Ar. Caffe et al., DISTRIBUTION OF PURKINJE CELL-SPECIFIC ZEBRIN-II ALDOLASE-C IMMUNOREACTIVITY IN THE MOUSE, RAT, RABBIT, AND HUMAN RETINA, Journal of comparative neurology, 348(2), 1994, pp. 291-297
The developmental, genetic, and biochemical similarities that have bee
n observed between the cerebellum and retina form the basis for ongoin
g investigations into retinal expression of cerebellar-specific protei
ns. We have examined the mouse, rat, rabbit, and human retina for expr
ession of a protein that is present in parasagittal Purkinje cell stri
ps and that is recognized by the antibody Zebrin-II. This protein has
recently been identified as a member of the aldolase C isoenzymes. Wes
tern blotting and immunocytochemistry have been used. The monoclonal a
ntibody Zebrin-II recognized a prominent 36 kDa protein band on immuno
blots of both the cerebellum and the retina of the examined species. I
mmunocytochemistry showed that, in the three nonhuman species, cells w
ere stained in the ganglion cell layer (GCL). In addition, in the mous
e and rabbit, cells in the inner nuclear layer (INL) were also labeled
. Except for the visual streak, there were more immunopositive cells i
n the rabbit GCL and INL than in corresponding areas of the mouse reti
na. In the human, in contrast to the other species, the photoreceptor
cell layer was strongly aldolase C immunoreactive. In all species exce
pt for the rat, the photoreceptor inner segments also displayed a weak
labeling. The results show that this aldolase C isoenzyme is another
protein that is selectively expressed by the cerebellum and retina. Fu
rthermore, the retinal expression is species specific, and this patter
n seems to show a good correlation with the oxygenation level of the i
ndividual compartments. The indication that this aldolase C isoenzyme
has specific developmental functions in the retina provides additional
clues for our understanding of cerebellar organization. (C) 1994 Wiie
y-Liss, Inc.