Accumulation of albumin-linked and free-form pentosidine in the circulation of uremic patients with end-stage renal failure: renal implications in the pathophysiology of pentosidine.

Pentosidine is an advanced glycation end product and its formation is shown to be closely related to oxidative processes. Recent studies have shown that pentosidine levels are increased not only in plasma and matrix proteins from diabetic patients, but also markedly in nondiabetic hemodialysis patients. Currently, the mechanism of accumulation and kinetics of pentosidine formation in hemodialysis patients remain unknown. Gel filtration of uremic plasma revealed that plasma pentosidine exists in the albumin fraction (approximately 90%) and, interestingly, in free form (approximately 5%) as well. Plasma free pentosidine was undetectable in subjects with normal renal function. There was a significant correlation between the plasma levels of albumin-linked and free pentosidine in hemodialysis patients. Kinetic studies indicated that dietary pentosidine was absorbed into the circulation and that, after either oral or intravenous administration of pentosidine to intact or nephrectomized rats, the plasma free pentosidine level was closely linked to the level of renal function. These findings demonstrate that: (1) Pentosidine accumulates as albumin-linked and in free form in the circulation of uremic patients; (2) dietary pentosidine can be absorbed into the circulation, thus being one possible origin of circulating free pentosidine; (3) free pentosidine may accumulate as a result of decreased glomerular filtration; and (4) the mechanism of accumulation of albumin-linked pentosidine is not related to high glucose levels. It suggests the simultaneous accumulation, during renal failure, of either unknown pentosidine precursor(s) or catalyst(s) of glycoxidation, independent of glucose.

[1]  V. Monnier,et al.  Identification of pentosidine as a native structure for advanced glycation end products in beta-2-microglobulin-containing amyloid fibrils in patients with dialysis-related amyloidosis. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[2]  H. Seo,et al.  Monocyte/macrophage response to beta 2-microglobulin modified with advanced glycation end products. , 1996, Kidney international.

[3]  J. Baynes,et al.  N epsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins. , 1995, Biochemistry.

[4]  J. Zweier,et al.  Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid β-peptide , 1995, Nature Medicine.

[5]  N. Taniguchi,et al.  Glycation of human beta 2-microglobulin in patients with hemodialysis-associated amyloidosis: identification of the glycated sites. , 1994, Biochemistry.

[6]  S. Grundy,et al.  Modification of low density lipoprotein by advanced glycation end products contributes to the dyslipidemia of diabetes and renal insufficiency. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[7]  V. Monnier,et al.  ELISA of pentosidine, an advanced glycation end product, in biological specimens. , 1994, Clinical chemistry.

[8]  A. Schmidt,et al.  Advanced glycation end products (AGEs) on the surface of diabetic erythrocytes bind to the vessel wall via a specific receptor inducing oxidant stress in the vasculature: a link between surface-associated AGEs and diabetic complications. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[9]  T. Miyata,et al.  Beta 2-microglobulin modified with advanced glycation end products induces interleukin-6 from human macrophages: role in the pathogenesis of hemodialysis-associated amyloidosis. , 1994, Biochemical and biophysical research communications.

[10]  E. Friedman,et al.  Reactive glycosylation endproducts in diabetic uraemia and treatment of renal failure , 1994, The Lancet.

[11]  G. Perry,et al.  Advanced Maillard reaction end products are associated with Alzheimer disease pathology. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[12]  R. Bucala,et al.  Advanced glycation end products contribute to amyloidosis in Alzheimer disease. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[13]  Y. Zou,et al.  Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins. , 1994, The Journal of biological chemistry.

[14]  H. Seo,et al.  Involvement of beta 2-microglobulin modified with advanced glycation end products in the pathogenesis of hemodialysis-associated amyloidosis. Induction of human monocyte chemotaxis and macrophage secretion of tumor necrosis factor-alpha and interleukin-1. , 1994, The Journal of clinical investigation.

[15]  N. Taniguchi,et al.  beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis. , 1993, The Journal of clinical investigation.

[16]  L. L. Moore,et al.  Increased collagen-linked pentosidine levels and advanced glycosylation end products in early diabetic nephropathy. , 1993, The Journal of clinical investigation.

[17]  T. Lyons,et al.  Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. , 1993, The Journal of clinical investigation.

[18]  A. Schmidt,et al.  Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products. , 1993, The Journal of clinical investigation.

[19]  V. Monnier,et al.  Effects of kidney or kidney-pancreas transplantation on plasma pentosidine. , 1993, Kidney international.

[20]  T. Lyons,et al.  Accumulation of Maillard reaction products in skin collagen in diabetes and aging. , 1993, The Journal of clinical investigation.

[21]  V. Monnier,et al.  Pentosidine Formation in Skin Correlates With Severity of Complications in Individuals With Long-Standing IDDM , 1992, Diabetes.

[22]  V. Monnier,et al.  Maillard Reaction-Mediated Molecular Damage to Extracellular Matrix and Other Tissue Proteins in Diabetes, Aging, and Uremia , 1992, Diabetes.

[23]  K. O. Elliston,et al.  Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins. , 1992, The Journal of biological chemistry.

[24]  R. Bucala,et al.  Immunochemical detection of advanced glycosylation end products in vivo. , 1992, The Journal of biological chemistry.

[25]  V. Monnier,et al.  Chromatographic Quantitation of Plasma and Erythrocyte Pentosidine in Diabetic and Uremic Subjects , 1992, Diabetes.

[26]  Z. Makita,et al.  Human and rat mesangial cell receptors for glucose-modified proteins: potential role in kidney tissue remodelling and diabetic nephropathy , 1991, The Journal of experimental medicine.

[27]  E. Friedman,et al.  Advanced glycosylation end products in patients with diabetic nephropathy. , 1991, The New England journal of medicine.

[28]  J. Baynes,et al.  Formation of pentosidine during nonenzymatic browning of proteins by glucose. Identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo. , 1991, The Journal of biological chemistry.

[29]  V. Monnier,et al.  Mechanism of formation of the Maillard protein cross-link pentosidine. Glucose, fructose, and ascorbate as pentosidine precursors. , 1991, The Journal of biological chemistry.

[30]  Y. Morino,et al.  Immunochemical approach to characterize advanced glycation end products of the Maillard reaction. Evidence for the presence of a common structure. , 1991, The Journal of biological chemistry.

[31]  J. Baynes.  Role of Oxidative Stress in Development of Complications in Diabetes , 1991, Diabetes.

[32]  S. Ogawa,et al.  Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor: role in vascular disease of diabetes and aging. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[33]  A. J. Furth.  The maillard reaction in aging, diabetes and nutrition: edited by John W. Baynes and Vincent M. Monnier, Alan R. Liss, 1989. $85.00 (xvii + 432 pages) ISBN 0 8451 5154 1 , 1990 .

[34]  V. Monnier,et al.  End-stage renal disease and diabetes catalyze the formation of a pentose-derived crosslink from aging human collagen. , 1990, The Journal of clinical investigation.

[35]  V. Monnier,et al.  Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process. , 1989, The Journal of biological chemistry.

[36]  K. Manogue,et al.  Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling. , 1988, Science.

[37]  A. Cerami,et al.  Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications. , 1988, The New England journal of medicine.

[38]  B. Frangione,et al.  Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[39]  M Arakawa,et al.  A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin. , 1985, Biochemical and biophysical research communications.

[40]  F. Smith,et al.  Experimental renal failure. , 1952, Clinical science.