Distribution pattern of three neural calcium-binding proteins (NCS-1, VILIP and @entity52447 ) in @entity1573 , @entity291 and XXXX retina.

@entity1 @entity35 @entity73199 @entity73197 @entity73198 @entity1573 @entity141 @entity291 @entity52447
Neural @entity141 -binding proteins (NCaPs) constitute a subfamily of 4-EF-hand proteins, and display a histological and structural dichotomy: the A-type NCaPs are selectively expressed by the retina and pineal organ and display two canonical EF-hands, whereas the B-type NCaPs are found in the entire brain and present three regular EF-hands. In this study, antisera were raised against the A-type NCaP @entity52447 (26 kDa) and the B-type NCaPs @entity73197 and @entity73198 (22 kDa). Since the sequence identity among NCaPs is high, specific polyclonal antibodies were purified by double cross-immunoaffinity chromatography; both ELISA and immunoblot analyses determined that the resulting antibodies showed selectivity ratios inferior to 1/363 for the two other related NCaPs. Besides, the anti- @entity73197 antibodies displayed some affinity toward @entity73199 , and the antirecoverin antibodies recognized a 24 kDa protein, which is most likely visinin. Thus, immunohistochemical studies on the @entity1573 , @entity35 and @entity291 retina revealed that anti- @entity52447 antibodies recognized the vertebrate photoreceptors and a small number of @entity1 bipolar cells. Anti- @entity73197 antibodies exclusively labelled the inner retina, i.e. the amacrine and ganglion cells. @entity73198 was mainly present in the photoreceptor inner segments, the inner plexiform layer and the ganglion cells. @entity73198 showed the highest species disparity. The retinal localization of @entity73198 and @entity73197 offered an important morphological basis for the understanding of their function. Furthermore, specific antibodies against the NCaPs may enable the identification of cell populations in more complex neural tissues, such as the brain.
