Introduction: We investigated changes of vesical gap junctions in relation to changes of the micturition reflex in rats with partial bladder-outlet obstruction (BOO).
Materials And Methods: A total of 66 female Sprague-Dawley rats were divided into six groups: sham operation (control); 3, 14, and 28 days after BOO; and 3 and 28 days after relief of BOO lasting for a three-day period. Under urethane anesthesia, isovolumetric cystometry was performed on each group. Expression of mRNA for the gap-junction protein connexin 43 (Cx43) in the bladder was measured in each group. Immunohistochemistry using Cx43 antibody was also performed on the bladder after BOO.
Results: The interval between bladder contractions was shorter in all of the other groups than in the control group. Expression of Cx43 mRNA was increased 3, 14, and 28 days after BOO (the peak increase was twofold), and three days after the relief of BOO, but it returned to the control level by 28 days after relief of BOO. Histologically, smooth muscle hypertrophy was detected in the bladder after BOO and punctate staining of the smooth muscle by Cx43 antibody increased after BOO.
Conclusion: These results suggest that partial BOO produces detrusor overactivity that may depend on increased intercellular communication via gap junctions in the bladder. Relief of BOO led to a decrease of Cx43 mRNA, but detrusor overactivity persisted in the chronic phase, suggesting a reversible change of vesical gap junctions and an irreversible change of bladder activity after BOO.
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http://dx.doi.org/10.1007/s11255-008-9516-7 | DOI Listing |
J Cell Biol
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While membrane proteins such as ion channels continuously turn over and require replacement, the mechanisms of specificity of efficient channel delivery to appropriate membrane subdomains remain poorly understood. GJA1-20k is a truncated Connexin43 (Cx43) isoform arising from translation initiating at an internal start codon within the same parent GJA1 mRNA and is requisite for full-length Cx43 trafficking to cell borders. GJA1-20k does not have a full transmembrane domain, and it is not known how GJA1-20k enables forward delivery of Cx43 hemichannels.
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