Nonenzymatic Glycosylation of Collagen and other Proteins: Relationship to Development of Diabetic Complications

Perejda, Andrea J.; Uitto, Jouni

doi:10.1016/s0174-173x(82)80042-3

Cited by 49 publications

(13 citation statements)

References 42 publications

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“…The effect of nonenzymatic glycation on either fibronectin or gelatin, or of both of these components, on heparin binding was also assessed by incubating 3 Smith and Furcht. 33 Human plasma fibronectin that had undergone prior in vitro nonenzymatic glycation (12 days in the presence of 500 mM glucose) was also labeled by reductive methylation as described above except that 6.6 mg of protein was the starting material.…”

Section: Methodsmentioning

confidence: 99%

“…To date, hemoglobin, albumin, low-density lipoprotein, immunoglobulins, basement membrane collagen (type IV), lens crystallins, and peripheral nerve protein have been found to be nonenzymatically glycated to a greater extent in diabetes when compared with normals (see reviews, refs. [1][2][3][4]. The mechanism of this reaction involves the formation of a Schiff base between glucose and the N-terminal amino group of a polypeptide or the e-amino group of lysine in the polypeptide with subsequent formation of a stable ketoamine linkage via an Amadori rearrangement.…”

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confidence: 99%

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Nonenzymatic Glycation of Fibronectin and Alterations in the Molecular Association of Cell Matrix and Basement Membrane Components in Diabetes Mellitus

et al. 1985

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This study reports the nonenzymatic glycation of plasma fibronectin in vivo in diabetic dogs and also in vitro by incubation of human plasma fibronectin with excess glucose. Although no difference is observed in the total plasma fibronectin level, the nonenzymatic glycation of fibronectin is increased 2.3-fold in inbred male beagle dogs made diabetic with alloxan in comparison with age-matched controls. The extent of non-enzymatic glycation of fibronectin is shown to be proportional to blood glucose levels. HPLC reverse-phase analysis of the hydrolyzed amino acids and glyco-amino acids from plasma fibronectin samples of normal and diabetic dogs show that nonenzymatic glycation occurs only on lysine residues. When purified human plasma fibronectin was incubated in vitro with 500 mM glucose, the extent of nonenzymatic glycation of fibronectin was observed to increase proportionately with time. Ligand binding assays conducted in solution with varying concentrations of 3H-heparin in the presence of a constant amount of normal or nonenzymatically glycated human plasma fibronectin gave virtually identical binding curves. However, the binding of 3H-heparin to normal fibronectin could be increased fourfold by the concomitant addition of normal gelatin (denatured calfskin collagen). If in vitro glycated fibronectin and/or in vitro glycated gelatin are added under this latter condition with 3H-heparin, there is a tremendous decrease in the expected heparin binding seen with normal levels of nonenzymatic glycation. Other experiments were performed to quantitate the binding of 3H-labeled fibronectin to gelatin-coated nitrocellulose filters. Nonenzymatic glycation of fibronectin in vitro resulted in markedly decreased binding of 3H-fibronectin to collagen.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

Nonenzymatic Glycation of Fibronectin and Alterations in the Molecular Association of Cell Matrix and Basement Membrane Components in Diabetes Mellitus

et al. 1985

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“…This effect has been well-studied for proteins with long life spans, such as collagen and lens crystallin [16,17], as well for some proteins with shorter life spans, such as hemoglobin [18]. However, there has also been an increasing interest in the glycation of human serum albumin (HSA) and closely-related proteins (e.g., bovine serum albumin, or BSA).…”

Section: Introductionmentioning

confidence: 99%

Review: Glycation of human serum albumin

Anguizola

Matsuda

Barnaby

et al. 2013

Clinica Chimica Acta

336

308

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Glycation involves the non-enzymatic addition of reducing sugars and/or their reactive degradation products to amine groups on proteins. This process is promoted by the presence of elevated blood glucose concentrations in diabetes and occurs with various proteins that include human serum albumin (HSA). This review examines work that has been conducted in the study and analysis of glycated HSA. The general structure and properties of HSA are discussed, along with the reactions that can lead to modification of this protein during glycation. The use of glycated HSA as a short-to-intermediate term marker for glycemic control in diabetes is examined, and approaches that have been utilized for measuring glycated HSA are summarized. Structural studies of glycated HSA are reviewed, as acquired for both in vivo and in vitro glycated HSA, along with data that have been obtained on the rate and thermodynamics of HSA glycation. In addition, this review considers various studies that have investigated the effects of glycation on the binding of HSA with drugs, fatty acids and other solutes and the potential clinical significance of these effects.

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“…Using a very sensitive and specific method for nonenzymatic glycosylation (e.g., furosine), Vogt et al (14) demonstrated that significant increases in early glycosylated products were measured on tissues such as tendon, aorta, coronary arteries, peripheral nerves, lung connective tissue, and glomerular basement membrane at autopsy in diabetic compared with nondiabetic subjects. In addition, there has been extensive research evaluating nonenzymatic glycosylation of nerve myelin and collagen in the diabetic state (15)(16)(17)(18)(19). Finally, it has been shown that specific membrane proteins, such as those occurring in erythrocytes, can be shown to accumulate twice the quantitative level of nonenzymatically attached glucose in diabetic compared with control subjects (20).…”

Section: Discussionmentioning

confidence: 99%

Liver and Kidney Tissue Membranes As Tissue Markers for Nonenzymatic Glycosylation

Cefalu

Wang²,

Bell-Farrow³

et al. 1991

Diabetes

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We investigated the relationship of serum protein glycosylation to peripheral tissue membrane glycosylation. We studied 27 Sprague-Dawley rats and induced diabetes in 20 of them. Blood glucose levels were treated in 10 of the diabetic animals with daily subcutaneous insulin. After 8 wk, liver and kidney tissue was removed, purified membranes were prepared, and the percentage of glycosylated membrane protein was determined for the liver and kidney membranes by boronate-affinity methods. The percentage of glycosylated membrane protein for both liver and kidney tissue was found to correlate significantly with the glycemic state of the animal as assessed with glycosylated serum albumin, total glycosylated serum proteins, and glycosylated hemoglobin determinations (P less than 0.001 for each glycosylated protein parameter). In addition, the percentage of glycosylated membrane protein in the liver tissue correlated significantly with the measured level in the corresponding kidney tissue (r = 0.78, P less than 0.001). To identify the nature of the glycosylated membrane proteins, boronate-affinity methods were used to separate the glycosylated and nonglycosylated membrane proteins. It was determined that two major glycosylated protein bands exist for the liver membrane (78,000 and 58,700 Mr) and four for the kidney membranes (ranging from 48,700 to 74,000 Mr). The ultrastructural location and identification of these glycosylated membrane proteins are not known. This study demonstrates that measurement of clinical glycemic state, as reflected in glycosylated blood protein parameters such as glycosylated serum albumin and glycosylated hemoglobin, correlates significantly with ongoing tissue membrane accumulation of glucose.

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Nonenzymatic Glycosylation of Collagen and other Proteins: Relationship to Development of Diabetic Complications

Cited by 49 publications

References 42 publications

Nonenzymatic Glycation of Fibronectin and Alterations in the Molecular Association of Cell Matrix and Basement Membrane Components in Diabetes Mellitus

Nonenzymatic Glycation of Fibronectin and Alterations in the Molecular Association of Cell Matrix and Basement Membrane Components in Diabetes Mellitus

Review: Glycation of human serum albumin

Liver and Kidney Tissue Membranes As Tissue Markers for Nonenzymatic Glycosylation

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