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      Renal and Urinary Glycosaminoglycans in an Experimental Model of Chronic Renal Failure in Rats

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          The present paper reports the glomerular and renal individual glycosaminoglycan levels in an experimental model of chronic renal failure (CRF) that was induced in Wistar rats by five-sixths mass ablation. Glycemia, body weight, blood systolic pressure and urinary excretions of creatinine, albumin and glycosaminoglycans were measured for 12 weeks. At the end of the experiment, the weight and the glycosaminoglycan composition of the kidneys were determined. In control rats, heparan sulfate was the main glycosaminoglycan found both in whole kidney and isolated glomeruli, with trace amounts of dermatan sulfate. Isolated glomeruli presented higher heparan sulfate concentrations than whole kidney (expressed as mg/g dry weight). In CRF rats, albuminuria appeared from the 2 week on, and dermatan sulfate and chondroitin sulfate contents of the kidney increased, whereas heparan sulfate levels remained unaltered. Changes in urine glycosaminoglycans (heparan sulfate, chondroitin sulfate and dermatan sulfate) were not statistically significant. The increase in glomerular dermatan sulfate and chondroitin sulfate observed in this experimental model could be related to the mechanisms involved in the glomerulosclerosis and proteinuria that occur in CRF.

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          Most cited references 8

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          Immunochemical quantitation of antigens by single radial immunodiffusion.

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            Matrix proteoglycans: from molecular design to cellular function.

             Renato Iozzo (1997)
            The proteoglycan superfamily now contains more than 30 full-time molecules that fulfill a variety of biological functions. Proteoglycans act as tissue organizers, influence cell growth and the maturation of specialized tissues, play a role as biological filters and modulate growth-factor activities, regulate collagen fibrillogenesis and skin tensile strength, affect tumor cell growth and invasion, and influence corneal transparency and neurite outgrowth. Additional roles, derived from studies of mutant animals, indicate that certain proteoglycans are essential to life whereas others might be redundant. The review focuses on the most recent genetic and molecular biological studies of the matrix proteoglycans, broadly defined as proteoglycans secreted into the pericellular matrix. Special emphasis is placed on the molecular organization of the protein core, the utilization of protein modules, the gene structure and transcriptional control, and the functional roles of the various proteoglycans. When possible, proteoglycans have been grouped into distinct gene families and subfamilies offering a simplified nomenclature based on their protein core design. The structure-function relationship of some paradigmatic proteoglycans is discussed in depth and novel aspects of their biology are examined.
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              Decorin, biglycan and their endocytosis receptor in rat renal cortex.

              Among the small proteoglycans, biglycan and decorin have been proposed to be potent modulators of TGF-beta-mediated inflammatory kidney diseases. They were considered to become induced during glomerulonephritis and to subsequently inactivate the cytokine. Decorin and biglycan as well as their endocytosis receptor were investigated in normal rat renal cortex, in anti-Thy-1 glomerulonephritis, in polycystic kidneys, in the remnant kidney following 5/6-nephrectomy, and in kidneys from the Milan normotensive strain by immunohistochemistry and in situ hybridization. Northern blots were used for the detection of mRNA expression for decorin and biglycan in isolated glomeruli. Functional aspects of the endocytosis of decorin and biglycan were studied in cultured mesangial cells. In the normal adult rat kidney decorin was expressed preferentially by Bowman's capsule and by interstitial connective tissue cells, but only in trace amounts by mesangial cells. In contrast, biglycan was found in tubular epithelial cells, in association with glomerular capillaries, podocytes and occasionally in the mesangium. In the tubulointerstitium of diseased kidneys (polycystic kidneys, 5/6-nephrectomy, kidneys from the Milan normotensive strain) there was a general up-regulation of decorin expression, while biglycan was localized only in distinct foci of fibrotic lesions. Glomerulosclerosis (5/6-nephrectomy, Milan normotensive strain) was associated with an increased staining for both decorin and biglycan within glomeruli. However, even in the anti-Thy-1 model of an acute mesangioproliferative glomerulonephritis where the greatest accumulation of decorin was found there was only a slight enhancement of decorin mRNA in isolated glomeruli. Decorin and biglycan become degraded upon receptor-mediated endocytosis. Immunohistochemical investigations indicated that the pattern of expression of the receptor protein correlated well with the immunolocalization of both decorin and biglycan. In vitro experiments with cultured mesangial cells provided direct evidence for the expression of the receptor and for the cell's capability to endocytose decorin as well as biglycan. Decorin and biglycan are characterized by a distinct expression pattern in the normal rat kidney, whereas the presence of their endocytosis receptor protein correlates with the expression of both proteoglycans. Decorin is almost completely absent in the normal mesangium. Both proteoglycans become up-regulated in various models of renal disease. The mesangial accumulation of decorin in the anti-Thy-1 glomerulonephritis that is observed in spite of the only slightly enhanced mRNA expression could result from decreased decorin turnover and/or increased mesangial retention.

                Author and article information

                Nephron Exp Nephrol
                Cardiorenal Medicine
                S. Karger AG
                October 2000
                06 October 2000
                : 9
                : 1
                : 40-48
                aDisciplina de Biologia Molecular, Departamento de Bioquímica, and bDisciplina de Nefrologia, Departamento de Medicina, Universidade Federal de São Paulo, Escola Paulista de Medicina, São Paulo, Brazil
                20706 Exp Nephrol 2001;9:40–48
                © 2000 S. Karger AG, Basel

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                Page count
                Figures: 6, Tables: 4, References: 43, Pages: 9
                Self URI (application/pdf): https://www.karger.com/Article/Pdf/20706
                Original Paper

                Cardiovascular Medicine, Nephrology

                Chronic renal failure, Glycosaminoglycans, Kidney, Glomerulus


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