Talk:Amyloid-beta precursor protein

A fact from Amyloid-beta precursor protein appeared on Wikipedia's Main Page in the Did you know column on 29 January 2007. The text of the entry was as follows:

Did you know... that human amyloid precursor protein (pictured), when cleaved by specific types of proteases, generates the amyloid beta peptide that may be a cause of Alzheimer's disease?

A record of the entry may be seen at Wikipedia:Recent additions/2007/January.

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Molecular Biology: MCB

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Holy cow. I am impressed. A five eyed genius !--Filll 03:30, 29 January 2007 (UTC)[reply]

Thanks ;) I don't know about this one, but I hope to make amyloid beta an FA eventually. Opabinia regalis 06:08, 31 January 2007 (UTC)[reply]

this article might give more information on what app does: NeuroRx: THe Journal of the American Society for experimental NeuroTherapeutics (2005) Vol. 2, 612-626 01:56, 4 April 2007 (UTC)ashok

Gamma-secretase[edit]

Gamma-secretase is now much more fully understood than this article indicates. presenillin 1 forms the core of the enzyme, but yeast two hybrid assays have shown interactions with several other proteins and nicastrin, Aph1A and PEN2 have been shown to be critical for gamme secretease activity. I will do the proper edit when I get some time. Povmcdov 14:32, 14 April 2007 (UTC)[reply]

The gamma secretase article has that information. This article does say gamma secretase is "a large multi-subunit complex whose components have not yet been fully characterized, but notably include presenilin, whose gene has been identified as a major genetic risk factor for Alzheimer's." I think it's fine as is. Flyguy649^talk_contribs 14:46, 14 April 2007 (UTC)[reply]

Formatting help?[edit]

Just noticed that my previous change to add an updated protein infobox (using ProteinBoxBot data) messed up some formatting. In firefox, all the section edit links show up at the bottom, and in IE, the main text does not flow along the side of the new infobox. Anyone have any insights here? Cheers, AndrewGNF 16:44, 15 August 2007 (UTC)[reply]

Up-regulated has a hyphen[edit]

Or am I out-dated? —Preceding unsigned comment added by 201.9.218.149 (talk) 21:31, 17 February 2008 (UTC)[reply]

Sexual Behavoir[edit]

Amyloid precursor protein regulates libido in experimental rats^[1]

Difference between APP and prion[edit]

They are both part of amyloidosis. They both bind copper. Can anybody tell me the difference between PrP and APP? 137.186.47.81 (talk) 10:40, 8 March 2012 (UTC)[reply]

The amyloidoses are a family of diseases with one pathological feature in common: the presence of amyloid deposits in some tissues. The composition of that amyloid and the location of the deposits vary widely from one disease to another, something that is prominently and thoroughly addressed in amyloidosis. You really need to start reading and understanding the articles on these topics before you continue to edit (or suggest edits to) the articles in this area. If you read the articles at APP and PrP (as you've now been told several times to do) you'd know the difference between them. While APP's cleavage product beta amyloid and the protein PrP can both form amyloid deposits (beta amyloid in Alzheimer's disease, PrP in mammalian prion disease) that doesn't mean that both proteins are the same. By analogy, brick and wood can both be used to make houses, but that doesn't mean that brick and wood are the same material. TenOfAllTrades(talk) 16:35, 8 March 2012 (UTC)[reply]

It's very simple. A protein is defined by its amino acid sequence. APP and PrP are the names for two proteins, that have totally different amino acid sequences. Joannamasel (talk) 15:59, 8 March 2012 (UTC)[reply]

All that the prion article specifiez iz statistics on the bonding and molecular weight of a protein that can become protease resistant. Please avoid abbreviations. An earlier version of the document on protease resistant protein noted that prion was often found in amyloid fibres, and that Alzheimer's was a prion disease. It went on to define spiroid protein az normal, and sheet protein az diseased (ignoring a third barrel conformation that protease resistant protein can take). That turned out to be defective theory, as Brown showed that the presence of Manganese made prion mostly into a spiroid, while copper made it mostly into a sheet.^[2] Both proteins bind copper. Iz one part of the other? Or are they both merely found in amyloidosis.

"The plaques are composed of a tangle of regularly ordered fibrillar aggregates called amyloid fibers,^[3] a protein fold shared by other peptides such as the prions associated with protein misfolding diseases.", is a segment of beta amyloid, so I submit that APP and PrP are the same, that PrP is part of APP, or that this sentence needs to be re-cast to make it clearly distinguish between amyloid precursor protein and protease resistant protein. PrP becomes protease resistant when it forms (part of) amyloid plaques.

Okay, so finally I got PrP, as different from prion. HAH! That's retarded, and yet I sit corrected. 137.186.47.81 (talk) 17:19, 9 March 2012 (UTC)[reply]

^ Park, J. H.; Bonthius, P. J.; Tsai, H. -W.; Bekiranov, S.; Rissman, E. F. (2010). "Amyloid Precursor Protein Regulates Male Sexual Behavior". Journal of Neuroscience. 30 (30): 9967–9972. doi:10.1523/JNEUROSCI.1988-10.2010. PMC 3040978. PMID 20668181. {{cite journal}}: no-break space character in |title= at position 9 (help)
^ Zhu, F.; Davies, P.; Thompsett, A. R.; Kelly, S. M.; Tranter, G. E.; Hecht, L.; Isaacs, N. W.; Brown, D. R.; Barron, L. D. (2008). "Raman Optical Activity and Circular Dichroism Reveal Dramatic Differences in the Influence of Divalent Copper and Manganese Ions on Prion Protein Folding†". Biochemistry. 47 (8): 2510–2517. doi:10.1021/bi7022893. PMID 18205409.
^ Parker MH, Reitz AB (2000). "Assembly of β-Amyloid Aggregates at the Molecular Level". Chemtracts-Organic Chemistry. 13 (1): 51–56.

[1] Park, J. H.; Bonthius, P. J.; Tsai, H. -W.; Bekiranov, S.; Rissman, E. F. (2010). "Amyloid Precursor Protein Regulates Male Sexual Behavior". Journal of Neuroscience. 30 (30): 9967–9972. doi:10.1523/JNEUROSCI.1988-10.2010. PMC 3040978. PMID 20668181. {{cite journal}}: no-break space character in |title= at position 9 (help)

[2] Zhu, F.; Davies, P.; Thompsett, A. R.; Kelly, S. M.; Tranter, G. E.; Hecht, L.; Isaacs, N. W.; Brown, D. R.; Barron, L. D. (2008). "Raman Optical Activity and Circular Dichroism Reveal Dramatic Differences in the Influence of Divalent Copper and Manganese Ions on Prion Protein Folding†". Biochemistry. 47 (8): 2510–2517. doi:10.1021/bi7022893. PMID 18205409.

[3] Parker MH, Reitz AB (2000). "Assembly of β-Amyloid Aggregates at the Molecular Level". Chemtracts-Organic Chemistry. 13 (1): 51–56.

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