Glycation of human serum albumin: inhibition by Diclofenac

Boekel, M.A.M. van; Bergh, Paul J.P.C. van den; Hoenders, Herman J.

doi:10.1016/0167-4838(92)90270-n

Cited by 40 publications

(22 citation statements)

References 17 publications

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“…Several attempts have been made to seek suitable glycation inhibitors from both experimental and thera peutic standpoints. Compounds already test ed and found to be inhibitory include aminoguanidine (AG) [2], aspirin [3], bendazac [4], D-lysine [5], ibuprofen [6], vitamin E [7], L-arginine and L-lysine [8], captopril [9], di clofenac [10], and a-lipoate [11]. Among them, AG has been widely used as a potent glycation inhibitor in vitro and in vivo [12][13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Inhibition of Advanced Protein Glycation by 8-Quinolinecarboxylic Hydrazide

Miwa

Tsugawa²,

Koyasu³

et al. 1996

Pharmacology

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Glycation of proteins is believed to be involved in the pathogenesis of diabetic complications, and thus the development of potent inhibitors of protein glycation is highly desirable. We tested the inhibitory effects of 12 hydrazide compounds against protein glycation and compared them with the effects of aminoguanidine (AG), a well-known inhibitor. When bovine serum albumin (BSA) was incubated with 100 mmol/l mannose for 10 days at 37 °C in the presence and absence of hydrazide compounds or AG at 1 mmol/l, only p-anisic hydrazide inhibited Amadori product formation. On the other hand, 8 hydrazides as well as AG inhibited the formation of advanced glycation end products (AGEs). 8-Quinolinecarboxylic hydrazide (8-QCH), the most potent hydrazide, was more effective than AG. Neither 8-QCH nor AG affected the spontaneous decrease in Amadori products of preglycated BSA in the absence of sugar, but suppressed the spontaneous increase in AGEs from preglycated BSA, with higher potency of 8-QCH relative to AG. The results indicate that 8-QCH is a more potent inhibitor of AGE formation than AG and suggest that the inhibition mechanisms of 8-QCH and AG resemble each other.

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Section: Introductionmentioning

confidence: 99%

Inhibition of Advanced Protein Glycation by 8-Quinolinecarboxylic Hydrazide

Miwa

Tsugawa²,

Koyasu³

et al. 1996

Pharmacology

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“…Diclofenac, an anti-inflammatory drug, could also protect proteins from sugar attachment thanks to its non-covalent interactions with proteins such as serum albumin. Results suggest that diclofenac specifically blocked at least one of the major glycation sites of human serum albumin [96]. Some inhibitors are scavengers of free carbonyl.…”

Section: Therapy For Age-mediated Neurodegenerative Diseases With Synmentioning

confidence: 95%

The role of advanced glycation end products in various types of neurodegenerative disease: a therapeutic approach

Salahuddin

Rabbani

Khan

2014

Cellular and Molecular Biology Letters

150

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of advanced glycation end products; ROS -reactive oxygen species; SNCA -synuclein alpha; sRAGE -soluble receptor of advanced glycation end products; TTR -transthyretin; TKtransketolase; TNF -tumor necrosis factor-α; TPP -thiamine pyrophosphate Review THE ROLE OF ADVANCED GLYCATION END PRODUCTS IN VARIOUS TYPES OF NEURODEGENERATIVE DISEASE:A THERAPEUTIC APPROACH Abstract: Protein glycation is initiated by a nucleophilic addition reaction between the free amino group from a protein, lipid or nucleic acid and the carbonyl group of a reducing sugar. This reaction forms a reversible Schiff base, which rearranges over a period of days to produce ketoamine or Amadori products. The Amadori products undergo dehydration and rearrangements and develop a cross-link between adjacent proteins, giving rise to protein aggregation or advanced glycation end products (AGEs). A number of studies Unauthenticated Download Date | 5/11/18 1:17 PM

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“…EXO-226, a glycation inhibitor, has been reported to significantly reduce urine protein excretion accompanied by a lowering in glycated albumin. 99 Other compounds that had previously been described to have inhibitory activity against AGE formation in vitro and in vivo are Aspirin, 100 Bendazac, 101 D-lysine, 102 Ibuprofen, 103 vitamin C, 104 vitamin E, 105 L-arginine and L-lysine, 106 Captopril, 107 Diclofenac, 108 and a-lipoate. 109 While AG is not an antioxidant, other compounds (Vitamins C and E, phenolic compounds) might act as antioxidants in preventing AGEs formation.…”

Section: Anti-advanced Glycation End-product Drugsmentioning

confidence: 98%

Diabetes complications and their potential prevention: Aldose reductase inhibition and other approaches

Costantino¹,

Rastelli²,

Vianello

et al. 1999

Med. Res. Rev.

148

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Despite recent advances both in the chemistry and molecular pharmacology of antidiabetic drugs, diabetes still remains a life‐threatening disease, which tends to spread all over the world. The clinical profile of diabetic subjects is often worsened by the presence of several long‐term complications, namely neuropathy, nephropathy, retinopathy, and cataract. Several attempts have been made to prevent or at least to delay them. The most relevant are reported in this review, including the development of compounds acting as aldose reductase inhibitors, anti‐advanced glycation end‐product drugs, free radical scavengers, vasoactive agents, essential fatty acid supplementation, and neurotropic growth factors. © 1999 John Wiley & Sons, Inc. Med Res Rev, 19, No. 1, 3–23, 1999.

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Glycation of human serum albumin: inhibition by Diclofenac

Cited by 40 publications

References 17 publications

Inhibition of Advanced Protein Glycation by 8-Quinolinecarboxylic Hydrazide

Inhibition of Advanced Protein Glycation by 8-Quinolinecarboxylic Hydrazide

The role of advanced glycation end products in various types of neurodegenerative disease: a therapeutic approach

Diabetes complications and their potential prevention: Aldose reductase inhibition and other approaches

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