. Takahashi, Y., Campbell, E.A., Hirata, Y., Takayama, T., Listowsky, I. J. Biol. Chem. (1993) [Pubmed]
  3. An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases. Patskovsky, Y.V., Patskovska, L.N., Listowsky, I. Biochemistry (1999) [Pubmed]
  4. Subunit diversity and tissue distribution of human glutathione S-transferases: interpretations based on electrospray ionization-MS and peptide sequence-specific antisera. Rowe, J.D., Nieves, E., Listowsky, I. Biochem. J. (1997) [Pubmed]
  5. Distinctive structure of the human GSTM3 gene-inverted orientation relative to the mu class glutathione transferase gene cluster. Patskovsky, Y.V., Huang, M.Q., Takayama, T., Listowsky, I., Pearson, W.R. Arch. Biochem. Biophys. (1999) [Pubmed]
  6. Multiple glutathione S-transferase isoforms are present on male germ cell plasma membrane. Rao, A.V., Shaha, C. FEBS Lett. (2001) [Pubmed]
  7. Mu class glutathione S-transferase mRNA isoform expression in acute lymphoblastic leukaemia. Kearns, P.R., Chrzanowska-Lightowlers, Z.M., Pieters, R., Veerman, A., Hall, A.G. Br. J. Haematol. (2003) [Pubmed]
 
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