By Pere Gines
There was little or no written at the interplay of the liver and kidney. This publication addresses the expanding prevalence and importance of ailments, resembling ascites, renal disorder, cirrhosis and high blood pressure the place either organs are concerned. This textbook is key, even for proven practitioners and comprises present information about therapy and remedy for sufferers with cirrhosis and ascites, in actual fact and successfully provided by means of the head overseas specialists inside this box. the second one variation is fullyyt revised and up to date and locations better emphasis on treatment.
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Extra resources for Ascites and Renal Dysfunction in Liver Disease: Pathogenesis, Diagnosis, and Treatment
Glomerular hemodynamics in rats with chronic sodium depletion: effect of saralasin. J Clin Invest 1979; 64:503–12. Badr KF, Ichikawa I. Prerenal failure. A deleterious shift from renal compensation to decompensation. N Engl J Med 1988; 319:623–9. Lu M, Zhu Y, Balazy M et al. Effect of angiotensin II on the apical K+ channel in the thick ascending limb of the rat kidney. J Gen Physiol 1996; 108:537–47. Seikaly MG, Arant BS Jr, Seney FD Jr. Endogenous angiotensin concentrations in specific intrarenal fluid compartments of the rat.
The effects of endothelin-1 are mediated through two different receptors, ETA and ETB (72,73). One very important and unusual characteristic of ET-1 is the fact that it remains associated with its receptor for a very long period of time (up to 2 h after endocytosis in the case of ET-1 and ETA) leading to a prolonged biological effect (74). Increased sensitivity of the renal vasculature to ET-1 results from the increased density of receptors in the renal vasculature (75,76). Human kidneys have a predominance of ETB receptor over ETA, ETA receptors being localized in the vasculature and ETB in renal tubules and medulla (77,78).
The human endothelin family: three structurally and pharmacologically distinct isopeptides predicted by three separate genes. Proc Natl Acad Sci USA 1989; 86:2863–7. 62 Emoto N, Yanagisawa M. Endothelin converting enzyme2 is a membrane-bound phosphoramidon-sensitive metalloprotease with acidic pH optimum. J Biol Chem 1995; 270:15262–8. 63 Xu D, Emoto N, Giaid A et al. ECE-l: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1. Cell 1994; 78:473–85. 64 Kohan DE.