Influence of advanced glycation end-products and AGE-inhibitors on nucleation-dependent polymerization of β-amyloid peptide

Münch, Gerald; Mayer, Samantha; Michaelis, J.; Hipkiss, Alan R.; Riederer, Peter; Müller, Renate; Neumann, Arne; Schinzel, Reinhard; Cunningham, Anne M.

doi:10.1016/s0925-4439(96)00062-2

Cited by 169 publications

(87 citation statements)

References 43 publications

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“…Different groups have demonstrated that AGE-related modifications decrease protein solubility and increase protease resistance (43) of several proteins present in the pathological lesions associated with AD (44). AGE product accumulation has been demonstrated in NPs and NFTs in different brain areas of patients with AD (45). Indeed, it appears that aggregation of amyloid-␤ is accelerated by AGE-mediated cross-linking of extracellular proteins.…”

Section: Discussionmentioning

confidence: 99%

Type 2 Diabetes, APOE Gene, and the Risk for Dementia and Related Pathologies

2002

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Type 2 diabetes may be a risk factor for dementia, but the associated pathological mechanisms remains unclear. We evaluated the association of diabetes alone or combined with the apolipoprotein E (APOE) gene with incident dementia and neuropathological outcomes in a population-based cohort of 2,574 Japanese-American men enrolled in the Honolulu-Asia Aging Study, including 216 subjects who underwent autopsy. Type 2 diabetes was ascertained by interview and direct glucose testing. Dementia was assessed in 1991 and 1994 by clinical examination and magnetic resonance imaging and was diagnosed according to international guidelines. Logistic regression was used to assess the RR of developing dementia, and log-linear regression was used to estimate the incident rate ratio (

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Section: Discussionmentioning

confidence: 99%

Type 2 Diabetes, APOE Gene, and the Risk for Dementia and Related Pathologies

2002

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“…Carnosine is dipeptide containing histidine. Carnosine-like compounds can prevent AGE-induced crosslinking (21). Recently, Seidler et al (22) suggested that histidine is the representative structure for an anti-crosslinking agent.…”

Section: Discussionmentioning

confidence: 99%

Isolation, purification and characterization of histidino-threosidine, a novel Maillard reaction protein crosslink from threose, lysine and histidine

Dai¹,

Nemet²,

Shen³

et al. 2007

Archives of Biochemistry and Biophysics

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We isolated a novel acid-labile yellow chromophore from the incubation of lysine, histidine and Dthreose and identified its chemical structure by one and two-dimensional 1 H and DEPT NMR spectroscopy combined with LC-tandem mass spectrometry. This new cross-link exhibits a UV absorbance maximum at 305 nm and a molecular mass of 451 Da. The proposed structure is 2-amino-5-(3-((4-(2-amino-2-carboxyethyl)-1H-imidazol-1-yl)methyl)-4-(1,2-dihydroxyethyl)-2-formyl-1H-pyrrol-1-yl)pentatonic acid, a cross-link between lysine and histidine with addition of two threose molecules. It was in part deduced and confirmed through synthesis of the analogous compound from n-butylamine, imidazole and D-threose. We assigned the compound the trivial name histidino-threosidine. Systemic incubation revealed that histidino-threosidine can be formed in low amounts from fructose, glyceraldehyde, methylglyoxal, glycolaldehyde, ascorbic acid, and dehydroascorbic acid, but at a much higher yield with degradation products of ascorbic acid, i.e. threose, erythrose, and erythrulose. Bovine lens protein incubated with 10 and 50 mM threose for two weeks yielded 560 and 2840 pmol/mg histidino-threosidine. Histidino-threosidine is to our knowledge the first Maillard reaction product known to involve histidine in a crosslink.

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“…[41]. A aggregation follows a nucleation-dependent polymerization mechanism, which is significantly accelerated by AGE-mediated crosslinking [42]. The A aggregation consists of two distinctive stages, an initial, slow, nucleusformation step, followed by a rapid elongation phase.…”

Section: Glycation In Alzheimer's Diseasementioning

confidence: 99%

“…Nucleation-dependent polymerization of A, the major component of plaques in patients with Alzheimer's disease, is significantly accelerated by AGEs in vitro. Formation of AGE-crosslinked amyloid  peptide aggregates was inhibited by the AGEinhibitor tenilsetam [42], which is covalently attached to glycated proteins and blocks the reactive sites for further polymerization reactions. Most likely, it reacts with Amadori products.…”

Section: Therapy For Age-mediated Neurodegenerative Diseases With Synmentioning

confidence: 99%

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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Influence of advanced glycation end-products and AGE-inhibitors on nucleation-dependent polymerization of β-amyloid peptide

Cited by 169 publications

References 43 publications

Type 2 Diabetes, APOE Gene, and the Risk for Dementia and Related Pathologies

Type 2 Diabetes, APOE Gene, and the Risk for Dementia and Related Pathologies

Isolation, purification and characterization of histidino-threosidine, a novel Maillard reaction protein crosslink from threose, lysine and histidine

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

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