BIBLIOGRAFIA
[1] Poon TC, Johnson PJ. Proteome analysis and its impact on the discovery of serological tumormarkers. Clin Chim Acta. 2001, 313: 231239.
[2] Piccolomini F. Impiego delle tecniche proteomiche nello studio del pattern proteico del siero di pazienti nefropatici con insufficienza renale cronica. Tesi di Lurea, 2006.
[3] Bianchi C, Donadio C, Tramonti G, Consani C, Lorusso P, Rossi G. Reappraisal of serum beta2-microglobulin as marker of GFR. Ren Fail. 2001, 23: 419-429.
[4] Kanwar YS. Biology of disease: Biophysiology of glomerular filtration and proteinuria. Lab Invest. 1984, 51: 7-21.
[5] Verroust P, Ronco PM, Chatelet F. Monoclonal antibodies and identification of glomerular antigens. Kidney Int. 1986, 30: 649-655.
[6] Takami H, Naramoto A, Shigematsu H, Ohno S. Ultrastructure of glomerular basement membrane by quick-freeze and deep-etch methods. Kidney Int. 1991, 39:
659-664.
[7] Rodewald R, Karnovsky MJ. Porous structure of glomeular slit diaphragm in the rat and mouse. J Cell Biol. 1974, 60: 423-433.
[8] Brenner BM, Bohrer MP, Baylis C, Deen WM. Determinants of glomerular permeselectivity: Insights derived from observation in vivo. Kidney Int. 1977, 12:
229-237.
[9] Bohrer MP, Baylis C, Humes HD, Glassock RJ, Robertson CR, Brenner MB.
Permeselectivity of the glomerular capillary wall: Facilitated filtration of circulating polycations. J Clin Invest. 1978, 61: 72-78.
[10] Kanwar YS, Farquhar MG. Presence of heparin sul fate in the glomerular basement membrane. Procl Natl Acad Sci USA. 1979, 76: 1303-1307.
[11] Kanwar YS, Farquhar MG. Anionic sites in the glomerular basement membrane: In vitro and in vivo localization to the lamina rarae by cationic probes. J Cell Biol.
1979, 81: 137-153.
[12] Martinez-Hernandez A, Amenta PS. The basement membrane in pathology. Lab Invest. 1983, 48: 656-677.
[13] Rennke HG, Cotran RS, Venkatachalam MA. Role of glomerular charge in glomerular permeability. Tracer studies with cationized ferritins. J Cell Biol. 1975, 67: 638-646.
[14] Groggel GC, Stevenson J, Hovingh P, Linker A, Border WA. Charges in heparin sulfate correlate with increased glomerular permeability. Kidney Int. 1988, 33: 517- 523.
[15] Kanwar YS, Farquhar MG. Detachment of endothelium and epithelium from the glomerular basement membrane produced by kidney perfusion with neuraminidase.
Lab Invest. 1980, 42: 375-384.
[16] Latta H, Johnston WH, Stanley TM. Sialoglycoproteins and filtration barriers in the glomerular capillary wall. J Ultrastruct Res. 1975, 51: 354-376.
[17] Mohos SC, Skoza L. Histochemical demonstration and localization of sialoproteins in the glomerulus. Exp Mol Pathol. 1970, 12: 316-323.
[18] Kerjaschki D, Sharkey DJ, Farquhar MG. Identification and characterization of podocalyxin – the major sialoglycoprotein of the renal glomerular epithelial. J Cell Biol. 1982, 98: 1591-1596.
[19] Seiler MW, Rennke HG, Venkatachalam MA, Cotran RS. Pathogenesis of polycation-induced alterations (“fusion”) of glomerular epithelium. Lab Invest.
1977, 36: 48-61.
[20] Bennet CM, Glassock RJ, Chang RL, Deen WM, Robertson CR, Brenner BM, Troy JL, Ueki IR, Rasmussen B. Permeselectivity of the glomerular capillary wall.
Studies of experimental glomerulonephritis in the rat using dextran sulfate. J Clin Invest. 1976, 57: 1287-1294.
[21] Mayer G, Lafayette RA, Oliver J, Deen WM, Myers BD, Meyer TW. Effects of angiotensin II receptor blokade on remnant glomerular permeselectivity. Kidney Int.
1993, 43: 346-353.
[22] Hunsicker LG, Shearer TP, Shaffer SJ. Acute reversible proteinuria induced by infusion of the polycation hexadimethrine. Kidey Int. 1981, 20: 7-17.
[23] Ryan GB. The glomerular sieve and the mechanism of proteinuria. Aust N Z J Med.
1981, 11: 197-206.
[24] Bohrer MP, Deen WM, Robertson CR, Brenner BM. Mechanism of angiotensin II- induced proteinuria in the rat. Am J Physiol. 1977, 233: 13-21.
[25] Eisenbach GM, Liew JB, Boylan JW, Manz N, Muir P. Effect of angiotensin on the filtration of protein in the rat kidney: a micropuncture study. Kidney Int. 1975, 8:
80-87.
[26] Loon N, Shemesh O, Morelli E, Myers BD. Effect of angiotensin II infusion on the human glomerular filtration barrier. Am J Physiol. 1989, 257: 608-614.
[27] Hegg JE, de Jong PE, van der Hem GK, de Zeeuw D. Reduction of proteinuria by angiotensin convertine enzyme inhibition. Kidney Int. 1987, 32: 78-83.
[28] Ryan GB, Karnovsky MJ. Distribution of endogenous albumin in the rat glomerulus: role of hemodynamic factors in glomerular barrier function. Kidney Int.
1976, 9: 36-45.
[29] Yoshioka T, Mitarai T, kon V, Deen WM, Rennke HG, Ichikawa I. Role for angiotensin II in an overt functional proteinuria. . Kidney Int. 1986, 30: 538-545.
[30] Lianos EA. Eicosanoids and the modulation of glomerular immune injury. Kidney Int. 1989, 35: 985-992.
[31] Deen WM, Bridges CR, Brenner BM, Myers BD. Heteroporous model of glomerular size selectivity: application to normal and nephrotic humans. AmJ physiol. 1985, 18: F374-F389.
[32] Stryer L. Biochimica 2002, 9: 263,269.
[33] Myers BD, Okarma TB, Friedman S, Bridges C, Ross J, Asseff S, Deen WM.
Mechanism of proteinuria in human glomerulonephritis. J Clin Invest. 1982, 70:
732-746.
[34] Marre M, Bouhanick B, Berrut G. Microalbuminuria. Current Opinion in Nephrology and Hypertension. 1994, 3: 558-563.
[35] Ala-Houhala I, Koskinen M, Ahola T, Harmoinen A, Kouri T, Laurila K, Mustonen J, Pasternack A. Increased glomerular permeability in patients with nephropathia epidemica caused by Puumala hantavirus. Nephrol Dial Transplant. 2002, 17: 246- 252.
[36] Grant GH. The protein of normal urine; II. From the urinary tract. J Clin .Pathol.
1959, 12: 510-517.
[37] Tamm I, Horsfall FL. Characterization and separation of an Inhibitor of Viral Hemagglutination Present in Urine. Proceedings of the Society of Experimental Biology and Medicine. 1950, 74: 108-114.
[38] Hunt JS, McGiven AR, Groufsky A, Lynn KL, Taylor MC. Affinity-purified antibodies of defined specificità for use in a solid-phase miroplate radioimmunoassay of human Tamm-Horsfall glycoprotein in urine. Biochem J.
1985, 227: 957-963.
[39] McKenzi JK, Patel R, McQueen EG. The excretion rate of tamm-horsfall urinary mucoprotein in normals and in patients with renal disease. Australs Ann Med. 1964, 13: 32-39.
[40] Mogensen CE, Solling. Studies on renal tubular protein reabsorption: partial and near complete inhibition by certain amino acids. Scand J Clin Lab Invest. 1977, 37:
477-486.
[41] Bordeau JE, Carone FA, Gante CE. Serum albumin uptake in isolated perfused renal tubules. Quantitative and electron microscope radioautographic studies in three anatomical segments of the rabbit nephron. J Cell Biol. 1972, 54: 382-398.
[42] Madsen KM, Park CH. Lysosome distribution and cathepsin B and L activity along the rabbit proximal tubule. Am J Physiol. 1987, 253: 1290-1301.
[43] Maack T, Johnson V, Kau ST, Figueiredo J, Sigulem D. Renal filtration, transport, and metabolism of low-molecular-weight proteins: a review. Kidney Int. 1979, 16:
251-270.
[44] Rennke HG, Venkatachalam MA. Glomerular permeability of macromolecules:
effect of molecular configuration on the fractional clearance of uncharged dextran and neutral horseradish peroxidase in the rat. J Clin Invest. 1979, 63: 713-717.
[45] Brenner BM, Hostetter TH, Humes HD. Molecular basis of proteinuria of glomerular origin. N Engl J Med. 1978, 298: 826-833.
[46] Deen WM, Bohrer MP,Brenner BM. Macromolecole transport across glomerular capillaries: application of pore theory. Kidney Int. 1979, 16: 353-365.
[47] Abuelo JG. Proteinuria: diagnostic principles and procedures. Ann Intern Med.
1983, 98: 186-191.
[48] Wolvius D, Verschure JC. The diagnostic value of the protein excretion pattern in various types of proteinuria. J Clin Pathol. 1957, 10: 80-83.
[49] Boesken WH, Kopf K, Schollmeyer P. Differentiation of proteinuric diseases by discelectrophoretic molecular weight analysis of urinary proteins. Clin Nephrol.
1973, 1: 311-318.
[50] Waldmann TA, Strober W, Mogielnicki RP. The renal handling of low molecular weight proteins. II. Disorders of serum protein catabolism in patients with tubular proteinuria, the nephrotic syndrome, or uremia. J Clin Invest. 1972, 51: 2162-2174.
[51] Dirks JH, Clapp JR, Berliner RW. The protein concentration in the proximal tubule of the dog. J Clin Invest. 1964, 43: 916-921.
[52] Mcgarry E, Sehon AH, Rose B. The isolation and electrophoretic characterization of the protein in the urine of normal subjects. J Clin Invest. 1955, 34: 832-844.
[53] Oken DE, Flamenbaum W. Micropuncture studies of proximal tubule albumin concentrations in normal and nephrotic rats. . J Clin Invest. 1971, 50: 1498-1505.
[54] Van Liew JB, Buentig W, Stolte H, Boylan JW. Protein excretion: micropunture study of rat capsular and proximal tebule fluid. Am j Physiol. 1970, 219: 299-305.
[55] Oken DE, Cotes SC, Mende CW. Micropuncture study of tubular transport of albumin in rats with aminonucleoside nephrosis. Kidney Int. 1972, 1: 3-11.
[56] Oken DE, Kirschbaum BB, Landwehr DM. Micropuncture studies of the mechanisms of normal and pathologic albuminuria. Contrib Nephrol. 1981, 24: 1-7.
[57] Corteney MA, Sawin LL, Weiss DD. Renal tubular protein absorption in the rat. J Clim Invest. 1970, 49: 1-4.
[58] Katz J, Rosenfeld S, Sellers AL. Role of the kidney in plasma albumin catabolism.
Am J Physiol. 1960, 198: 814-818.
[59] Oliver J, Macdowell M, Lee YC. Cellular mechanism of protein metabolism in the nephron. I. The structural aspects of proteinuria; tubular absorption, droplet formation, and the disposal of proteins. J Exp Med. 1954, 99: 589-604.
[60] Maunsbach AB. Absorption of I-125-labeled homologous albumin by rat kidney proximal tubule cells. A study of microperfused single proximal tubules by electrn microscopic autoradiography and histochemistry. J Ultrastruct Res. 1966, 15: 197- 241.
[61] Miller F, Palede GE. Lytic activities in renal protein absorption droplets. An electron microscopical cytochemical study. J Cell Biol. 1964, 23: 519-552.
[62] Strass W. Cytochemical observations on the relationship between lysosomes and phagosomes in kidney and liver by combined staining for acid phosphatase and intravenously injected horseradish peroxidase. J Am Soc Nephrol. 2001, 12: 2528- 2537.
[63] Minghetti PP, Ruffner DE, Kuang WJ, Dennison OE, Hawkins JW, Beattie WG, Dugaiczyk A. Molecular structure of the human albumin gene is revealed by nucleotide sequenze within q11-22 of chromosome 4. J Biol Chem. 1986, 261:
6747-6757.
[64] Peters TJ. All about albumin. Biochemistry, Genetics, and Medical Applications.
San Diego, Academic Press. 1996.
[65] Peters TJ. Serum albumin. Adv Protein Chem. 1985, 37: 161-245.
[66] Curry S, Brick P, Franks NP. Fatty acid binding to human serum albumin: new insights from crystallographic studies. Biochim Biophys Acta. 2001, 1441: 131-140.
[67] Era S, Kuwata K, Imai H, Nakamura K, Hayashi T, Sogami M. Age-related in redox state of human serum albumin. Biochim Biophys Acta. 1995, 1247: 12-16.
[68] Gryzunov YA, Arroyo A, Vigne J-L, Zhao Q, Tyurin VA, Hubel CA, Gandley RE, Vladimirov YA, Taylor RN, Kagan VE. Binding of fatty acids facilities oxidaion of cysteine-34 and converts copper-albumin complexs from antioxidants to prooxidants. Archives of Biochemistry and Biophysics. 2003, 413: 53-66.
[60] Bar-Or D, Thomas GW, Rael LT, Lau LT, Winkler JV. Asp-Ala-His-Lys (DAHK) inhibits copper-induced oxidative DNA double strand breaks and telomere shortening. Biochemical and Biophysical Research Communications. 2001, 282:
356-360.
[70] Brennan SO, Arai K, Madison J, Laurell CB, Galliano M, Watkins S, Peach R, Myles T, Gorge P, Putnam FW. Hypermutability of CpG dinucleotides in the propeptide-encoding sequenze of the human albumin gene. Pro Nat Acad Sci USA.
1990, 87: 3909-3913.
[71] Madison J, Galliano M, Watkins S, Minchiotti L, Porta F, Rossi A, Putnam FW.
Genetic variants of human serum albumin in Italy: point mutants and a carboxyl- terminal variant. Proc Natl Acad Sci USA. 1994, 91: 6476-6480.
[72] Kragh-Hansen U, Pedersen AO, Galliano M, Minchiotti L, Brennan SO, Tarnoky L, H.L.P. Franco M, Salzano MF. High-affinity binding of laurate to naturally occurring mutants of human serum albumin and proalbumin. Biochem J. 1996, 320: 911-916.
[73] Chua EK, Brennan SO, George PM. Albumin Church Bay: Lys>Glu a new mutation detected by electrospray ionisation mass spectrometry. Biochim Biophys Acta. 1998, 1382: 305-310.
[74] Arai K, Huss K, Madison J, Putnam FW, Salzano FM, H.L.P. Franco M, S.E.B.
Santos, Freitas MJM. Amino acid substitutions in albumin variants found in Brazil.
Proc Natl Acad Sci USA. 1989, 86: 1821-1825.
[75] Takahashi N, Takahashi Y, Toshiaki I, Putnam FW, Fujita M, Satoh C, Neel JV.
Amino acid substitutions in inherited albumin variants from Amerindian and Japanese populations. Proc Natl Acad Sci USA. 1987, 84: 8001-8005.
