CHARACTERIZATION OF GLYCOCONJUGATES OF GUINEA-PIG SEMINAL-VESICLE BY LECTIN HISTOCHEMISTRY

In the present study, the expression of glycoconjugates in the guinea pig seminal vesicle was localized and partially characterized by lecti n histochemistry using a battery of 30 different lectins specific for different carbohydrate residues. The results indicate that the glandul ar epithelium of the guinea pig seminal vesicle exhibits complex glyco conjugates rich in Man, beta-GlcNAc, beta-Gal, alpha/beta-GalNAc, Fuc and complex NeuAc(alpha 2,6)Gal/GalNAc residues, as shown by its posit ive reactions to most lectins used. The Golgi region of the luminal se cretory epithelial cells expresses a complex glycoconjugate pattern, a s shown by its strong reactions to Man-(PSA, GNA), beta-GlcNAc-(S-WGA, PWA, DSA, UDA), beta-Gal-(RCA-I and -II), alpha/beta-GalNAc-(SBA, Jac , VVA, BPA) and complex NeuAc-(SNA) specific lectins, indicating that the secretory epithelial cells are active in glycosylation and secreti on process. It was also shown in the present study that the basal and luminal epithelial cells are different in their glycoconjugates. The b asal epithelial cells are rich in NeuAc(alpha 2,3)Gal residues as they are stained specifically by MAA. The fibroblasts in the epithelial-sm ooth muscle interface and the smooth muscle cells close to the glandul ar epithelium are shown to express more glycoconjugates as they are st ained intensely by GS-I-B-4, GS-II and SBA. However, their role in the epithelial-stromal interaction in the seminal vesicle remains to be e lucidated. In summary, the present study reports for the first time on the lectin binding patterns of the guinea pig seminal vesicle, and th e results show that the seminal vesicle epithelium elaborates and secr etes glycoconjugates in a complex pattern. Some of the lectins might b e useful as histochemical markers for the secretory activity and speci fic structural components in the guinea pig seminal vesicle. (C) 1998 Chapman & Hall.