MEMBRANE-BOUND CARBONIC-ANHYDRASE ACTIVITY IN THE RAT CORNEAL ENDOTHELIUM AND RETINA

Localization of carbonic anhydrase (CA) was investigated in the rat ey e by light and electron microscopy, and the inhibitory effects on CA d istribution in the rat eye were compared between dorzolamide and aceta zolamide. The cobalt sulfide histochemical method was used to study th e CA localization. Acidic osmification was carried out for postfixatio n of the electron microscopic observations. The inhibition of CA activ ity was examined with different concentrations of acetazolamide and do rzolamide. The cytoplasm, lateral cell membranes and karyoplasm of the corneal endothelium showed CA activity. In the retina, the processes and cell bodies of Muller cells, the tips of the outer segments of the rods, and apical villi and basolateral membranes of the pigment epith elium indicated CA activity. CA activity was inhibited by dorzolamide at lower concentrations than needed for acetazolamide and only the CA activity of the nerve fiber layer remained at 10(-6) M of acetazolamid e and 5 x 10(-7) M of dorzolamide. The presence of membrane-bound CA a ctivity was confirmed in the corneal endothelium and Muller cells. CA activity was also demonstrated in the apices of rod outer segments and scleral fibroblasts. The CA inhibition test revealed that dorzolamide was a stronger CA inhibitor than acetazolamide and that the CA activi ty of the nerve fiber layer was strongest in the rat eye.