Immunolocalization of copper-zinc superoxide dismutase. II. Rat.
Copper-zinc superoxide dismutase (CuZn SOD) has been localized in formalin-fixed rat tissues. Staining with a modified immunoenzyme bridge technique using the avidin-biotin-peroxidase complex revealed abundant endogenous CuZn SOD in cells that function in transporting ions, either cellularly, as in the case of tracheal, bronchiolar, and colonic epithelial cells, gastric oxyntic cells, and cells lining the salivary ducts and proximal convoluted tubules in the nephron, or intracellularly, as exemplified by skeletal muscle and neurons. Additionally, the enzyme was consistently demonstrable in hepatocytes, endocrine cells of the islets of Langerhans, and the highly membranous oligodendrocytes in the central nervous system. Cellular processes that maintain high ionic gradients appear especially vulnerable to the superoxide anion, thus necessitating the presence of CuZn SOD to scavenge toxic free radicals of oxygen. Comparison of these observations with other immunocytochemical reports indicates that the cellular distribution of CuZn SOD varies between different species.
D000818:Animals; D003300:Copper / Q000378:metabolism; D005557:Formaldehyde; D005609:Free Radicals; D006651:Histocytochemistry; D007124:Immunoenzyme Techniques; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains / Q000378:metabolism*; D013482:Superoxide Dismutase / Q000032:analysis*; D014018:Tissue Distribution; D015032:Zinc / Q000378:metabolism
D005609:Free Radicals; D005557:Formaldehyde; D003300:Copper; D013482:Superoxide Dismutase; D015032:Zinc