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Expression of Glutathione S‐Transfer α, P1–1 and T1–1 in the Human Gastrointestinal Tract
Author(s) -
Bruin Wieke C. C.,
Wagenmans Muriel J. M.,
Peters Wilbert H. M.
Publication year - 2000
Publication title -
japanese journal of cancer research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 141
eISSN - 1349-7006
pISSN - 0910-5050
DOI - 10.1111/j.1349-7006.2000.tb00946.x
Subject(s) - gastrointestinal tract , isozyme , glutathione , carcinogen , biology , immunohistochemistry , glutathione s transferase , gstp1 , secretion , xenobiotic , enzyme , human gastrointestinal tract , carcinogenesis , biochemistry , microbiology and biotechnology , immunology , gene
Glutathione S‐transferases (GSTs) form a family of enzymes, which play an important role in the prevention of cancer by detoxifying numerous potentially carcinogenic compounds. GSTs catalyze the conjugation of glutathione to such harmful molecules, and enable their secretion. Human GSTs can be divided into five main classes. The θ class of isoenzymes was only recently identified and limited (immunohistochemical) data on these enzymes are available. In the present study, paraffinembedded sections of different gastrointestinal tissues were analyzed immunohistochemically for GSTα, GSTP1–1 and GSTT1–1 expression using specific antibodies. GSTα, GSTP1–1 and GSTT1–1 were highly expressed in all gastrointestinal tissues examined, with a unique cellular distribution. GSTT1–1 is the first GST isoenzyme demonstrated in duodenal Paneth cells and glands of Brunner. The common expression of GSTα, GSTT1–1 and GSTP1–1 in many cell types along the human gastrointestinal tract suggests an important role in the protection against carcinogens and other xenobiotics.

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