Expression of glyoxalase, glutathione peroxidase and glutathione S-transferase isoenzymes in different bovine tissues

J D Hayes, S W Milner, S W Walker

    Research output: Contribution to journalArticle

    22 Citations (Scopus)

    Abstract

    (1) The tissue-specific expression of various glutathione-dependent enzymes, including glutathione S-transferase (GST), glutathione peroxidase and glyoxalase I, has been studied in bovine adrenals, brain, heart, kidney, liver, lung and spleen. Of the organs studied, liver was found to possess the greatest GST and glyoxalase I activity, and spleen the greatest glutathione peroxidase activity. The adrenals contained large amounts of these glutathione-dependent enzymes, but significant differences were observed between the cortex and medulla. (2) GST and glyoxalase I activity were isolated by S-hexylglutathione affinity chromatography. Glyoxalase I was found in all the organs examined, but GST exhibited marked tissue-specific expression. (3) The alpha, mu and pi classes of GST (i.e., those that comprise respectively Ya/Yc, Yb/Yn and Yf subunits) were all identified in bovine tissues. However, the Ya and Yc subunits of the alpha class GST were not co-ordinately regulated nor were the Yb and Yn subunits of the mu class GST. (4) Bovine Ya subunits (25.5-25.7 kDa) were detected in the adrenal, liver and kidney, but not in brain, heart, lung or spleen. The Yc subunit (26.4 kDa) was expressed in all those organs which expressed the Ya subunit, but was also found in lung. The mu class Yb (27.0 kDa) and Yn (26.1 kDa) subunits were present in all organs; however, brain, lung and spleen contained significantly more Yn than Yb type subunits. The pi class Yf subunit (24.8 kDa) was detected in large amounts in the adrenals, brain, heart, lung and spleen, but not in kidney or liver. (5) Gradient affinity elution of S-hexylglutathione-Sepharose showed that the bovine proteins that bind to this matrix elute in the order Ya/Yc, Yf, Yb/Yn and glyoxalase I. (6) In conclusion, the present investigation has shown that bovine GST are much more complex than previously supposed; Asaoka (J. Biochem. 95 (1984) 685-696) reported the purification of mu class GST but neither alpha nor pi class GST were isolated.

    Original languageEnglish
    Pages (from-to)21-9
    Number of pages9
    JournalBiochimica et Biophysica Acta: General Subjects
    Volume994
    Issue number1
    DOIs
    Publication statusPublished - 19 Jan 1989

    Fingerprint

    Lactoylglutathione Lyase
    Glutathione Peroxidase
    Glutathione Transferase
    Isoenzymes
    Tissue
    Spleen
    Lung
    Glutathione S-Transferase pi
    Liver
    Brain
    Kidney
    Glutathione
    Enzymes
    Affinity Chromatography
    Affinity chromatography
    Purification
    Proteins

    Keywords

    • Adrenal Glands/enzymology
    • Animals
    • Blotting, Western
    • Brain/enzymology
    • Cattle
    • Chromatography, Affinity
    • Cytosol/enzymology
    • Electrophoresis, Polyacrylamide Gel
    • Glutathione Peroxidase/metabolism
    • Glutathione Transferase/metabolism
    • Isoenzymes/metabolism
    • Kidney/enzymology
    • Lactoylglutathione Lyase/metabolism
    • Liver/enzymology
    • Lung/enzymology
    • Lyases/metabolism
    • Myocardium/enzymology
    • Spleen/enzymology
    • Thiolester Hydrolases/metabolism
    • Tissue Distribution

    Cite this

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    title = "Expression of glyoxalase, glutathione peroxidase and glutathione S-transferase isoenzymes in different bovine tissues",
    abstract = "(1) The tissue-specific expression of various glutathione-dependent enzymes, including glutathione S-transferase (GST), glutathione peroxidase and glyoxalase I, has been studied in bovine adrenals, brain, heart, kidney, liver, lung and spleen. Of the organs studied, liver was found to possess the greatest GST and glyoxalase I activity, and spleen the greatest glutathione peroxidase activity. The adrenals contained large amounts of these glutathione-dependent enzymes, but significant differences were observed between the cortex and medulla. (2) GST and glyoxalase I activity were isolated by S-hexylglutathione affinity chromatography. Glyoxalase I was found in all the organs examined, but GST exhibited marked tissue-specific expression. (3) The alpha, mu and pi classes of GST (i.e., those that comprise respectively Ya/Yc, Yb/Yn and Yf subunits) were all identified in bovine tissues. However, the Ya and Yc subunits of the alpha class GST were not co-ordinately regulated nor were the Yb and Yn subunits of the mu class GST. (4) Bovine Ya subunits (25.5-25.7 kDa) were detected in the adrenal, liver and kidney, but not in brain, heart, lung or spleen. The Yc subunit (26.4 kDa) was expressed in all those organs which expressed the Ya subunit, but was also found in lung. The mu class Yb (27.0 kDa) and Yn (26.1 kDa) subunits were present in all organs; however, brain, lung and spleen contained significantly more Yn than Yb type subunits. The pi class Yf subunit (24.8 kDa) was detected in large amounts in the adrenals, brain, heart, lung and spleen, but not in kidney or liver. (5) Gradient affinity elution of S-hexylglutathione-Sepharose showed that the bovine proteins that bind to this matrix elute in the order Ya/Yc, Yf, Yb/Yn and glyoxalase I. (6) In conclusion, the present investigation has shown that bovine GST are much more complex than previously supposed; Asaoka (J. Biochem. 95 (1984) 685-696) reported the purification of mu class GST but neither alpha nor pi class GST were isolated.",
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    author = "Hayes, {J D} and Milner, {S W} and Walker, {S W}",
    year = "1989",
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    day = "19",
    doi = "10.1016/0167-4838(89)90057-5",
    language = "English",
    volume = "994",
    pages = "21--9",
    journal = "Biochimica et Biophysica Acta: General Subjects",
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    number = "1",

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    Expression of glyoxalase, glutathione peroxidase and glutathione S-transferase isoenzymes in different bovine tissues. / Hayes, J D; Milner, S W; Walker, S W.

    In: Biochimica et Biophysica Acta: General Subjects, Vol. 994, No. 1, 19.01.1989, p. 21-9.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Expression of glyoxalase, glutathione peroxidase and glutathione S-transferase isoenzymes in different bovine tissues

    AU - Hayes, J D

    AU - Milner, S W

    AU - Walker, S W

    PY - 1989/1/19

    Y1 - 1989/1/19

    N2 - (1) The tissue-specific expression of various glutathione-dependent enzymes, including glutathione S-transferase (GST), glutathione peroxidase and glyoxalase I, has been studied in bovine adrenals, brain, heart, kidney, liver, lung and spleen. Of the organs studied, liver was found to possess the greatest GST and glyoxalase I activity, and spleen the greatest glutathione peroxidase activity. The adrenals contained large amounts of these glutathione-dependent enzymes, but significant differences were observed between the cortex and medulla. (2) GST and glyoxalase I activity were isolated by S-hexylglutathione affinity chromatography. Glyoxalase I was found in all the organs examined, but GST exhibited marked tissue-specific expression. (3) The alpha, mu and pi classes of GST (i.e., those that comprise respectively Ya/Yc, Yb/Yn and Yf subunits) were all identified in bovine tissues. However, the Ya and Yc subunits of the alpha class GST were not co-ordinately regulated nor were the Yb and Yn subunits of the mu class GST. (4) Bovine Ya subunits (25.5-25.7 kDa) were detected in the adrenal, liver and kidney, but not in brain, heart, lung or spleen. The Yc subunit (26.4 kDa) was expressed in all those organs which expressed the Ya subunit, but was also found in lung. The mu class Yb (27.0 kDa) and Yn (26.1 kDa) subunits were present in all organs; however, brain, lung and spleen contained significantly more Yn than Yb type subunits. The pi class Yf subunit (24.8 kDa) was detected in large amounts in the adrenals, brain, heart, lung and spleen, but not in kidney or liver. (5) Gradient affinity elution of S-hexylglutathione-Sepharose showed that the bovine proteins that bind to this matrix elute in the order Ya/Yc, Yf, Yb/Yn and glyoxalase I. (6) In conclusion, the present investigation has shown that bovine GST are much more complex than previously supposed; Asaoka (J. Biochem. 95 (1984) 685-696) reported the purification of mu class GST but neither alpha nor pi class GST were isolated.

    AB - (1) The tissue-specific expression of various glutathione-dependent enzymes, including glutathione S-transferase (GST), glutathione peroxidase and glyoxalase I, has been studied in bovine adrenals, brain, heart, kidney, liver, lung and spleen. Of the organs studied, liver was found to possess the greatest GST and glyoxalase I activity, and spleen the greatest glutathione peroxidase activity. The adrenals contained large amounts of these glutathione-dependent enzymes, but significant differences were observed between the cortex and medulla. (2) GST and glyoxalase I activity were isolated by S-hexylglutathione affinity chromatography. Glyoxalase I was found in all the organs examined, but GST exhibited marked tissue-specific expression. (3) The alpha, mu and pi classes of GST (i.e., those that comprise respectively Ya/Yc, Yb/Yn and Yf subunits) were all identified in bovine tissues. However, the Ya and Yc subunits of the alpha class GST were not co-ordinately regulated nor were the Yb and Yn subunits of the mu class GST. (4) Bovine Ya subunits (25.5-25.7 kDa) were detected in the adrenal, liver and kidney, but not in brain, heart, lung or spleen. The Yc subunit (26.4 kDa) was expressed in all those organs which expressed the Ya subunit, but was also found in lung. The mu class Yb (27.0 kDa) and Yn (26.1 kDa) subunits were present in all organs; however, brain, lung and spleen contained significantly more Yn than Yb type subunits. The pi class Yf subunit (24.8 kDa) was detected in large amounts in the adrenals, brain, heart, lung and spleen, but not in kidney or liver. (5) Gradient affinity elution of S-hexylglutathione-Sepharose showed that the bovine proteins that bind to this matrix elute in the order Ya/Yc, Yf, Yb/Yn and glyoxalase I. (6) In conclusion, the present investigation has shown that bovine GST are much more complex than previously supposed; Asaoka (J. Biochem. 95 (1984) 685-696) reported the purification of mu class GST but neither alpha nor pi class GST were isolated.

    KW - Adrenal Glands/enzymology

    KW - Animals

    KW - Blotting, Western

    KW - Brain/enzymology

    KW - Cattle

    KW - Chromatography, Affinity

    KW - Cytosol/enzymology

    KW - Electrophoresis, Polyacrylamide Gel

    KW - Glutathione Peroxidase/metabolism

    KW - Glutathione Transferase/metabolism

    KW - Isoenzymes/metabolism

    KW - Kidney/enzymology

    KW - Lactoylglutathione Lyase/metabolism

    KW - Liver/enzymology

    KW - Lung/enzymology

    KW - Lyases/metabolism

    KW - Myocardium/enzymology

    KW - Spleen/enzymology

    KW - Thiolester Hydrolases/metabolism

    KW - Tissue Distribution

    U2 - 10.1016/0167-4838(89)90057-5

    DO - 10.1016/0167-4838(89)90057-5

    M3 - Article

    C2 - 2909253

    VL - 994

    SP - 21

    EP - 29

    JO - Biochimica et Biophysica Acta: General Subjects

    JF - Biochimica et Biophysica Acta: General Subjects

    SN - 0304-4165

    IS - 1

    ER -