Talk:Amyloid

message: There are amyloid deposits of IAPP aggressively taking over beta-cell mass in estimated 80% of Type-two diabetes cases...  Whether or not IAPP *causes* diabetes is up to debate, but, the deposits are definitely there.  This is generally the case for all amyloidoses; whether or not the amyloid peptide is the causative agent is unknown. - (unsigned)
:Reasonable enough emendation. I missed this explanation at first: sorry, my oversight, but a "see talk" or some similar notation in an edit summary would  make it harder to overlook. - Nunh-huh 06:31, 5 Jul 2004 (UTC)
thread_title: IAPP

message: I would like to see an expanded discussion of what Amyloidosis (which redirects here) is! — brighterorange (talk) 18:26, 25 September 2005 (UTC)
replies: text: Perhaps that should be a seperate page. Amyloid is the substance, while amyloidosis is the disease entity. That page itself should distinguish between the primary amyloidoses (AL amyloidosis, transthyretin-, ApoB-, lysozyme- or fibrinogen-related hereditary amyloid), AA amyloidosis secondary to chronic inflammatory conditions such as rheumatoid arthritis and FMF and some organ-specific amyloid. Clinical info from this page can then be merged there. Would you like to take the first step, Brighterorange? JFW | T@lk 19:12, 25 September 2005 (UTC)
replies: text: I see the invitation is still open. Since amyloidosis desparately needs a page of its own, perhaps I will start one up after I finish a few of the more developed projects. InvictaHOG 21:17, 3 August 2006 (UTC)
thread_title: Amyloidosis

message: It says cross polymerisation is the mechanism of prion replication. What is cross-polymerisation and how is it known that prions replicate that way? It's not a term I've heard of. --Purple 22:36, 7 February 2006 (UTC)
replies: text: OK I think I get that it's referring to molecules from one species seeding fibrils of the same protein from another species...--Purple 02:59, 11 March 2006 (UTC)
replies: text: Based on the term that sounds in the ballpark, it should go in :) Tyciol 11:54, 12 October 2006 (UTC)
thread_title: Cross-polymerisation?

message: I think a paragraph needs to be added to explain simply the effects and causes of this disease. Recovery statistics, treatments, etc. If this information is already on the page, it is too dificult to understand. Druidan 21:49, 1 May 2006 (UTC)
replies: text: The problem is that this is primarily an article about a set of proteins, not a disease. We need to work to bring about a page on amyloidosis itself. InvictaHOG 21:15, 3 August 2006 (UTC)
replies: text: This makes sense, it's kind of like wanting an article for atherosclerosis on the cholesterol article. This should remain neutral to simply describing the physical properties, with a note leading to further emphasis on the disease it causes when building up extracellularly, especially in brain tissue for Alzheimers seeing as how popular that is to talk about. Tyciol 11:54, 12 October 2006 (UTC)
replies: text: Amyloidosis is a fascinating disease which can more than fill its own article. Bits of both amyloid and amyloidosis will most likely end up on the other page, but separating the clinical syndrome and causes from the biochemistry seems like a natural break. It will probably improve both articles to limit the focus. Your cholesterol/atherosclerosis analogy is a good one! InvictaHOG 12:51, 12 October 2006 (UTC)

text: It's still on my list. Sorry, I'll probably work on it in November! InvictaHOG 01:33, 11 October 2006 (UTC)

text: Bio guys sure are crazy, but hey, comes with figuring out how you're basically descended from bacteria :p Tyciol 11:54, 12 October 2006 (UTC)
replies: text: Most people are crazy, in my experience. InvictaHOG 12:51, 12 October 2006 (UTC)
thread_title: English please?

message: In the mid-1980s, Pittsburgh Mayor Richard S. Caliguiri was diagnosed with amyloidosis.  Within a few years, three of Pennsylvania's most prominent political leaders were also afflicted with the disorder.  Caliguiri, longtime Erie Mayor Louis Tullio, and Governor Robert P. Casey were all diagnosed with the incurable and usually fatal disease.  All three eventually died from it.
: Maybe it's the scrapple? Amyloidosis has been linked to amyloid enhancing factor (AEF), which is found in diseased meat. And Pennsylvania Dutch cuisine is all about organ and scrap meats. Not to mention homemade preserving and canning. 70.184.72.38 17:54, 11 June 2007 (UTC)
thread_title: Unusual cluster among Pennsylvania politicians

message: I've nominated the prion article for peer review, any comments welcome here! --Purple 02:59, 11 March 2006 (UTC)
replies: text: Prions and amyloids are good together? Tyciol 11:54, 12 October 2006 (UTC)
thread_title: Prion peer review

message: This is mentioned in the article as a key point to explaining what amyloids are, but despite that, it lacks an article. I've honestly no clue, but if no one's going to do it yet, perhaps we can redirect it here, with an explanation of what it is, or theories or whatever, on this page? Tyciol 11:54, 12 October 2006 (UTC)
thread_title: Cross-beta

message: Hi. I've read this article, but I still have no idea what an Amyloid is. Can someone please explain in layman's terms? --Rebroad 23:24, 17 March 2007 (UTC)
replies: text: Gotta agree, and I possess at least a rudimentary (if dated) OChem background.  Perhaps a preliminary statement reading something like "potentially-harmful protein by product" or "a cellular deposit composed of proteins and manufactured as a by-product of protein processing, but otherwise similar to plaque/fatty deposits" ???  That's as close as I got after the opening 3-4 paragraphs.  --Sskoog 05:27, 28 March 2007 (UTC)
thread_title:  pardon?? 

message: The problem of ambiguity in this article is alluded to in the introduction. The histopathological definition, although historically first, is itself ambiguous. Amyloid in this context is an insoluble protein deposit that displays apple green birefringence when treated with congo red dye. The problem is that this definition provides no further insight beyond a phenomenological observation, although it accurately describes what histopathologists observe in their microscopes.
The biophysical definition is more precise, but the histopathologists do not like applying this more precise definition, perhaps because it encroaches on their linguistic domain. To avoid conflict, biophysicists have come to using the term "amyloid-like", as if anyone would know what amyloid is "like" without a biophysical characterization.
A new word is needed here, but that would ruffle more feathers than simply borrowing the old word. Welcome to science.  — Preceding unsigned comment added by 129.24.128.122 (talk) 00:12, 21 May 2014 (UTC)
thread_title:  You're excused 

message: The amyloid class of fold is different from the amyloid protein (which is so called because it adopts an amyloid fold). I vote for a disambiguation link
Although this technically correct, there is little information on this page as is. I would vote to complete this page before starting another--Biophysik (talk) 07:35, 6 October 2008 (UTC)
thread_title: Disambiguation

message: Substituted at 07:40, 29 April 2016 (UTC)
thread_title: Assessment comment

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thread_title:  External links modified 

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thread_title:  External links modified 

message: I am reading from the Buck Institute for Research on Aging that amyloid plaque may be a more complex phenomenon than previously thought.  Based on research from the lab of [Rudolph E. Tanzi]] at Harvard, it now is thought to be produced by the brain as a protection - or protective response rather than as causing the problem, since amyloid has been shown to kill microbes and to respond to chemical crises.  
Research wants to find out why the brain produces the amyloid as a response to three different toxic metabolic conditions: (1) inflammation (like oral bacteria) or spirochetes or fungi molds - or high sugar usage, which causes inflammation which activates inflammatory pathways, which includes making this amyloid, where the brain 'elaborates' this as a protectant; (2) Type II Alzheimers, a withdrawal of trophic support (a drop in estradiol, testosterone, vitamin D, nerve growth factor, brain-derived neurotrophic factor, et al.), many trophic molecules that support brain structure and the interactive synapses in the brain, where the response is to make amyloid as part of a brain-downsizing program; and (3) Type III Alzheimers, the amyloid plaque response may result from exposure to certain toxins (divalent metals, mercury, copper, iron, which amyloid binds tightly) or biotoxins, such as mycotoxins, lime-related toxins, etc..  
There may be two sides to the amyloid - both protective and capable of harming (neurodegeneration).  Many folks have been told that amyloid is a bad thing which gums up the brain and causes Alzheimers, but some research indicates that (a) the amyloid plaque is a protective development which may ALSO be neurodegenerative at some point.  Why does the brain 'need' to make this protective response which can ALSO lead to 'collateral damage' - protecting against organisms and binding toxins, but depending upon the genetic predisposition of the individual - to make more or less anyloid, in some this may lead to 'brain downsizing' far earlier than would be biologically necessary?
Also, I'm reading that working with large datasets about very complex organisms discloses that there may be three different root causes for this development, why the patients have the Alzheimer's pathology: inflammatory, atrophic, toxic reasons for producing the amyloid.  And there can be combinations of these reasons for the underlying degeneration, such as a glycotoxic insulin resistance which may also couple later with an atrophic response.
Can this be researched in order to improve the article? MaynardClark (talk) 22:14, 1 October 2017 (UTC)
replies: text: It is sad that almost 5 years since this important post by Maynard Clark, this issue has not been addressed in the article. I had to open the Talk page to become better informed. JD Lambert(T|C) 00:39, 12 August 2021 (UTC)
thread_title:  Protective? 

message: I think this section needs a total rework. It makes repeated references to figures that are not included in the section - only the first reference to the sigmoidal growth curve is included. More importantly, the language needs to be far more precise. In distinguishing the models the writing suggests that it is describing how fibrils form, but then in the "Most modern model" it suggests that fibrils form from...pre-existing fibrils that fragment and grow larger? This explains the exponential phase, but it's presented as an alternative to the previous models which focus on the kinetics of nucleation i.e. the lag phase. The first two models present a clear difference: can a single monomer form a "nucleus" or does it have to be an oligomeric non-nucleus that then converts into a nucleus. But once nucleation has occurred, fragmentation and growth is a separate model for the exponential phase. Finally, there is a statement about nucleation to the "surface" of the fibril rather than the ends. After going through a lot of papers on my own I understand somewhat better what mechanism this section is trying to describe, but it's unintelligible and possibly incorrect. This paper seems to pretty forcefully suggest that the mechanism is as follows: monomers can bind to the surface of existing fibrils, upon which they are rapidly converted to generate oligomers, which then fragments off to form a standalone fibril. Can someone with more expertise than me clean up this section and make it reasonably intelligible for non-experts? It took me quite a bit of work to figure out what was being described.   — Preceding unsigned comment added by 69.181.36.22 (talk) 01:33, 20 May 2020 (UTC)
thread_title:  Formation