Talk:Amyloid beta

"The expression of the ZnT3 is significantly lower in Alzheimer’s patients compared to healthy patients"

Should this be "higher" given the preceding and succeeding sentences imply that ZNT3 promotes AD? — Preceding unsigned comment added by 220.246.51.33 (talk) 02:21, 26 August 2013 (UTC)Reply

Where specifically do AB plaques form in the brain of AD patients? Do they mostly aggregate within neurons, or is more across synaptic junctions? —Preceding unsigned comment added by 152.3.178.172 (talk) 05:35, 2 April 2008 (UTC)Reply

Hi Beta-A plaques form in the extracellular fluid/matrix, though, the peptide also exists in solution (as in, not just as plaque aggreagates) and there is some evidence to show that it is the in solution/pre aggregate form is what actually causes the ill effects, rather than the bundles themselves, i.e. the number of plaques in a brain section doesn't appear to correlate to the severity of the neurological atrophy or dementia

Sorry, I can't remember which papers I read this in, but if I come across them again, I'll remember to link them back here, though I'm pretty sure it's basicly agreed upon about the plaques being extracellular 59.167.95.241 (talk) 13:39, 19 October 2009 (UTC)Reply

I've reverted a change that specified Alzheimer's as only disease involving Aβ. Both cerebral amyloid angiopathy and dementia with Lewy bodies are also characterized by the aggregation of this peptide. --Ipeltan 01:42, 24 April 2006 (UTC)Reply

I was the one who changed this, because amyloid "plaques" are not seen in pure congophilic amyloid angiopathy. Rather, CAA is characterized by amyloid deposition in the walls of cerebral vessels, but not parenchymal plaques. CAA can accompany AD, but it best to consider them as separate entities. Similarly, amyloid plaques are not part of the diagnostic criteria for Lewy body dementia, and are not an essential characteristic of the disease. Amyloid plaques and Lewy bodies can sometimes co-exist in substantial numbers in the cerebral cortex; in those cases, dual diganoses of AD and LBD, or alternatively use of the term "Lewy body variant" of AD, are warranted. Thus, the statement as it stands is incorrect - in neurologic disorders, amyloid plaques (generally of the neuritic variety) are a specific feature of AD, and are not charcateristic of any other neurologic disorder. However, since you have seen fit to change it back, I will wait for you to correct it. --Ve ri tas, 24 April 2006

Since this article is about amyloid beta rather than congophilic plaques, I think it's important to mention these other diseases in which deposits of this specific peptide are seen. This is particularly true since "amyloid plaque" is a term often used to describe the fibrillar structure of pathologic protein aggregates not containing a fragment of APP. I agree, however, that CAA represents a fundamentally different form of Abeta deposit. I've made an update along these lines. Feel free to make further changes back. --Ipeltan 06:29, 14 June 2006 (UTC)Reply

Since Amyloid precursor protein redirects here, it would be nice to say something about it. It may not be important to the pathogenesis of Alzheimer's, but it's natural for an enquiring mind to wonder what this thing is in its own right. We could mention it purely to dismiss it as irrelevant, but it would be better to say something positive.

I'd write something myself, but i know nothing - that's why i came here.

A recent paper called Unraveling in vivo functions of amyloid precursor protein: insights from knockout and knockdown studies might be a good place to start. Other reviews to look at would be The amyloid precursor protein and postnatal neurogenesis/neuroregeneration and The amyloid precursor protein and its network of interacting proteins: physiological and pathological implications.

-- Tom Anderson 2006-10-30 17:22 +00:00

Since Abeta peptide is produced in healthy brain as well as in diseased brain, does anyone know the normal role of this peptide ? And if it has neurotrophic role, would that mean that inhibition of beta and/or gamma sercetases would be bad ? Igoruha 10:03, 28 December 20006 (UTC)

• I went to a talk on the subject a few months back, and this exact question was posed to the presenter (but not by me, I'm shy). He responded that the protein's role is not yet known. That was about four months ago, and I have heard nothing that would suggest that we may have learned much more about it. – ClockworkSoul 22:11, 28 December 2006 (UTC)Reply

• Anyone know anything? Also, is AB42 found at all in normal patients? —Preceding unsigned comment added by 152.3.178.172 (talk) 05:28, 2 April 2008 (UTC)Reply

• The normal function of Aβ is unknown. Mice with Aβ precursor protein knocked out show various abnormalities, indicating that it may have a normal role. Aβ42 is present in normal patients but in Alzheimer's disease it is increased relative to Aβ40. Referenced from Findeis, MA (2007)The role of amyloid beta peptide 42 in Alzheimer's disease. Pharmacology & Therapeutics, 116(2):266-86. PMID 17716740 Movingturtle (talk) 13:16, 14 September 2010 (UTC)Reply

• I'm glad I came across this article. There has been a great deal of research on the normal functions of Aβ, going back several years. Obviously, popularizers and "reporters" of science don't care what the normal functions are. I have partially rectified the gap front and center in the article. Normal function is more important than disease function. Dogface (talk) 16:59, 29 August 2011 (UTC)Reply

Have heard reports that when it was tested for those suffering from Multiple Scelrosis seem to have levels of Aβ that are far lower than normal, but not read of what those levels are/how many were tested. It could be exerting some kind of protective effective against MS. Following on from that seems there's been work such as [1]Newscientist August 2012 -Alzheimer's villain cures multiple sclerosis in mice which reported some work on Aβ with mice that had had induced experimental mouse encephalitis-( looks somewhat like MS- and is usual animal model for MS). Injecting Aβ, into the nerves of those mice seemed to reduce levels of immune-signalling molecules involved in inflammation, and reduced damage. — Preceding unsigned comment added by 109.145.71.94 (talk) 05:51, 20 December 2012 (UTC)Reply

See the literature on copper homeostasis- I did not see it mentioned but it also seems this page is very inactive . 73.7.22.202 (talk) 19:17, 1 April 2016 (UTC)Reply

Someone added the following in "further reading":

• Grimm, M. O. W. et al. (2005) Regulation of cholesterol and sphingomyelin metabolism by amyloid-β and presenilin. 'Nature Cell Biology'. Vol. 7 (11), p. 1118 [2]

I can't figure out why this is so important, so I suggest it is only incorporated when context is provided. JFW | T@lk 21:51, 30 April 2008 (UTC)Reply

a connection is probably OR but perhaps http://www.ncbi.nlm.nih.gov/pubmed/15793579 provides some context? 109.145.71.94 (talk) 03:26, 23 December 2012 (UTC)Reply

Why is the title beta-A??? —Preceding unsigned comment added by 83.146.12.41 (talk) 23:29, 18 November 2008 (UTC)Reply

Agreed. Why not "Amyloid Beta" instead? Seabra (talk) 14:23, 10 February 2010 (UTC)Reply

i think it should be this too —Preceding unsigned comment added by 64.206.141.60 (talk) 03:55, 19 August 2010 (UTC)Reply

Haven't cited this specific paper, but this function is now mentioned in the article. Dogface (talk) 17:00, 29 August 2011 (UTC)Reply

I added this section based on this paper: http://www.plosone.org/article/info:doi/10.1371/journal.pone.0009505 but I do not know how to properly format it for the references list. 98.70.57.253 (talk) 16:19, 26 March 2010 (UTC)Reply

How can an entire page about this plaque not include any links to Insulin degrading enzyme? There are numerous published papers on the role of IDE in clearing away Aβ plaques. This enzyme just happens to be preferential to insulin over Aβ in a reaction. Chronic insulin levels will result in decreased cleanup of Aβ. Be careful however you might have to conclude that a doughnut is giving you Alzheimer's and nobody wants to admit that. —Preceding unsigned comment added by 24.19.119.3 (talk) 18:29, 20 August 2010 (UTC)Reply

What are "chronic insulin levels"? — Preceding unsigned comment added by Pathrider (talk • contribs) 22:09, 27 January 2011 (UTC)Reply

If you have reliable sources about that, it could be included. Could you show the papers? --Cyclopia^talk 23:50, 27 January 2011 (UTC)Reply

There are several Aβ-clearing enzymes, including neprilysin and IDE/insulysin. I'll add something about this some time soon.Dogface (talk) 17:01, 29 August 2011 (UTC)Reply

It could be useful to point out that researchers continue to refine immunotherapy strategies to improve trial designs, choice of amyloid species target, and vaccine design. Perhaps add the following sentence and references after the note on CAD106:

Another immunotherapy candidate is UB-311, directed against Aβ_1-14 (an exposed epitope in fibrils targeted by aducanumab) and designed to avoid adverse events associated with prior Aβ vaccines.^[1][2]

Mahamenacloud (talk)

@Jytdog: The only other clinical trial of an immunotherapy mentioned in the Intervention strategies section of this article is about CAD-106, which was added with this edit 6 years ago by Boghog. My question asks, was this claim about CAD-106 and the references used to source it grandfathered-in after MEDRS took effect? If not, I believe it should be re-evaluated to gauge its worthiness. Otherwise, wouldn't you agree that leaving it in the article leaves open the floodgates for every immunotherapy in clinical trials to be included in the article (23 at last count)? I'll guess that the COI editor's argument for wanting to include info on UB-311 (shown in the edit request above) is that "we're already mentioning one other clinical trial — so not mentioning all of them is unfair." What are your thoughts on this? .spintendo⋅⋅) 03:51, 18 May 2018 (UTC)Reply

WP:MEDRS is retroactive and hence there is no grandfathering of sources. However I think that misses the point. The source was used merely to document that a particular medication was in clinical trials, not that it was safe or efficacious. This limited use is outside the scope of MEDRS. Of source, if high quality secondary sources become available, those should replace primary sources. Since the publication of PMID 22677258 several reviews have been published. In addition to PMID 29067343 mentioned above, there is also PMID 29751505. This source document all the Alzheimer's immunotherapies currently in the clinic. Boghog (talk) 06:05, 18 May 2018 (UTC)Reply

Thank you @Boghog: for your reply. So to recap, what you're saying is when the language involves claims of safety and efficacy, then it's a matter for MEDRS. I'm wondering, would safe and efficacious-type language also include a company's stated hypothetical outcomes with regards to a drug's hoped-for effects in the body? In the Alzheimer's disease research article, a request is asking to place language which speaks to the hopes and desires of a manufacturer regarding their drug's actions within the body. The makers of UB-311 hope that the drug does not "invoke the immune system to produce antibodies at high titer levels for an extended period," and they desire for it to "avoid T-cell-mediated inflammation" thereby potentially "providing a wider therapeutic window." They're using this type of language because the drug is still in clinical trials, and they cannot say with certainty that it is able to do what they hope and desire it to do. So my question asks, would that COI request be governed by WP:CRYSTALBALL- because they are speaking about a hypothetical; or is it governed by MEDRS- because that hypothetical involves a statement about a hoped-for efficacy? In other words, is it ok for the company to, instead of saying "this drug will have this effect on a disease", is it ok for them to say "we hope it will have this effect on the cells of the body" because that is what it seems like their COI request at the Alzheimer's disease research article is trying to do. Is that just bringing through the back door what wont fit through the front, or am I over-analyzing it? Thank you again for any info you can offer, I appreciate it. .spintendo⋅⋅) 13:51, 18 May 2018 (UTC)Reply

Perhaps not everyone would agree with me, but IMHO it is OK to say that drug candidate X is being developed for the treatment of disease Y based on a primary source. (As always, a secondary source should be used if available). It is also OK to say that drug X has been approved for the treatment of disease Y in country Z by linking to an official statement by the regulatory authority in country Z. It is not OK to say that that drug X is effective for the treatment of disease Y unless a high quality secondary source is supplied that supports that claim. Boghog (talk) 18:19, 18 May 2018 (UTC)Reply

  Thank you for your feedback. .spintendo⋅⋅) 15:21, 20 May 2018 (UTC)Reply

If you follow the publications you will find out that many publication showing neurotoxicity have flawed methods (traces of HFIP) or are faked. I was doing cell cultures and observed co-scientists doing "experiments". I was never able to reproduce neurotoxicity. Some colleagues repeated experiements and selected only data samples which showed what they wanted to see or did not evaporate HFIP completely. Animal models with Aß-Overexpression show often not much of a difference, but have a plaque load orders of magnitude higher than in humans. Probably all unwanted animals "dissappear" in the trials anyway. There is no single Aß-only-related pathway despite involvement of the immun-system and tau that explains Aß-related "toxicity". There is no single Aß-related therapy aproach, which was successful and there will probably no successfull Anti-Aß-IGG in future. I hope someone will write a review paper and destroys the Aß-hyothesis entirely. After this publication, evidence grows:

https://www.nature.com/articles/s41591-019-0611-3.epdf?referrer_access_token=sD0rQpIzwadtilK3r7rZftRgN0jAjWel9jnR3ZoTv0MD-VV86aAAyEwkkG6LIbiRdl1gDXOz3el6NPWbJcYPfrcOips7AklR-EY0IJ9SwnZ1sSApqF_8eppLRQ2qH_GjN4ZWkcr8uxVU0P-rCrDb5YkUv4vXy1ISlhxij-iy-KRrwWs4-AUPF9HIltFgrvvXhmTNuuBSq2uiRe3cGJq2Tw%3D%3D&tracking_referrer=www.tagesspiegel.de&fbclid=IwAR2QJQ5XYLIVwQ15AaGXbXISv-pn2ucj29PlS0fBSUZmldYeKH1tp_-VRDQ — Preceding unsigned comment added by Dgdaniel87 (talk • contribs) 10:21, 6 November 2019 (UTC)Reply

Who wants to update the page according to this new information? https://www.science.org/content/article/potential-fabrication-research-images-threatens-key-theory-alzheimers-disease Bork (talk) 05:45, 23 July 2022 (UTC)Reply

Hello I'm student from the uskudar university I edit amyloid beta article for biotechnology course Baff123 (talk) 14:04, 2 January 2024 (UTC)Reply

This is not a good topic for student editing as it requires knowledge and experience of understanding WP:MEDRS sources. More importantly, it is unlikely that your limited abilities with English writing are suitable for this encyclopedia. Please choose a subject for your course in the Turkish Wikipedia. Inform your instructor and fellow students. Zefr (talk) 15:03, 2 January 2024 (UTC)Reply

  This article is currently the subject of a Wiki Education Foundation-supported course assignment, between 27 August 2024 and 13 December 2024. Further details are available on the course page. Student editor(s): HeelHooked (article contribs).

— Assignment last updated by HeelHooked (talk) 22:43, 30 September 2024 (UTC)Reply