The glycoconjugates of the mucosal surface of urinary bladder act as a barrier against invasion by pathogenic microorganisms and injury from toxic substances. Furthermore, they serve as a source of soluble urinary glycoproteins, which actively modify the urine composition. Glycoconjugate pattern characterizes distinct cellular populations, cell differentiation and maturation, as well as cell morpho-functional changes. We investigated the glycan pattern in the bladder epithelium by lectin histochemistry, comparatively in the horse and donkey. Tissue fragments were fixed in 4% (w/v) neutral formalin and then embedded in paraffin wax. Sections were stained with a panel of twelve lectins, in combination with sialidase (s) digestion. The entire urothelium reacted with SNA, s-PNA, s-SBA, Con A, GSA II in horse bladder, and also with MAL II and GSA I-B4 in the donkey one. The urothelium luminal surface bound MAL II, DBA, LTA in the horse and DBA and LTA in the donkey. In addition, the horse bladder stained with PNA, SBA and GSA I-B4 in the basal and luminal regions and with UEA I in the adluminal zone. These results demonstrate remarkable inter-specific difference of the glycoprotein pattern in the bladder urothelium of two Equine species, despite their close taxonomic vicinity. It is noteworthy that glycans binding PNA and UEA I lack in the epithelium lining the donkey urinary bladder.
Diversity of glycoconjugate pattern in the bladder urothelium of horse and donkey revealed by lectin histochemistry
DESANTIS, Salvatore;ACCOGLI, GIANLUCA;
2011-01-01
Abstract
The glycoconjugates of the mucosal surface of urinary bladder act as a barrier against invasion by pathogenic microorganisms and injury from toxic substances. Furthermore, they serve as a source of soluble urinary glycoproteins, which actively modify the urine composition. Glycoconjugate pattern characterizes distinct cellular populations, cell differentiation and maturation, as well as cell morpho-functional changes. We investigated the glycan pattern in the bladder epithelium by lectin histochemistry, comparatively in the horse and donkey. Tissue fragments were fixed in 4% (w/v) neutral formalin and then embedded in paraffin wax. Sections were stained with a panel of twelve lectins, in combination with sialidase (s) digestion. The entire urothelium reacted with SNA, s-PNA, s-SBA, Con A, GSA II in horse bladder, and also with MAL II and GSA I-B4 in the donkey one. The urothelium luminal surface bound MAL II, DBA, LTA in the horse and DBA and LTA in the donkey. In addition, the horse bladder stained with PNA, SBA and GSA I-B4 in the basal and luminal regions and with UEA I in the adluminal zone. These results demonstrate remarkable inter-specific difference of the glycoprotein pattern in the bladder urothelium of two Equine species, despite their close taxonomic vicinity. It is noteworthy that glycans binding PNA and UEA I lack in the epithelium lining the donkey urinary bladder.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
