Functional and structural characteristics of the glycosaminoglycans of the bladder luminal surface

• Published in: The Journal of urology Vol. 138; no. 2; p. 433
• Main Authors: Hurst, R E, Rhodes, S W, Adamson, P B, Parsons, C L, Roy, J B
• Format: Journal Article
• Language: English
• Published: United States 01.08.1987
• Subjects: Animals; Bacterial Adhesion; Chromatography, Gel; Electrophoresis; Glycosaminoglycans - physiology; Glycosaminoglycans - urine; Kidney - metabolism; Mucins - analysis; Rats; Urinary Bladder - analysis; Urinary Bladder - physiology
• ISSN: 0022-5347; 1527-3792
• DOI: 10.1016/S0022-5347(17)43180-6

The glycosaminoglycan layer of bladder has been proposed to play a crucial role in protecting the bladder from harmful substances in urine. Rats were partially cystectomized to determine whether bladder glycosaminoglycans are routinely eluted from the bladder surface in detectable quantities. Cystectomy produced no detectable qualitative or quantitative changes in excreted GAG thereby showing that most urinary glycosaminoglycan originates in the kidney and not from the bladder. Damaging the glycosaminoglycan layer by a dilute acid wash, however, leads to a consistent decrease in the output of urinary GAG which recovers to normal at the same rate as the layer regenerates. This suggests that the newly exposed sites tightly bind urinary GAG. We suggest that such binding may be a component of the normal physiological defense mechanism of the bladder. The bladder glycosaminoglycan layer was isolated, dilute acid being used to elute ionically-bound material and brief trypsinization to elute intercalated proteoglycans from the luminal surface. The GAG from the luminal surface, which was present at a density of one chain per 50 nm.2 of bladder surface, was quite different in composition from that isolated from the whole bladder.