A sheep antibody to human Tamm-Horsfall protein, the major protein in normal urine, was used in an immunohistological study of organs of 48 species of vertebrate animals, representing the classes Mammalia, Aves, Reptilia, Amphibia, Osteichthyes and Chondrichthyes. Immunoreactivity was shown in the thick limb of the loop of Henle in the kidney of mammals, but there was no reactivity with tissues of birds or reptiles. Superficial layers of the skin of several amphibians and fish, superficial layers of the oral mucosa and gills of fish, and the distal tubules of the kidney of some amphibians, reacted with the antibody. Immunoreactivity with mammalian kidney was removed by passage of the antibody down an immunoadsorption column coated with human Tamm-Horsfall protein, and amphibian immunoreactivity was removed by incubation of the antibody with material prepared from frogs in the same way as Tamm-Horsfall protein. These findings suggest that immunoreactive Tamm-Horsfall protein appeared early in vertebrate phylogeny, initially in skin and gills and later in kidney, and that although conserved in evolution, it shows antigenic differences between amphibians and mammals. Its distribution is consistent with the hypothesis that is acts as a waterproofing agent.
SUMMARYChicks were treated at 2 weeks of age with 4, l5, 40, 100 and 150 mg/kg of monensin, an ionophore used for its anticoccidial and growth-promoting properties. In the present immunohistochemical study, the expressions and distribution of Na
Seven lectins were employed to localize glycoconjugates in the skin of a toad (Bufo viridis). Each of the lectins exhibited a particular, specific and selective binding pattern. Peanut lectin (PNA) and WGA bound to mitochondria-rich (MR) cells, but WGA bound also abundantly, in the dermis. Band 3-like protein, as indicated by the reaction with polyclonal anti band 3 antibody, was localized exclusively in MR cells. Ionic acclimation (200 mmol/L NaCl, or 50 mmol/L KCl) affected profoundly the binding pattern of the lectins. High NaCl acclimation resulted also in diminishing anti band 3 antibody binding, whereas in skins of KCl-acclimated toads the staining remained similar to the control. The binding of WGA but not PNA, corresponded with the same cells that stained with anti band 3 antibody. PNA in concentration of > 10 micrograms/mL reduced reversibly, both the resting and activated Cl- conductance by 25-30%. Based on differential binding of band 3, WGA and PNA, these observations provide conclusive verification of the presence of at least two populations of MR cells in the toad skin epithelium. It is suggested that the PNA positive MR cells may correspond to a beta-type MR cell. The information can be used to study molecular mechanisms that are involved in ionic acclimation.
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