In Vivo Formation of a Schiff Base of Aminoguanidine with Pyridoxal Phosphate

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

doi:10.1016/s0006-2952(98)00010-0

Cited by 65 publications

(32 citation statements)

References 18 publications

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“…To perform kinetic studies, incubations lasted between 0 and 20 h. Aliquots were removed at various times, and pyridoxal 5'-phosphate content was assayed by HPLC (24). In brief, a 10-l solution of reaction mixture was injected into an HPLC system and separated on a Waters Purecil C18 column (5 m, 4.6 ϫ 250 mm).…”

Section: Entrapment Of Pyridoxal 5'-phosphatementioning

confidence: 99%

“…Oral administration of OPB-9195 to rats after balloon injury of their carotid arteries effectively reduces neointima proliferation in arterial walls (23). Unfortunately, clinical benefits of both compounds given to diabetic patients have been hampered by side effects related to their characteristic trapping of pyridoxal with an attendant vitamin B6 deficiency (24).…”

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confidence: 99%

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Angiotensin II Receptor Antagonists and Angiotensin-Converting Enzyme Inhibitors Lower In Vitro the Formation of Advanced Glycation End Products

Miyata¹,

Strihou²,

Ueda³

et al. 2002

Journal of the American Society of Nephrology

282

218

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Abstract. The implication of advanced glycation end products (AGE) in the pathogenesis of atherosclerosis and of diabetic and uremic complications has stimulated a search for AGE inhibitors. This study evaluates the AGE inhibitory potential of several well-tolerated hypotensive drugs. Olmesartan, an angiotensin II type 1 receptor (AIIR) antagonist, as well as temocaprilat, an angiotensin-converting enzyme (ACE) inhibitor, unlike nifedipine, a calcium blocker, inhibit in vitro the formation of two AGE, pentosidine and N ⑀ -carboxymethyllysine (CML), during incubation of nonuremic diabetic, nondiabetic uremic, or diabetic uremic plasma or of BSA fortified with arabinose. This effect is shared by all tested AIIR antagonists and ACE inhibitors. On an equimolar basis, they are more efficient than aminoguanidine or pyridoxamine. Unlike the latter two compounds, they do not trap reactive carbonyl precursors for AGE, but impact on the production of reactive carbonyl precursors for AGE by chelating transition metals and inhibiting various oxidative steps, including carbon-centered and hydroxyl radicals, at both the pre-and post-Amadori steps. Their effect is paralleled by a lowered production of reactive carbonyl precursors. Finally, they do not bind pyridoxal, unlike aminoguanidine. Altogether, this study demonstrates for the first time that widely used hypotensive agents, AIIR antagonists and ACE inhibitors, significantly attenuate AGE production. This study provides a new framework for the assessment of families of AGE-lowering compounds according to their mechanisms of action.Advanced glycation and oxidation irreversibly modify proteins over the years and thus contribute to aging phenomena (1). Their local or generalized acceleration is associated with atherosclerosis (2-6) as well as with various diabetic (7-10) and uremic complications (11-13). Inhibition of advanced glycation end products (AGE) formation has thus become a therapeutic goal.Aminoguanidine, the first AGE inhibitor discovered in 1986 (14), and (Ϯ)-2-isopropylidenehydrazono-4-oxo-thiazolidin-5-ylacetanilide (OPB-9195) (15) are both hydrazine-derivatives. They inhibit in vitro the formation of AGE, pentosidine (16), and N ⑀ -carboxymethyllysine (CML) (17) from a variety of individual precursors, such as ribose, glucose, and ascorbate, as well as that of advanced lipoxidation end products (ALE), malondialdehyde-lysine and 4-hydroxynonenal-protein adduct (18), from arachidonate (19). They also inhibit pentosidine generation in diabetic and uremic plasma incubated for 4 wk (20).As expected, both compounds correct several biologic effects that are associated with AGE formation. In murine thymocyte and fibroblasts, they inhibit the phosphorylation of tyrosine residues of a number of intracellular proteins induced by cell surface Schiff base formation (21). Given to diabetic animal models, such as Otsuka-Long-Evans-Tokushima-Fatty (OLETF) or streptozotocin-treated rats, they reduce urinary albumin excretion and improve glomerular morphology (15,22). Oral admi...

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Section: Entrapment Of Pyridoxal 5'-phosphatementioning

confidence: 99%

mentioning

confidence: 99%

Angiotensin II Receptor Antagonists and Angiotensin-Converting Enzyme Inhibitors Lower In Vitro the Formation of Advanced Glycation End Products

Miyata¹,

Strihou²,

Ueda³

et al. 2002

Journal of the American Society of Nephrology

282

218

View full text Add to dashboard Cite

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“…It dropped nearly two orders of magnitude after three months of storage. Experimental evidence indicates that amino- (20,26). Despite this evidence aminoguanidine (Pimagedine) has been introduced into clinical trials for prevention of diabetic nephropathy (2) but withdrawn later in the crucial Phase III because of neurotoxicity (10).…”

Section: Resultsmentioning

confidence: 99%

Impact of Glycation Inhibitors on the Biologic Activity of Recombinant Human Interferon-Gamma

Tsekovska

Boyanova

Mironova

et al. 2012

Biotechnology & Biotechnological Equipment

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“…Aminoguanidine 1.0 mM caused significant decrease of enzyme activity by 21.7% after 240 min of incubation. This inhibitory effect of AG may be explained by its binding to PLP coenzyme forming a Schiff base, which disturbs tissue distribution of PLP in vivo and decreases its concentration in liver (Okada & Ayabe, 1995;Taguchi et al, 1998). Trolox 2.5 mM did not influence AST activity.…”

Section: Enzyme Assaymentioning

confidence: 94%

Non-Enzymatic Glycation of Aminotransferases and the Possibilities of Its Modulation

Boušová¹,

Srbová²,

Dršata³

2012

Enzyme Inhibition and Bioapplications

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In Vivo Formation of a Schiff Base of Aminoguanidine with Pyridoxal Phosphate

Cited by 65 publications

References 18 publications

Angiotensin II Receptor Antagonists and Angiotensin-Converting Enzyme Inhibitors Lower In Vitro the Formation of Advanced Glycation End Products

Angiotensin II Receptor Antagonists and Angiotensin-Converting Enzyme Inhibitors Lower In Vitro the Formation of Advanced Glycation End Products

Impact of Glycation Inhibitors on the Biologic Activity of Recombinant Human Interferon-Gamma

Non-Enzymatic Glycation of Aminotransferases and the Possibilities of Its Modulation

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