hallmark of aging is mithocondrial disfunction.
Carnosine is present in large amounts in skeletal
muscle and is actively synthesized by muscle cells in culture
MG-damaged proteins and other aberrant polypeptides can induce ROS generation, promote mitochondrial dysfunction and inhibit proteasomal activity
carnosine and anserine could
decrease membrane lipid oxidation rates
It is suggested that carnosine forms a complex with copper in a manner that decreases the reactivity of copper and that carnosine might be capable of
scavenging free radicals
ages
inflammation
oxidative stress
its made by two amminoacids banked together: l histidine and beta alanine.
sugars react with proteins and form cross cross linked avanced glycosilation endproducts (AGEs). Carnosine inhibits formation of cross links by reacting wuth aldheydes, MDA. lipofoscin is the result, age pigment.
Inhibits proteotoxicity and advanced lipoxidation adducts.
it binds copper ios and lipid peroxidation.
high glucose – high MG – toxic effect and resembles aging
AGEs create inflammation which creates oxidative stress.
carnosine helps with glycosilation (glycation of proteins).
fly stick paper effect
carnosinase degrades carnosine levels.
carnosine is made by beta ??? and l-hystidine.
protecs LDL against glucose ninduced oxidation and glycation.
Hidrophilic carnosine competes with ldl particles for glucose. AGEs alter functioning of collagen.
Shiff base -> amadori rearrangement -> AGEs
high heat/dry cooking produces high AGEs
high buffering effect at the ph level.
it has good bioavailability and its readily available into the plasma.
protects cellular proteins from modifications when cerlls are exposed to glucose.
not only prevent but also reverses cross linking aging.
B alaine not effective alone on glycation and hystidine has shown potential toxicity.
bulk of carnosine is localized in the muscles. due to carnosinase in the other organs content is minimal, decreasses membrane lipid peroxidation.
coumpling of CA-pump
neutralizes LPO being accumulated.
Very good for cataracts.
chataracts are misfolded proteins in the lens of the eye. they are due to protein glycation
acetly form may be more resistant to breakdown into betalamine and histidine.
Can rejuvenate fibroblasts (increase in the hayflick limit)
it sacrifices itself instead of a protein in the formation of AGEs.
Most published/patented items on carnosine derive from Japan and the ex-Soviet Union and indicate anti-oxidant roles.
Carnosine is one of the few agents that can extend maximum cell division capacity (the Hayflick limit) of cultured human fibroblasts converting mature/senescent cells to juvenile phenotypes
glucose inside blood vessels, especially when a lot of glucose in the bloodstream.
Carnosine also inhibited cross-linking of the MG-treated ovalbumin to lysine and normal, untreated α-crystallin. We conclude that carnosine can react with protein CO groups (termed “carnosinylation”) and thereby modulate their deleterious interaction with other polypeptides. It is proposed that, should similar reactions occur intracellularly, then carnosine’s known “anti-aging” actions might, at least partially, be explained by the dipeptide facilitating the inactivation/removal of deleterious proteins bearing carbonyl groups.
Carnosine treatment decreased high MDA, DC and PC levels and caused significant increases in vitamin E level and SOD activity in the liver of aged rats. There were no changes in non-enzymatic and enzymatic antioxidants in the heart and brain of carnosine-treated aged rats. In conclusion, carnosine treatment was found to be useful in the decrease of age-related oxidative stress in the liver.
Although carnosine is read¬
ily metabolized in the body, its effects after in¬
jection are prolonged.17 This long-lasting action
cannot be explained by the appearance of
degradation products, since neither histidine
nor /3-alanine show similar effects, and high
doses of histidine actually depress physiologi¬
cal activity.8
Our observations with MDA and MAO b suggest the possibility that carnosine not only
scavenges ROS but also may reduce ROS
production. Carnosine treatment suppressed
MDA accumulation in brain membranes, but
also suppressed its production in response to
in vitro stimulation of LPO (Table 2). The ac¬
tivity of MAO b, a major generator of ROS, is
significantly higher in SAMPl brains than in
SAMR1,1 but, after treatment with carnosine,
falls to levels approaching those in the SAMR1
controls.