Nicotine and amyloid formation

Zeng, Hong; Zhang, Yongbo; Peng, Li Jun; Shao, Huili; Menon, N; Yang, Jing; Salomon, Arthur R.; Freidland, Robert P.; Zagorski, Michael G.

doi:10.1016/s0006-3223(00)01111-2

Cited by 71 publications

(58 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Gratifyingly, the diffusion coefficients resulting from the DECRA analysis are in agreement with those obtained from DOSY analysis of the data. Further corroborative evidence of covalent modification can been seen by analyzing nicotine-A␤ incubations as nicotine can only inhibit aggregation via a noncovalent mechanism (39,40). In this data set, two populations of nicotine molecules cannot be observed (data not shown).…”

Section: Covalent Modification Of A␤ By Nornicotine and Inhibition Ofsupporting

confidence: 55%

“…The beneficial effects of nicotine have been attributed to a number of factors including an up-regulation of nicotine receptors that are deficient in the brain, or possibly a protection from the A␤-induced neurotoxicity (38). Others have postulated that nicotine also serves another role by inhibiting ␤-amyloidosis through noncovalent binding to either the ␣-helical structure of A␤ (39) or a small, soluble ␤-sheet aggregate (40).…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Glycation of the amyloid β-protein by a nicotine metabolite: A fortuitous chemical dynamic between smoking and Alzheimer's disease

Dickerson

Janda²

2003

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The origin of Alzheimer's disease (AD) has been subjected to an intense amount of examination; however, a clear conclusion as to the nature of this crippling disease has yet to be identified. What is readily accepted is that a definitive marker of this disease is the aggregation of the amyloid ␤-peptide (A␤) into neuritic plaques. The recent observation that nicotine exposure leads to delayed onset of AD has stimulated a flurry of research into the nature of this neuroprotective effect. This phenomenon has been debated, but no consensus has been reached, and although these studies have targeted nicotine, the primary alkaloid in tobacco, few studies have considered the physiological role of nicotine metabolites in disease states. Nornicotine is a major nicotine metabolite in the CNS and has been shown to participate in the aberrant glycation of proteins in vivo in a process termed nornicotine-based glycation. Herein is detailed a potentially fortuitous role of nornicotine-based glycation in relation to the pathology of AD. Specifically, nornicotine was found to covalently alter A␤, leading to reduced peptide aggregation. Potential consequences of this reaction cascade include reduced plaque formation and͞or altered clearance of the peptide, as well as attenuated toxicity of soluble A␤ aggregates. The findings described provide an alternative mechanism for nicotine neuroprotection in AD and a means for the alteration of amyloid folding based on a covalent chemical event.

show abstract

Section: Covalent Modification Of A␤ By Nornicotine and Inhibition Ofsupporting

confidence: 55%

Section: Resultsmentioning

confidence: 99%

Glycation of the amyloid β-protein by a nicotine metabolite: A fortuitous chemical dynamic between smoking and Alzheimer's disease

Dickerson

Janda²

2003

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…Few studies have shown that nicotine may actually improve short‐term cognitive performance7, 30 and inhibit amyloid formation 31, 32. On the other hand, various other studies have shown that smoking is a risk factor for Alzheimer's disease, namely due to reactive oxygen species produced by smoking 33, 34, 35, 36, 37.…”

Section: Discussionmentioning

confidence: 99%

Effect of smoking cessation on the risk of dementia: a longitudinal study

Choi

Park

2018

Ann Clin Transl Neurol

View full text Add to dashboard Cite

ObjectiveTo determine the risk of developing dementia in relation to duration of smoking cessation by using a nationwide health claims database.MethodsThis cohort study included 46,140 men aged 60 years or older from Korean National Health Insurance System – National Health Screening Cohort, a population‐based national health screening program from 2002 to 2013. The changes in smoking habit from a questionnaire during the first (2002 and 2003) and second (2004 and 2005) health examination periods, participants were divided into continual smokers, short‐term (less than 4 years) quitters, long‐term (4 years or more) quitters, and never smokers. Participants were followed‐up for 8 years from January 1, 2006 for the development of overall dementia, Alzheimer's disease, and vascular dementia.ResultsCompared to continual smokers, long‐term quitters and never smokers had decreased risk of overall dementia (hazard ratio, HR 0.86 95% CI, confidence interval 0.75–0.99 and HR: 0.81; 95% CI: 0.71–0.91, respectively). Never smokers had decreased risk of Alzheimer's disease (HR: 0.82; 95% CI: 0.70–0.96) compared to continual smokers. Finally, both long‐term quitters (HR: 0.68; 95% CI: 0.48–0.96) and never smokers (HR: 0.71; 95% CI: 0.54–0.95) had decreased risk of vascular dementia compared to continual smokers.InterpretationSmoking was associated with increased risk of dementia. Smokers who quit for a prolonged period of time may benefit from reduced risk of dementia. Therefore, smokers should be encouraged to quit in order to reduce the risk of developing dementia, especially in the elderly population who are already at risk.

show abstract

“…Tomiyama et al (1996) suggested that Rif binds to Aß by hydrophobic interactions between its lipophilic ansa chain and the hydrophobic region of Aß, thus blocking associations between Aß molecules leading to fAß formation. The anti-amyloidogenic and fibril-destabilizing activity of tetracycline (Tc), small-molecule anionic sulphonates or sulphates, melatonin, ß-sheet breaker peptides (iAß5) and nicotine may also be related to the propensity to bind to the specific sites of Aß (Kisilevsky et al 1995;Soto et al 1996;Pappolla et al 1998;Forloni et al 2001;Zeng et al 2001). Thus, it may be reasonable to consider that NSAIDs could exhibit their anti-amyloidogenic and fibril-destabilizing effects by directly binding to Aßs and/or fAßs.…”

Section: Discussionmentioning

confidence: 99%

Non-steroidal anti-inflammatory drugs have anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro

et al. 2005

View full text Add to dashboard Cite

The pathogenesis of Alzheimer's disease (AD) is characterized by cerebral deposits of amyloid ß-peptides (Aß) and neurofibrillary tangles which are surrounded by inflammatory cells. Long-term uses of non-steroidal anti-inflammatory drugs (NSAIDs) reduce the risk of developing AD and delay the onset of the disease. In the present study, we used fluorescence spectroscopy with thioflavin T and electron microscopy to examine the effects of NSAIDs such as ibuprofen, aspirin, meclofenamic acid sodium salt, diclofenac sodium salt, ketoprofen, flurbiprofen, naproxen, sulindac sulfide and indomethacin on the formation, extension, and destabilization of ß-amyloid fibrils (fAß) at pH 7.5 at 37˚C in vitro. All examined NSAIDs dose-dependently inhibited formation of fAß from fresh Aß(1-40) and Aß(1-42), as well as their extension. Moreover, these NSAIDs dose-dependently destabilized preformed fAßs. The overall activity of the molecules examined was in the following order: ibuprofen ≈ sulindac sulfide ≥ meclofenamic acid sodium salt > aspirin ≈ ketoprofen ≥ flurbiprofen ≈ diclofenac sodium salt > naproxen ≈ indomethacin. Although the mechanisms by which these NSAIDs inhibit fAß formation from Aß, and destabilize preformed fAß in vitro are still unclear, NSAIDs may be promising for the prevention and treatment of AD.

show abstract

Nicotine and amyloid formation

Abstract: The major protein constituents of amyloid deposits in Alzheimer's disease (AD) are the 40-residue ␤-amyloid (A␤)

Cited by 71 publications

References 53 publications

Glycation of the amyloid β-protein by a nicotine metabolite: A fortuitous chemical dynamic between smoking and Alzheimer's disease

Glycation of the amyloid β-protein by a nicotine metabolite: A fortuitous chemical dynamic between smoking and Alzheimer's disease

Effect of smoking cessation on the risk of dementia: a longitudinal study

Non-steroidal anti-inflammatory drugs have anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro

Contact Info

Product

Resources

About