Glutathione transferases of classes alpha, mu and pi show selective expression in different regions of rat kidney.
1. Glutathione transferases (GST) are mainly cytosolic and occur in multiple forms, which can be arranged in three distinct, structural classes. The different enzyme forms show distinct substrate specificities with electrophilic and genotoxic substances. The expression of the alpha subunits 1, 2 and 8, the mu subunits 3, 4 and 6, and the pi subunit 7 of GST in different parts of the rat kidney was determined immunohistochemically. 2. GST immunoreactivity was present predominantly in the nephron, collecting duct and urothelium. 3. A conspicuous finding was that subunits 1, 2 and 8 were localized to the proximal tubules, while the mu subunit 3 was demonstrable in epithelial tubular cells from the distal tubules to the urothelium. The immunoreactivity of subunits 4 and 6 could be visualized in epithelial cells from the ascending thin limb to the collecting ducts. Subunit 7 was found in the thin limb of the loop of Henle, and in scattered cells in the distal tubules. 4. The urothelial cells covering the papilla and the renal calyces showed immunoreactivity to GST subunits 2-4 and 6-8. 5. Thus, in the nephron the class alpha GSTs were selectively expressed in the proximal tubules and the class mu and class pi GST in the thin loop of Henle and distal tubules. The cells in the collecting ducts and the urothelium, which have a different ontogeny than the nephron, do not show any corresponding differential distribution of the GST classes. 6. Cells in a given location were in some cases found to be non-reactive with a given antiserum in an otherwise immunoreactive cell population, demonstrating a spatial variation in GST expression. The immunoreactivity to the different forms of GST was predominantly cytoplasmic but a nuclear localization could also be demonstrated. 7. The panel of antibodies to GST may tentatively be used as markers in localizing lesions in restricted parts of the nephrons and to elucidate dynamic alterations in the tubular system in response to physiological and toxic agents.
Rozell
B
B
Department of Histology, University of Göteborg, Sweden.
Hansson
H A
HA
Guthenberg
C
C
Tahir
M K
MK
Mannervik
B
B
D000818:Animals; D000918:Antibody Specificity; D005591:Chemical Fractionation; D005982:Glutathione Transferase / Q000032:analysis*; D015151:Immunoblotting; D007150:Immunohistochemistry; D007527:Isoenzymes / Q000032:analysis*; D007668:Kidney / Q000737:chemistry*; D008297:Male; D011506:Proteins / Q000032:analysis; D051381:Rats; D017207:Rats, Sprague-Dawley; D012995:Solubility
D007527:Isoenzymes; D011506:Proteins; D005982:Glutathione Transferase