Summary
Glycation involves both circulating proteins, such as albumin, and structural proteins, such as the components of the glomerular basement membrane. A preferential excretion of glycated albumin (more anionic at physiological pH compared with unmodified plasma albumin) has been reported by some authors, but not by others. We therefore investigated the selectivity index (renal clearance of non-glycated albumin/clearance of glycated albumin) in 25 insulin-dependent diabetic patients with normal urinary albumin excretion and in 19 well-matched control subjects. The selectivity index was significantly higher in diabetic patients than in control subjects: 1.38±0.05 SEMvs 0.98±0.02, p<0.0001. This result is not consistent with a preferential urinary excretion of glycated albumin, at least in normoalbuminuric uncomplicated insulin-dependent diabetic patients.
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Bertolatus J. A., Abuyouset M., Hunsicker L. G.: Glomerular sieving of high molecular weight proteins in proteinuric rats—Kidney int.31, 1257–1266, 1987.
Brownlee M., Pongor S., Cerami A.: Covalent attachment of soluble proteins by nonenzymatically glycosylated collagen: role in thein situ formation of immune complexes—J. exp. Med.138, 1739–1744, 1983.
Brownlee M., Vlassara H., Cerami A.: Nonenzymatic glycosylation and the pathogenesis of diabetic complications—Ann. intern. Med.101, 527–537, 1984.
Cecchini G., Calefato V., Chiambretti A., Cavallo M., Dianzani M. U., Vitelli A.: Glycosylated serum albumin: high performance liquid chromatography (HPLC) evaluation in normal and diabetic patients—IRCS med. Sci.14, 1027–1028, 1986.
Christensen E. I., Carone F. A., Rennke H. C.: Effect of molecular charge on endocytic uptake of ferritin in renal proximal tubule cells—Lab. Invest.44, 351–358, 1981.
Christensen E. I., Rennke H. C., Carone F. A.: Renal tubular uptake of protein: effect of molecular charge—Amer. J. Physiol244, F436-F441, 1983.
Cohen M. P., Urdanivia E., Surma M., Wu V.-Y.: Increased glycosylation of glomerular basement membrane collagen in diabetes—Biophys. Res. Commun.95, 765–769, 1980.
Day J. F., Thorpe S. R., Baynes J. W.: Nonenzymatically glycosylated albumin—J. biol. Chem.254, 595–597, 1979.
Fabini D. L., Ertingshausen C.: Automated reaction-rate method for determination of serum creatinine with the CentrifiChem—Clin. Chem.17, 696–700, 1971.
Ghiggeri G. M., Candiano G., Delfino G., Bianchini F., Queirolo C.: Glycosyl albumin and diabetic microalbuminuria: demonstration of an altered renal handling—Kidney int.25, 565–570, 1984.
Ghiggeri G. M., Candiano G., Delfino G., Queirolo C.: Electrical charge of serum and urinary albumin in normal and diabetic humans—Kidney int.28, 168–177, 1985.
Gragnoli G., Signorini A. M., Tanganelli I.: Non-enzymatic glycosylation of urinary proteins in type I (insulin-dependent) diabetes: correlation with metabolic control and the degree of proteinuria—Diabetologia26, 411–414, 1984.
Kanwar Y. S., Rosenzweig L. J.: Clogging of the glomerular basement membrane—J. cell. Biol.93, 489–494, 1982.
Kennedy L., Baynes J. W.: Non-enzymatic glycosylation and the chronic complications of diabetes: an overview—Diabetologia26, 93–98, 1984.
Kennedy L., Mehl T. D., Riley W. J., Merimee T. J.: Non-enzymatically glycosylated serum proteins in diabetes mellitus: an index of short term glycemia—Diabetologia21, 94–98, 1981.
Krempf M., Marre M.: La microalbuminurie chez les diabétiques. I.—Définition, intérêt et physiopathologie—Diabète et Metabol.13, 225–231, 1987.
Kverneland A., Feldt-Rasmussen B., Vidal P., Welinder B., Bent-Hansen L., Soegaard U., Deckert T.: Evidence of changes in renal charge selectivity in patients with type 1 (insulin-dependent) diabetes mellitus—Diabetologia29, 634–639, 1986.
Kverneland A., Welinder B., Feldt-Rasmussen B., Deckert T.: Improved metabolic control does not alter the charge-dependent glomerular filtration of albumin in uncomplicated type 1 (insulin-dependent) diabetes—Diabetologia31, 708–710, 1988.
Melvin T., Kim Y., Michael A. F.: Selective binding of IgG4 and other negatively charged plasma proteins in normal and diabetic human kidneys—Amer. J. Pathol.115, 443–446, 1994.
Michael A. F., Brown D. M.: Increased concentration of albumin in kidney basement membranes in diabetes mellitus—Diabetes30, 843–846, 1981.
Michelis L. D., Davidman M., Keane W. E.: Glomerular permeability to neutral and anionic dextrans in experimental diabetes—Kidney int.21, 699–705, 1982.
Schleicher E., Wieland O. H.: Specific quantitation by HPLC of protein (Lysine) bound glucose in human serum albumin and other glycosylated proteins—J. clin. Chem. clin. Biochem.19, 81–87, 1981.
Schleicher E., Wieland E.: Changes of human glomerular basement membrane in diabetes mellitus—J. clin. Chem. clin. Biochem.22, 223–227, 1984.
Sumpio B. E., Maack T.: Kinetics, competition and selectivity of tubular absorption of proteins —Amer. J. Physiol.243, 379–392, 1982.
Tarsio J. F., Wigness B., Rhode T. D., Rupp W. M., Buchwald H., Furcht L. T.: Nonenzymatic glycation of fibronectin and alterations of cell matrix and basement membrane components in diabetes mellitus—Diabetes34, 477–484, 1985.
Tetta C., Cavallo-Perin P., Roggero S., Malavasii ?., Estivi P., Triolo G., Camussi G., Pagano G.: Exercise-induced microalbuminuria in diabetes is associated with the urinary excretion of cationic proteins—Clin. Nephrol.30, 270–275, 1988.
Wahl P., Deppermann D., Hasslacher C.: Biochemistry of glomerular basement membrane of the normal and diabetic human—Kidney int.21, 744–749, 1982.
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Pagano, G., Chiambretti, A., Calefato, V. et al. Urinary excretion of glycated albumin in insulin-dependent diabetic patients with normal urinary albumin excretion. Acta diabet. lat 28, 39–45 (1991). https://doi.org/10.1007/BF02732112
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DOI: https://doi.org/10.1007/BF02732112