| pubmed-article:6199584 | pubmed:abstractText | The nature and distribution of lectin receptors were studied in normal, atrophic, metaplastic, hyperplastic, and neoplastic epithelium of canine prostate. Results were compared with prostatic epithelium of castrated dogs treated for 2 weeks with estradiol-17 beta 17-cyclopentylpropionate, 5 alpha-adrostane-3 alpha,17 beta-diol dipropionate, or 5 alpha-dihydrotestosterone. Eight biotinylated lectins were used as histochemical probes and avidin-biotin-peroxidase complex served as the visualant. Receptors for Ulex europaeus agglutinin-I were present in atrophic prostatic epithelium. Receptors for U. europaeus agglutinin-I, wheat, germ agglutinin, Dolichos biflorus agglutinin, and soybean agglutinin were present in epithelium that had undergone squamous metaplasia. Binding of peanut agglutinin receptors was present, to a limited extent, in squamous epithelium and was increased after they were unmasked (sialic acid residues cleaved with neuraminidase). In glandular cells of normal canine prostate and in benign prostatic hyperplasia, receptor sites were stained with Ricinus communis agglutinin-I, Concanavalia ensiformis agglutinin wheat germ agglutinin, and U. europaeus agglutinin-I. The basal cells in these tissues did not bind lectins. Prostatic carcinoma cells demonstrated receptors for wheat germ agglutinin and U. europaeus agglutinin-I. Responding and atrophic acini were present in prostates of castrated dogs treated with estradiol-17 beta 17-cyclopentylpropionate. Glandular cells of atrophic acini exhibited lectin receptor profiles similar to counterparts in castrated-untreated dogs. However, glandular cells responding to estrogen exhibited staining of free and cryptic peanut agglutinin receptor sites. Glandular cells of castrated dogs treated with 5 alpha-androstane 3 alpha,17 beta-diol dipropionate and 5 alpha-dihydrotestosterone have a pattern of lectin receptors similar to that found in normal and hyperplastic epithelium. Our studies show significant differences in lectin-binding patterns in the epithelium of atrophic, metaplastic, hyperplastic, and neoplastic canine prostate. They also demonstrate that the species of carbohydrate residues present in the glandular cells can be modified with sex hormones. | lld:pubmed |
