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The major alpha-class glutathione S-transferases of rabbit lung and liver. Primary sequences, expression, and regulation
The complete primary structures of two distinct rabbit alpha-class glutathione S-transferase (GST) subunits, rbGST alpha I and rbGST alpha II, have been derived from cDNA sequences. Clones encoding rbGST alpha I were isolated from both hepatic and pulmonary cDNA libraries, whereas clones encoding rb...
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Published in: | The Journal of biological chemistry 1991-10, Vol.266 (29), p.19681-19687 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The complete primary structures of two distinct rabbit alpha-class glutathione S-transferase (GST) subunits, rbGST alpha I
and rbGST alpha II, have been derived from cDNA sequences. Clones encoding rbGST alpha I were isolated from both hepatic and
pulmonary cDNA libraries, whereas clones encoding rbGST alpha II were isolated only from the hepatic library. Immunochemical
and peptide sequence data confirmed that rbGST alpha I corresponds to the 27-kDa alpha-class subunit purified from rabbit
lung (Serabjit-Singh, C. J., and Bend, J. R. (1988) Arch. Bioch. Biophys. 267, 184-194). Expression of rbGST alpha II in liver
but not in lung and expression of rbGST alpha I in both liver and lung was substantiated by Northern and immunochemical analyses.
rbGST alpha I and rbGST alpha II are composed of 223 and 221 amino acids, respectively, and are 78% identical in amino acid
sequence. Compared to published GST sequences, both proteins are most closely related to the human Ha subunit (greater than
80% identity). On the basis of sequence comparison and Northern and Southern analyses, we conclude that rbGST alpha I and
rbGST alpha II are products of different genes that are independently regulated. Further, the regulatory elements of the alpha-class
GST genes may be significantly different in the rabbit as compared to the rat, as evidenced by the lack of induction by phenobarbital
of rabbit hepatic or pulmonary alpha-class GST subunits, enzymatic activity, or mRNA. This tissue- and species-dependent expression
of the predominant class of cytosolic GST implies unique functions for each isozyme and may contribute to the differential
susceptibility of tissues and animals to toxicants. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(18)55046-8 |