Talk:Glycation
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[edit] 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 Nonenzymatic glycosylation seems to be little used in the current literature, having been replaced by the more elegant single word.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)
[edit] 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)
[edit] 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)
[edit] 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)
