TY - JOUR
T1 - Localization of the thioredoxin system in normal rat kidney
AU - Oberley, Terry D.
AU - Verwiebe, Eric
AU - Zhong, Weixiong
AU - Kang, Sang Won
AU - Rhee, Sue Goo
N1 - Funding Information:
This work was supported by the Veterans Administration Research Service and a grant from the Department of Pathology and Laboratory Medicine, University of Wisconsin Medical School. The authors would like to thank Dr. Larry Oberley for critical reading of the manuscript.
PY - 2001/2/15
Y1 - 2001/2/15
N2 - Components of the thioredoxin system were localized in normal rat kidney using immunoperoxidase techniques at the light microscopic level and immunogold techniques at the ultrastructural level. Results from both methods were similar. Thioredoxin, thioredoxin reductases, and peroxiredoxins showed cell-type-specific localization, with the same cell types (proximal and distal tubular epithelial, papillary collecting duct, and transitional epithelial cells) previously identified as having high amounts of antioxidant enzyme immunoreactive proteins and oxidative damage products also having high levels of proteins of the thioredoxin system. In addition, peroxiredoxins II and IV were found in high levels in the cytoplasm of red blood cells, identified in kidney blood vessels. While thioredoxin and thioredoxin reductase 1 were found in all subcellular locations in kidney cells, thioredoxin reductase 2 was found predominantly in mitochondria. Thioredoxin reductase 1 was identified in rat plasma, suggesting it is a secreted protein. Peroxiredoxins often had specific subcellular locations, with peroxiredoxins III and V found in mitochondria and peroxiredoxin IV found in lysosomes. Our results emphasize the complex nature of the thioredoxin system, demonstrating unique cell-type and organelle specificity.
AB - Components of the thioredoxin system were localized in normal rat kidney using immunoperoxidase techniques at the light microscopic level and immunogold techniques at the ultrastructural level. Results from both methods were similar. Thioredoxin, thioredoxin reductases, and peroxiredoxins showed cell-type-specific localization, with the same cell types (proximal and distal tubular epithelial, papillary collecting duct, and transitional epithelial cells) previously identified as having high amounts of antioxidant enzyme immunoreactive proteins and oxidative damage products also having high levels of proteins of the thioredoxin system. In addition, peroxiredoxins II and IV were found in high levels in the cytoplasm of red blood cells, identified in kidney blood vessels. While thioredoxin and thioredoxin reductase 1 were found in all subcellular locations in kidney cells, thioredoxin reductase 2 was found predominantly in mitochondria. Thioredoxin reductase 1 was identified in rat plasma, suggesting it is a secreted protein. Peroxiredoxins often had specific subcellular locations, with peroxiredoxins III and V found in mitochondria and peroxiredoxin IV found in lysosomes. Our results emphasize the complex nature of the thioredoxin system, demonstrating unique cell-type and organelle specificity.
KW - Free radicals
KW - Kidney
KW - Peroxiredoxin
KW - Reactive oxygen species
KW - Thioredoxin
KW - Thioredoxin reductase
UR - http://www.scopus.com/inward/record.url?scp=0035865858&partnerID=8YFLogxK
U2 - 10.1016/S0891-5849(00)00486-X
DO - 10.1016/S0891-5849(00)00486-X
M3 - Article
C2 - 11182297
AN - SCOPUS:0035865858
SN - 0891-5849
VL - 30
SP - 412
EP - 424
JO - Free Radical Biology and Medicine
JF - Free Radical Biology and Medicine
IS - 4
ER -