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      Urinary Podocytes in Primary Focal Segmental Glomerulosclerosis

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          Background/Aim: Focal segmental glomerulosclerosis (FSGS) is a common cause of nephrotic syndrome. Although the pathogenesis is not known, recent studies suggest that FSGS may be a podocyte disease. The aim of this study was to look for podocyte injury in this disease, using measurements of urinary podocytes. Methods: We examined the first morning urine of the day collected from 71 patients (45 men and 26 women, median age and range 11.2 and 3–29 years) diagnosed as having nephrotic syndrome. Freshly voided urine samples were examined by immunofluorescence labeling using monoclonal antibodies against human podocalyxin. Renal histological examinations were performed in 58 of the 71 patients: 28 had minimal-change disease, 20 had FSGS, and 10 had membranous nephropathy. Results: Median and range of urinary podocytes measured were 0.2 and 0–40.8 cells/ml for 71 patients with nephrotic syndrome and 0 and 0–0.8 cells/ml for normal healthy control subjects (n = 200). Patients with FSGS had significantly higher levels of urinary podocytes (median and range 1.3 and 0–40.8 cells/ml) than those with minimal-change disease (median and range 0 and 0–6.9 cells/m; p = 0.003) or membranous nephropathy (median and range 0 and 0–1.4 cells/ml; p = 0.02). Conclusions: The urinary excretion of podocytes is significantly higher in patients with FSGS as compared with those having membranous nephropathy or minimal-change disease. These findings suggest that podocyte injury and loss in the urine may have an important role in the pathogenesis of FSGS.

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          Molecular cloning of cDNAs encoding human GLEPP1, a membrane protein tyrosine phosphatase: characterization of the GLEPP1 protein distribution in human kidney and assignment of the GLEPP1 gene to human chromosome 12p12-p13.

          Human glomerular epithelial protein 1 (GLEPP1), a receptor-like membrane protein tyrosine phosphatase (PTPase), was cloned and sequenced from a human renal cortical cDNA library. The human nucleotide and derived amino acid sequences were, respectively, 90 and 97% identical to those of rabbit. Human GLEPP1 is predicted to contain 1188 amino acids. The predicted mature protein is 1159 amino acids long and contains a large extracellular domain, a single transmembrane domain, and a single intracellular PTPase domain. Monoclonal and polyclonal antibodies raised against a human GLEPP1 fusion protein recognized a protein with distribution restricted to the glomerulus in human kidney and with an apparent molecular weight of approximately 200 kDa. The GLEPP1 gene was assigned to human chromosome 12p12-p13 by fluorescence in situ hybridization.

            Author and article information

            S. Karger AG
            10 October 2001
            : 89
            : 3
            : 342-347
            aDepartment of Pediatrics, Yoshida Hospital, Niigata, and bDepartment of Pathology, Institute of Nephrology, Niigata University, Niigata, Japan
            46097 Nephron 2001;89:342–347
            © 2001 S. Karger AG, Basel

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            Figures: 2, Tables: 1, References: 20, Pages: 6
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            Preliminary Communication


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