Antibacterial activity of bladder surface mucin duplicated in the rabbit bladder by exogenous glycosaminoglycan (sodium pentosanpolysulfate).
Previous data from our laboratory suggest that the transitional epithelium of the urinary bladder secretes and binds to its surface a glycosaminoglycan. The presence of this substance at the bladder surface markedly reduces the ability of microorganisms to adhere to the mucosa. Furthermore, this glycosaminoglycan can be removed (with acid) and replaced by intravesical instillation of a synthetic sulfonated glycosaminoglycan (heparin), whose presence is as effective as that of the natural glycosaminoglycan in reducing adherence. We conducted the current study with a different sulfonated glycosaminoglycan to determine whether the antiadherence activity is generalized to heparin congeners and whether the antiadherence effect of heparin is independent of its known anticoagulant activity. In this study we examined the sulfonated glycosaminoglycan, sodium pentosanpolysulfate, which lacks significant anticoagulant activity, and found it to have a mechanism of antiadherence analogous to that of heparin and almost equally as active on a weight basis.
D000818:Animals; D004926:Escherichia coli / Q000187:drug effects / Q000502:physiology*; D008297:Male; D009092:Mucous Membrane / Q000382:microbiology*; D010426:Pentosan Sulfuric Polyester / Q000494:pharmacology*; D011134:Polysaccharides / Q000494:pharmacology*; D011817:Rabbits; D001743:Urinary Bladder / Q000187:drug effects / Q000382:microbiology*
D011134:Polysaccharides; D010426:Pentosan Sulfuric Polyester