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Departments of Internal Medicine and Pediatrics, University of Texas Medical Branch at Galveston, Galveston, Texas 77555
The polymeric immunoglobulin receptor (pIgR) transports polymeric immunoglobulins (IgA) from the basolateral to the apical surface of epithelial cells. At the apical surface, its amino-terminal domain, termed secretory component (SC), is proteolytically cleaved and released either unbound (free SC) or bound to IgA. We examined the effects of changes in water balance and vasopressin on the production and secretion of the pIgR in the rat kidney in vivo. Water deprivation induced a 2.7-fold increase in the pIgR mRNA and a 2.2-fold increase in intracellular pIgR protein compared with water-loaded animals. Physiological doses of desmopressin reproduced the effects of water deprivation on mRNA and intracellular protein levels, suggesting that pIgR expression may be regulated by a vasopressin-coupled mechanism. Secretion of free SC and secretory IgA in the urine, however, correlated directly with water intake and urine flow. These results suggest that hydration status and vasopressin may affect the mucosal immunity of the kidney by regulating at different steps the epithelial cell production and secretion of the polymeric immunoglobulin transporter/secretory component.
secretory component; hyperosmolar; mucosal immunity; pIgR messenger ribonucleic acid; desmopressin
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J. C. Rice, J. S. Spence, J. Megyesi, R. M. Goldblum, and R. L. Safirstein Expression of the polymeric immunoglobulin receptor and excretion of secretory IgA in the postischemic kidney Am J Physiol Renal Physiol, May 1, 1999; 276(5): F666 - F673. [Abstract] [Full Text] [PDF] |
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