If carnosine is used, it would be wise to use DMAE to remove lipofuscin that carnosine creates.
I think this is the paper that you are referring to...
Carnosine and protein carbonyl groups: a possible relationship.
Hipkiss AR.
Division of Biomolecular Sciences, GKT School of Biomedical Sciences, King's College London, London SE1 1UL, UK. alan.hipkiss@kcl.ac.uk.
Carnosine has been shown to react with low-molecular-weight aldehydes and ketones and has been proposed as a naturally occurring anti-glycating agent. It is suggested here that carnosine can also react with ("carnosinylate") proteins bearing carbonyl groups, and evidence supporting this idea is presented. Accumulation of protein carbonyl groups is associated with cellular ageing resulting from the effects of reactive oxygen species, reducing sugars, and other reactive aldehydes and ketones. Carnosine has been shown to delay senescence and promote formation of a more juvenile phenotype in cultured human fibroblasts. It is speculated that carnosine may intracellularly suppress the deleterious effects of protein carbonyls by reacting with them to form protein-carbonyl-carnosine adducts, i.e., "carnosinylated" proteins. Various fates of the carnosinylated proteins are discussed including formation of inert lipofuscin and proteolysis via proteosome and RAGE activities. It is proposed that the anti-ageing and rejuvenating effects of carnosine are more readily explainable by its ability to react with protein carbonyls than its well-documented antioxidant activity.
Publication Types:
* Review
PMID: 10951094 [PubMed - indexed for MEDLINE]
I don't think that it is that simple kurt. A few things can happen to a protein that is glycated/oxidized. The protein can form a cross-link or in the presence of carnoisne form a carnosinylated protein adduct. The fate of this carnosinylated protein adduct is still yet to be determined.
The possibility that this carnosinylated protein adduct could form lipofuscin comes from circumstantial support that carnosine is involved in lipofuscin synthesis because lipofuscin is usually found in large amounts in tissues rich in carnosine (muscle, nerve, and brain). The above paper argues that the lipofuscin formed from the carnosinylated protein adduct is a relatively inert by-product that's not capable of reacting with other cellular macromolecules.
Whilst carnosine appears to be relatively non-toxic a congential absence of the enzyme carnosinase coupled with excretion of large amount of carnosine is thought to be associated with mental retardation in humans. Hence, its thought that carnosine may have some unrecognized properties that are deleterious in some way. This is still just speculation though.
A recent study suggests that the histidine constituent of L-Carnosine (beta-alanine-histidine) is the active agent that results in carnosines ability to inhibit the productions of AGEs.
Anti-crosslinking properties of carnosine: significance of histidine.
Hobart LJ, Seibel I, Yeargans GS, Seidler NW.
Department of Biochemistry, University of Health Sciences, 1750 Independence Avenue, Kansas City, MO 64106-1453, USA.
Carnosine, a histidine-containing dipeptide, is a potential treatment for Alzheimer's disease. There is evidence that carnosine prevents oxidation and glycation, both of which contribute to the crosslinking of proteins; and protein crosslinking promotes beta-amyloid plaque formation. It was previously shown that carnosine has anti-crosslinking activity, but it is not known which of the chemical constituents are responsible. We tested the individual amino acids in carnosine (beta-alanine, histidine) as well as modified forms of histidine (alpha-acetyl-histidine, 1-methyl-histidine) and methylated carnosine (anserine) using glycation-induced crosslinking of cytosolic aspartate aminotransferase as our model. beta-Alanine showed anti-crosslinking activity but less than that of carnosine, suggesting that the beta-amino group is required in preventing protein crosslinking. Interestingly, histidine, which has both alpha-amino and imidazolium groups, was more effective than carnosine. Acetylation of histidine's alpha-amino group or methylation of its imidazolium group abolished anti-crosslinking activity. Furthermore, methylation of carnosine's imidazolium group decreased its anti-crosslinking activity. The results suggest that histidine is the representative structure for an anti-crosslinking agent, containing the necessary functional groups for optimal protection against crosslinking agents. We propose that the imidazolium group of histidine or carnosine may stabilize adducts formed at the primary amino group.
PMID: 15234195 [PubMed - indexed for MEDLINE]
You will most likely still get some sort of protein adduct after the reaction with histidine and in a similar fashion could increase lipofuscin production. Whether that lipofuscin is damanging is still not known.
In regards to DMAE and lipofuscin......what makes you think that DMAE protects against lipofuscin build up?
LongeCity
