Inhibition of advanced protein glycation by a Schiff base between aminoguanidine and pyridoxal

Taguchi, Tadao; Sugiura, Mariko; Hamada, Y.; Miwa, Ichitomo

doi:10.1016/s0014-2999(99)00471-9

Cited by 46 publications

(29 citation statements)

References 16 publications

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“…The first is the aminoguanidine-pyridoxal Schiff base adduct (Pl-AG), developed as a safer alternative to AG, that has been shown to be more effective than AG in preventing diabetic nephropathy in mice, [122] and diabetic neuropathy and cataracts in STZ-diabetic rats, without decreasing pyridoxal phosphate levels in tissues. [123,124] The second example is the 6-dimethylamino derivative of pyridoxamine (dmaPM), designed to act as both a carbonyl-and a radical-trapping agent. [125] This compound showed excellent inhibition of AGE formation in vitro [126] and seems to be extremely promising as an ALE inhibitor, but further studies are required to demonstrate its efficacy in vivo.…”

Section: Reaction Mechanism Of Rcs Scavengingmentioning

confidence: 99%

Lipoxidation‐Derived Reactive Carbonyl Species as Potential Drug Targets in Preventing Protein Carbonylation and Related Cellular Dysfunction

et al. 2006

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Section: Reaction Mechanism Of Rcs Scavengingmentioning

confidence: 99%

Lipoxidation‐Derived Reactive Carbonyl Species as Potential Drug Targets in Preventing Protein Carbonylation and Related Cellular Dysfunction

et al. 2006

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“…In a study, it was hypothesized that the Schiff base adduct formed from DOI: 10.3109/13880209.2015.1028080 aminoguanidine and pyridoxal might be a better compound than aminoguanidine (Taguchi et al, 1999). In another study, aminoguanidine, a scavenger of free methylglyoxal, considerably increased the wound healing in the young and old mice which is due to reduced migration of methylglyoxal and proliferation of fibroblasts (Fleming et al, 2013).…”

Section: In Vivo Inhibition Of Protein Glycationmentioning

confidence: 99%

Antiglycation therapy: Discovery of promising antiglycation agents for the management of diabetic complications

Abbas

Al‐Harrasi

Hussain

et al. 2015

Pharmaceutical Biology

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Context: During diabetes mellitus, non-enzymatic reaction between amino groups of protein and carbonyl of reducing sugars (Millard reaction) is responsible for the major diabetic complications. Various efforts have been made to influence the process of protein glycation. Objectives: This review article provides an extensive survey of various studies published in scientific literature to understand the process of protein glycation and its measurement. Moreover, evaluation and identification of potential inhibitors (antiglycation agents) of protein glycation from natural and synthetic sources and their mechanism of action in vitro and in vivo are also addressed. Method: In this review article, the mechanism involved in the formation of advanced glycation end products (AGEs) is discussed, while in second and third parts, promising antiglycation agents of natural and synthetic sources have been reviewed, respectively. Finally, in vivo studies have been addressed. This review is mainly compiled from important databases such as Science, Direct, Chemical Abstracts, SciFinder, and PubMed. Results: During the last two decades, various attempts have been made to inhibit the process of protein glycation. New potent inhibitors of protein glycation belonging to different classes such as flavonoids, alkaloids, terpenes, benzenediol Schiff bases, substituted indol, and thio compounds have been identified. Conclusion: Antiglycation therapy will be an effective strategy in future to prevent the formation of AGEs for the management of late diabetic complications Current review article highlighted various compounds of natural and synthetic origins identified previously to inhibit the protein glycation and formation of AGEs in vitro and in vivo.

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“…These compounds exhibited significant anti-glycation activities [10]. The Schiff bases of isatin also showed a promising anti-glycation potential in vitro [11].…”

Section: Research Articlementioning

confidence: 99%

Substituted benzenediol Schiff bases as promising new anti-glycation agents

Choudhary

Abbas

Ali

et al. 2010

Journal of Enzyme Inhibition and Medicinal Chemistry

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Inhibition of advanced protein glycation by a Schiff base between aminoguanidine and pyridoxal

Cited by 46 publications

References 16 publications

Lipoxidation‐Derived Reactive Carbonyl Species as Potential Drug Targets in Preventing Protein Carbonylation and Related Cellular Dysfunction

Lipoxidation‐Derived Reactive Carbonyl Species as Potential Drug Targets in Preventing Protein Carbonylation and Related Cellular Dysfunction

Antiglycation therapy: Discovery of promising antiglycation agents for the management of diabetic complications

Substituted benzenediol Schiff bases as promising new anti-glycation agents

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