Pharmacological reversal of advanced glycation end-product-mediated protein crosslinking

Ulrich, Peter; Zhang, X.

doi:10.1007/s001250051437

Cited by 31 publications

(24 citation statements)

References 10 publications

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“…The chemistry behind cross-link formation is complex and not fully understood but is thought to involve lysine residues [53]. This is supported by in vitro work using the agent phenacyl thiozolium bromide which is said to cleave chemical cross-links between two lysine residues [21]. Physiological cross-linking, which also tends to involve collagen, is better understood and requires the enzyme lysyl oxidase.…”

Section: Age and Cross-link Formationmentioning

confidence: 99%

“…Diabetic animal models using aminoguanidine have shown a reduction in diabetes related complications such as retinopathy, neuropathy and nephropathy [21,142]. Specifically, reductions in retinal microvessel formation, albuminuria and the prevention or decrease in motor and sensory nerve conduction velocity have been reported [20].…”

Section: Treatment Targeting Agementioning

confidence: 99%

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Advanced glycation end-products: a review

et al. 2001

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Diabetes is a common condition with multiple complications. There has been much work done to elaborate on the aetiology, prevention and treatment of diabetes related complications. The DCCT [1] and UKPDS [2] studies have emphasised the role of tight glucose control as being important in reducing diabetic microvascular disease in Type I (insulin-dependent) diabetes mellitus (DCCT) and Type II (non-insulin-dependent) diabetes mellitus (UKPDS). The relation between tight glucose control and macrovascular complications is, however, not clear [3]. Recently the importance of blood pressure control in reducing diabetic microvascular complications has been shown [4]. Apart from these factors, damage induced by hyperglycaemia involves a complex interaction between many influences including genetic predisposition, smoking, BMI, dyslipidaemia and alterations in coagulation factors [3]. The presence of advanced glycation end-products (AGE) is closely related to Diabetologia (2001) AbstractAdvanced glycation end-products are a complex and heterogeneous group of compounds that have been implicated in diabetes related complications. At present it is not known if they are the cause or the consequence of the complications observed. We discuss the chemistry of advanced glycated end-product formation and their patho-biochemistry particularly in relation to the diabetic microvascular complications of retinopathy, neuropathy and nephropathy as well as their role in the accelerated vasculopathy observed in diabetes. The concept of carbonyl stress as a cause for advanced glycated end-product toxicity is mentioned. We discuss alterations in the concentrations of advanced glycated end-products in the body, particularly in relation to changes occuring with age, diabetes and its complications such as nephropathy. Problems relating to current methods of advanced glycated end-product detection and measurement are highlighted including the lack of a universally established method of detection or unit of measurement. Agents used for the treatment of advanced glycated end-product accumulation are reviewed, with an emphasis on the results of the recent phase III trials using aminoguanidine and diabetes related complications. [Diabetologia (2001) 44: 129±146]Keywords Advanced glycated end-products, diabetes mellitus, microvascular disease, carbonyl stress, aminoguanidine.Corresponding author: Dr R. Singh MRCP (UK), FRACP, University Dept of Medicine, Royal Perth Hospital, PO Box X2213, Perth 6847, Western Australia Abbreviations: ESRD, End-stage renal disease; 3-DG, 3-deoxyglucosone; MGO, methylglyoxal; DOLD, deoxyglucosone-lysine dimer; MOLD, methyl glyoxal-lysine dimer; CML, N e -[carboxymethyl]-lysine; FFI, furoyl-furanyl imidazole; PTB, phenacyl thiozolium bromide; RAGE, receptor for AGE; NF-kB, nuclear factor-kB; VCAM-1, vascular cell adhesion molecule-1; ICAM-1, intracellular adhesion molecule-1; PECAM-1, platelet endothelial cell adhesion molecule-1; ELAM-1, endothelial leucocyte adhesion molecule-1; MSR, macrophage scavenger recepto...

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Section: Age and Cross-link Formationmentioning

confidence: 99%

Section: Treatment Targeting Agementioning

confidence: 99%

Advanced glycation end-products: a review

et al. 2001

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“…It has been implicated in the pathogenesis of many progressive diseases of ageing including vascular diseases, kidney disease, cataracts, Alzheimer's Dementia (Ulrich andZhang 1997, Perry andSmith 2001), complications of diabetes and cardiomyopathies (Bucala and Cerami 1992). It is believed that the loss of tissue elasticity results from rigidification of the extra cellular matrix due mostly to an increase in polymerization of collagen and elastin (Dimri et al 1995).…”

Section: Introductionmentioning

confidence: 99%

Human epithelial cells increase their rigidity with ageingin vitro: direct measurements

2004

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The decrease in elasticity of epithelial tissues with ageing contributes to many human diseases. This change was previously attributed to increased crosslinking of extracellular matrix proteins. Here we show that individual human epithelial cells also become significantly more rigid during ageing in vitro. Using atomic force microscopy (AFM), we found that the Young's modulus of viable cells was consistently increased two-to four-fold in older versus younger cells. Direct visualization of the cytoskeleton using a novel method involving the AFM suggested that increased rigidity of ageing cells was due to a higher density of cytoskeletal fibres. Our results identify a unique mechanism that might contribute to the age-related loss of elasticity in epithelial tissues.

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“…ALT-711, break covalent AGE cross-links and return the affected proteins to the uncross-linked state both in vitro and in vivo [18,19]. We consider that studies investigating the effect of cross-link breakers like ALT-711 on AGE levels may further broaden understanding of this condition.…”

Section: Discussionmentioning

confidence: 99%

The protective effect of aminoguanidine on erectile function in diabetic rats is not related to the timing of treatment

et al. 2004

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diabetic rats (60 mg/kg intraperitoneal) given free access to water; STZ diabetic rats treated with AG (1 g/L per day in the drinking water) immediately after inducing diabetes; and STZdiabetic rats treated with AG 1 month after inducing diabetes, respectively. Two months after inducing diabetes the intracavernosal pressure was measured after cavernosal nerve stimulation, and cavernosal AGE (5-hydroxy methyl furfural, 5-HMF) levels assessed.

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Pharmacological reversal of advanced glycation end-product-mediated protein crosslinking

Cited by 31 publications

References 10 publications

Advanced glycation end-products: a review

Advanced glycation end-products: a review

Human epithelial cells increase their rigidity with ageingin vitro: direct measurements

The protective effect of aminoguanidine on erectile function in diabetic rats is not related to the timing of treatment

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