Quantitative histochemical assay for superoxide dismutase in rat brain.
Superoxide anions are highly reactive radicals overproduced in many pathological situations such as inflammation and ischemia. One of the major factors in the protection from superoxide anions is the enzyme superoxide dismutase (SOD), which catalyzes the dismutation of superoxide to hydrogen peroxide. This study presents a quantitative histochemical method to estimate SOD activity in rat brain tissue sections. This method is based on the cerium capture method and 3,3'-diaminobenzidine amplification of transition cerium compounds. Substrate for SOD was provided by reduction of oxygen during the autoxidation of riboflavin in the presence of UV light. This histochemical method reveals the overall activity of the three different forms of SOD described in mammalian tissues: cytosolic copper-zinc SOD, mitochondrial manganese SOD, and the high molecular weight extracellular SOD. Eventually, this method can be used to quantify SOD activity in tissue sections by image analysis.
Viggiano
Alessandro
A
Department of Experimental Medicine, Second University of Naples, Via Constantinopoli 16, 80138 Naples, Italy.
Viggiano
Davide
D
Viggiano
Andrea
A
De Luca
Bruno
B
D000818:Animals; D001921:Brain / Q000201:enzymology*; D006651:Histocytochemistry; D007527:Isoenzymes / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D015203:Reproducibility of Results; D013482:Superoxide Dismutase / Q000378:metabolism*
D007527:Isoenzymes; D013482:Superoxide Dismutase