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      Molecular Interactions between Albumin and Proximal Tubular Cells

      Cardiorenal Medicine

      S. Karger AG

      Endocytosis, Proteinuria, Albumin receptor, Proximal tubule

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          In glomerular diseases the filtration of excess proteins into the proximal tubule, together with their subsequent reabsorption may represent an important pathological mechanism underlying progressive renal scarring. The most prominent protein in glomerular filtrate, albumin, is reabsorbed by receptor-mediated endocytosis by proximal tubular cells. It binds both to scavenger-type receptors and to megalin in the proximal tubule. Some of these receptors appear to be shared with other cell types, particularly endothelial cells. The endocytic uptake of albumin is subjected to complex hormonal and enzymatic regulation. In addition to being reabsorbed in the proximal tubule, albumin may act as a signalling molecule in these cells, and may induce the expression of numerous pro-inflammatory genes. Modulation of the interaction of albumin with proximal tubular cells may eventually prove to be of therapeutic importance in the treatment of renal diseases.

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          Characteristics of albumin binding to opossum kidney cells and identification of potential receptors.

          Albumin re-absorption in the kidney proximal tubule may be pathophysiological in disease. Opossum kidney (OK) cell monolayers were used to investigate the characteristics of [125I]-labelled albumin binding at 4 degrees C. Two binding sites were identified, one with high affinity (KD 154.8 +/-7 mg/l) and low capacity, the other with low affinity (KD 8300 +/- 1000 mg/l) and high capacity. Binding was sensitive to lectins Glycine max and Ulex europaeus I, but not other lectins, indicating involvement of a glycoprotein(s) in the binding process. Binding was also sensitive to a number of agents known to inhibit binding to scavenger receptors. [125I]-Labelled albumin ligand blotting of OK cell membrane proteins identified several albumin-binding proteins with identical lectin affinities to those proteins mediating albumin binding to OK cell monolayers. These results provide initial evidence of the identity of albumin receptors in kidney tubules, and suggest that they may be members of the family of scavenger receptors.

            Author and article information

            Nephron Exp Nephrol
            Cardiorenal Medicine
            S. Karger AG
            December 1998
            06 November 1998
            : 6
            : 6
            : 491-495
            Departments of Nephrology, and Cell Physiology and Pharmacology, Leicester University Medical School, Leicester, UK
            20562 Exp Nephrol 1998;6:491–495
            © 1998 S. Karger AG, Basel

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            Page count
            Figures: 1, Tables: 1, References: 23, Pages: 5
            Self URI (application/pdf): https://www.karger.com/Article/Pdf/20562

            Cardiovascular Medicine, Nephrology

            Proteinuria, Proximal tubule, Endocytosis, Albumin receptor


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