ISSN:0002-9629    

出版商:OVID    

年代:1998

数据来源: OVID

摘要:

The recent identification of aquaporin water channel proteins has provided detailed information about the molecular basis for transepithelial water transport. At least five aquaporins have been identified in the kidney; they have provided detailed molecular insight into the fundamental physiology of water balance. This article focuses primarily on the physiology and pathophysiologic significance of the vasopressin-regulated water channel aquaporin-2 (AQP2) in a number of conditions where body water balance is disturbed. AQP2 is regulated by vasopressin by both short- and long-term mechanisms. Acutely, vasopressin induces exocytic insertion of AQP2 into the apical plasma membrane to increase collecting duct water reabsorption. Moreover, long-term regulation of body water balance is achieved by changes in total collecting duct levels of AQP2. Recent studies have documented that both vasopressin and vasopressin-independent regulation play important roles in this. In conditions with acquired nephrogenic diabetes insipidus (eg, lithium treatment, hypokalemia, postobstructive polyuria), AQP2 expression and targeting have been found to be markedly reduced, providing an explanation for the polyuria and the inability to concentrate urine associated with these conditions. Conversely, in conditions with water retention (eg, heart failure, pregnancy), it has been shown that AQP2 levels and plasma membrane targeting are increased. Continued analysis of aquaporins is providing detailed molecular insight into the physiology and pathophysiology of water balance disorders.

ISSN:0002-9629    

出版商:OVID    

年代:1998

数据来源: OVID

摘要:

The regulation of water excretion by the kidney is one of the few physiologic processes that are prominent in everyday life. This process predominantly occurs in renal collecting duct cells, where transcellular water reabsorption is induced after binding of the pituitary hormone arginine-vasopressin to its vasopressin type-2 receptor and the subsequent insertion of aquaporin-2 (AQP2) water channels in the apical membrane of these cells. Removal of the hormone triggers endocytosis of AQP2 and restores the water-impermeable state of the collecting duct cells. Nephrogenic diabetes insipidus is characterized by the inability of the kidney to concentrate urine in response to vasopressin; the vasopressin type-2 receptor and the AQP2 water channel have both been shown to be involved in this disease. This article focuses on mutations in the vasopressin V2receptor and aquaporin-2 water channel identified in nephrogenic diabetes insipidus patients, and on the effects of these mutations on the transport and function of these proteins upon expression in cell systems.

ISSN:0002-9629    

出版商:OVID    

年代:1998

数据来源: OVID

摘要:

Several aquaporin-type water channels are expressed in mammalian kidney and lung: AQP1 in lung microvessels and kidney proximal tubule, thin descending limb of Henle, and vasa recta; AQP2 in apical membrane of collecting duct epithelium; AQP3 and AQP4 in basolateral membranes of airway and collecting duct epithelium; and AQP5 in alveolar epithelium. Novel quantitative fluorescence methods demonstrated very high water permeabilities of the alveolar epithelial and endothelial barriers, and moderately high water permeability across distal airways. In the kidney, water permeability is high in proximal tubule and thin descending limb of Henle, and regulated by vasopressin in collecting duct. The author's laboratory has studied the role of aquaporins in organ physiology using transgenic knockout mice lacking specific aquaporins. AQP1 null mice are mildly growth-retarded, manifest a severe urinary concentrating defect, and have reduced water permeability between air-space and capillary compartments. AQP4 null mice appear normal grossly except for a mild defect in maximum urinary concentrating ability. AQP2-deficient humans have hereditary non-X-linked nephrogenic diabetes insipidus (NDI). In transfected mammalian cells, many NDI-causing AQP2 mutants are retained in the endoplasmic reticulum. The author's laboratory has found that "chemical chaperones," that is, small compounds that promote protein folding in vitro, are able to correct defective AQP2 trafficking in cell culture models. The transenic mouse and mammalian cell models are thus beginning to provide clues about the role of aquaporins in normal physiology and disease.

ISSN:0002-9629    

出版商:OVID    

年代:1998

数据来源: OVID

摘要:

Traditionally, arginine vasopressin modulation of renal water, sodium, and urea excretion has been considered somewhat in isolation from factors that control divalent mineral ion homeostasis. Similarly, previous considerations of divalent mineral ion metabolism have focused mainly on the role of hormones, eg, parathyroid hormone and various forms of vitamin D, as principal modifiers of renal calcium handling. Recent data, however, have now suggested the existence of novel linkages that coordinate control of water and divalent mineral ion homeostasis. This article summarizes these data and highlights the fundamental roles of the extracellular calcium polyvalent cation-sensing receptor (CaR) as an integrator of water and divalent mineral ion homeostasis on a cellular, organ-specific, and whole-body basis. Organs where CaRs may integrate water and divalent mineral ion metabolism include endocrine tissues that express CaRs, the brain, various nephron segments of the kidney, bone, and the gastrointestinal tract. These new data suggest that considerable regulatory overlap exists between water and divalent mineral ion homeostasis.

ISSN:0002-9629    

出版商:OVID    

年代:1998

数据来源: OVID

ISSN:0002-9629    

出版商:OVID    

年代:1998

数据来源: OVID

ISSN:0002-9629    

出版商:OVID    

年代:1998

数据来源: OVID

ISSN:0002-9629    

出版商:OVID    

年代:1998

数据来源: OVID

ISSN:0002-9629    

出版商:OVID    

年代:1998

数据来源: OVID

ISSN:0002-9629    

出版商:OVID    

年代:1998

数据来源: OVID