Talk:Glycation

don't merge, move content to right page
I basically wrote both those articles at different times and, in light of 20/20 hind sight, didn't keep content on the correct pages. They are different things and need to remain separate as there are other routes to formation of AGEs. AGEs are a huge subject.

Glycation and glycosylation should also remain separate as they are distinct processes. Nonenzymatic glycosylation seems to be little used in the current literature, having been replaced by the more elegant single word. J W Anderson May 17, 2006


 * Along the lines of what I said on the Talk:Advanced glycation endproduct page, I agree with your assessment of the situation and would appreciate it if you implemented this plan of action. --Ben Best 03:21, 18 May 2006 (UTC)

merging glycation with advanced glycation endproducs
i think that theses article should not be merged rather should the "Glycation Article" focus on the chemical reactions (schiff base, amadori product, maillard reaction etc.) while it only gives a link to the "Advanced Glycation Article". In the "Advanced Glycation Endproducts Article" should be the endogenous role explained.


 * I would argue against this merger. AGEs are the product of both glycation and oxidation. An AGE is therefore distinct entity that should not be subsumed under "glycation". A more reasonable merger would be merging glycation with glycosylation because glycation is a non-enzymatic glycosylation, whereas glycosylation is (somewhat confusingly) equated with enzymatic glycosylation. --Ben Best 18:27, 14 May 2006 (UTC)

glucosepane
Recent research suggests that glucosepane is an important crosslink in aging. In Cross-linking of the extracellular matrix by the maillard reaction in aging and diabetes: an update on "a puzzle nearing resolution", Monnier VM, Mustata GT, Biemel KL, Reihl O, Lederer MO, Zhenyu D, Sell DR. write: " we provide an update of the field that leads to the conclusion that, while oxidation might be important for Maillard reaction-mediated cross-linking via Strecker degradation and allysine formation, the single most important collagen cross-link known to date in diabetes and aging is glucosepane, a lysyl-arginine cross-link that forms under nonoxidative conditions." PMID: 16037276

I am not sure where this information should be added.

It would also be good if someone more knowledgable than me could add an entry for glucosepane. --Manfred Bartz 10:45, 4 May 2006 (UTC)


 * I have created an entry for glucosepane, and have included an appropriate reference (not the same as the one you gave, but the same research team and the same year). --Ben Best 18:20, 14 May 2006 (UTC)

Merge
I took of the merge tag from both pages involved as the discussion seems to have reached a no consensus. -- Errant talk (formerly tmorton166) 12:57, 13 July 2006 (UTC)

red blood cells are NOT the shortest-living cells in the body!
In the section on endogenous glycation, this line appears: "Red blood cells are the shortest-lived cells in the body (120 days), so the half-life is about 240 days." Almost all the white blood cells, platelets, as well as epithelial (skin and gastrointestinal cells) live less than 120 days. The reason why RBCs are used to measure glucose levels over time is because they have a constant timeline with a relevant amount of time (4months) and are accessible relatively easily. —Preceding unsigned comment added by Shokod (talk • contribs) 03:54, 14 August 2008 (UTC)

I also believe that it is properly referred to as glycosylated hemoglobin, rather than glycated hemoglobin. The question would be whether it is glycosylated, glycated or both. Does anybody know? (1/31/09 —Preceding unsigned comment added by 198.22.21.50 (talk) 04:52, 1 February 2009 (UTC)

Lippincott's Illustrated Reviews: Biochemistry, 4th ed., refers to the HbA1c as being "nonenzymatically glycosylated" which appears to be a contradiction based on our definition. My best guess is that calling Hb "glycosylated" is technically not correct but commonplace enough it to be accepted casually. —Preceding unsigned comment added by 75.65.224.176 (talk) 07:53, 15 December 2009 (UTC)

Unfortunately there are many nomenclature issues related to chemically modified hemoglobins. But, according to p75 of Bunn and Forget's "Hemoglobin: molecular, genetic and clinical aspects": "The term "glycation" is preferable to "glycosylation" for designating ketoamine-linked glucose-protein adducts." —Preceding unsigned comment added by 76.165.219.25 (talk) 18:36, 31 March 2010 (UTC)

The Endogenous Section
Forgive me, I am new here. I didn't know how to appropriately show that much of the endogenous section was not cited. A lot of it seems to be logical, but the lack of citation makes it difficult to verify. BioSciEngr (talk) 15:03, 16 November 2009 (UTC)

Fructose and Galactose
Tell us more about these harmful sugars. Can I for example eat enzymes that convert fructose OR glucose to less-harmful sugars, like glucose?

91.214.167.2 (talk) 10:08, 14 July 2015 (UTC)

External links modified
Hello fellow Wikipedians,

I have just added archive links to 1 one external link on Glycation. Please take a moment to review my edit. You may add after the link to keep me from modifying it, if I keep adding bad data, but formatting bugs should be reported instead. Alternatively, you can add to keep me off the page altogether, but should be used as a last resort. I made the following changes:
 * Attempted to fix sourcing for http://www.alteon.com/scientific_publications/role/Vlassara.pdf

When you have finished reviewing my changes, please set the checked parameter below to true or failed to let others know (documentation at ).

Cheers.—cyberbot II  Talk to my owner :Online 06:54, 29 March 2016 (UTC)

Chemical Abstracts report
A search of Chemical Abstracts today for "glycation" yielded 33,827 references, of which 29,491 have appeared since the year 2000, 4,134 of these are reviews.--Smokefoot (talk) 14:42, 19 July 2019 (UTC)