Cytochemical characterization of cuprolinic blue-stained proteoglycans in the epithelial-stromal interface of the guinea pig lateral prostate.
Three types (T1, T2, T3) of proteoglycan (PG) filaments, as demonstrated by cuprolinic blue (CB) under critical electrolyte concentration method in the epithelial-stromal interface of the guinea pig lateral prostate, were characterized cytochemically by using a number of glycosaminoglycan(GAG)-degrading enzymes and nitrous acid. The results showed that T1 filaments located in basement membranes of the epithelium, endothelium, and smooth muscle cells, were removed by nitrous acid, heparitinase, and pronase but resistant to chondroitinase (Ch)-ABC and Ch-AC, heparinase, neuraminidase, and Streptomyces (S) hyaluronidase. The T1 filaments, therefore, contain heparan sulfate. The T2 filaments closely linked to collagen fibrils were removed by Ch-ABC, Ch-ABC plus S-hyaluronidase, and pronase but were resistant to nitrous acid, heparitinase, heparinase, neuraminidase, and S-hyaluronidase. These show that T2 filaments are rich in dermatan sulfate. The T3 filaments in the interstitial spaces and on the surface of fibroblasts were removed by Ch-ABC, Ch-AC, and pronase but were resistant to heparitinase, heparinase, hyaluronidase, neuraminidase, and nitrous acid. They are, therefore, rich in chondroitin sulfate.
Chan
L
L
Department of Anatomy, Faculty of Medicine, University of Hong Kong.
Wong
Y C
YC
D000818:Animals; D011508:Chondroitin Sulfate Proteoglycans / Q000032:analysis; D004848:Epithelium; D006025:Glycosaminoglycans / Q000032:analysis; D006168:Guinea Pigs; D007211:Indoles; D008297:Male; D009942:Organometallic Compounds; D011467:Prostate / Q000032:analysis* / Q000648:ultrastructure; D011509:Proteoglycans / Q000032:analysis*
D011508:Chondroitin Sulfate Proteoglycans; D006025:Glycosaminoglycans; D007211:Indoles; D009942:Organometallic Compounds; D011509:Proteoglycans; C015445:copper phthalocyanine