Advanced glycation endproducts in ageing and Alzheimer's disease

Münch, Gerald; Thome, Johannes; Foley, Paul; Schinzel, Reinhard; Riederer, Peter

doi:10.1016/s0165-0173(96)00016-1

Cited by 264 publications

(140 citation statements)

References 67 publications

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“…One of the factors triggering inflammation are advanced glycation endproducts (AGEs), which can be found in senile plaques (Mü nch et al, 1997). A role of oxidative damage in amyloid beta protein precursor-mediated cell death in cell cultures has also been suggested (Sopher et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

Alpha-lipoic acid as a new treatment option for Azheimer type dementia

Häger¹,

Marahrens²,

Kenklies³

et al. 2001

Archives of Gerontology and Geriatrics

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167

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Oxidative stress and energy depletion are characteristic biochemical hallmarks of Alzheimer's disease (AD), thus antioxidants with positive effects on glucose metabolism such as thioctic (a-lipoic) acid should exert positive effects in these patients. Therefore, 600 mg a-lipoic acid was given daily to nine patients with AD and related dementias (receiving a standard treatment with acetylcholinesterase inhibitors) in an open study over an observation period of, on avarage, 337 980 days. The treatment led to a stabilization of cognitive functions in the study group, demonstrated by constant scores in two neuropsychological tests (mini-mental state examination: MMSE and AD assessment scale, cognitive subscale: ADAScog). Despite the fact that this study was small and not randomized, this is the first indication that treatment with a-lipoic acid might be a successful 'neuroprotective' therapy option for AD and related dementias.

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Section: Discussionmentioning

confidence: 99%

Alpha-lipoic acid as a new treatment option for Azheimer type dementia

Häger¹,

Marahrens²,

Kenklies³

et al. 2001

Archives of Gerontology and Geriatrics

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167

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“…According to other authors, which used immunocytochemical techniques (Jackson and Lenney, 1996), the presence of the dipeptide would be restricted to the skeletal muscle and brain, although this might be linked to a sensitivity problem concerning the detection of this molecule using different techniques. The concentration of carnosine in the human skeletal muscle is very high (up to 20 mM) in comparison with other mammals, and a correlation between the amount of the dipeptide and the life span of the animals has been proposed (Munch et al, 1997). The features of aminoacyl-histidine dipeptides as a subset of small molecules which share similarities and which frequently coexist in the same tissue, raises the problem of their specific detection and discrimination using immunological techniques.…”

Section: Carnosine and Carnosine-related Dipeptidesmentioning

confidence: 99%

“…This consists of a series of posttranslational modifications in which protein amino groups and side chains react non-enzymatically with monosaccharides (forming the so called 'Amadori products'; Munch et al, 1997). The potential of carnosine to react with sugars is linked to its aminoacid sequence, which is similar to Lys-His, namely the preferred glycation sites in proteins (Shilton and Walton, 1991;Hipkiss et al, 1995).…”

Section: Inhibition Of Protein Glycosylationmentioning

confidence: 99%

“…In the process of protein glycosylation, subsequent oxidations and dehydrations lead to the formation of a wide range of products referred to as advanced glycation endproducts (AGEs). The accumulation of AGEs in the brain, as a cause of ageing/degeneration, has been proposed to play a direct role in the etiology and pathogenesis of Alzheimer's disease (Smith et al, 1995;Munch et al, 1997). Moreover, the reactions leading to the AGEs formation are accelerated by transition metals (which oxidize the protein-bound Amadori products) and involve the formation of oxigen free radicals.…”

Section: Inhibition Of Protein Glycosylationmentioning

confidence: 99%

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Carnosine-related dipeptides in the mammalian brain

Bonfanti

Peretto

Marchis

et al. 1999

Progress in Neurobiology

190

107

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-Carnosine and structurally related dipeptides are a group of histidine-containing molecules widely distributed in vertebrate organisms and particularly abundant in muscle and nervous tissue. Although many theories have been proposed, the biological function(s) of these compounds in the nervous system remains enigmatic. The purpose of this article is to review the distribution of carnosine-related dipeptides in the mammalian brain, with particular reference to some cell populations wherein these molecules have been demonstrated to occur very recently. The high expression of carnosine in the mammalian olfactory receptor neurons led to infer that this dipeptide could play a role as a neurotransmitter/modulator in olfaction. This prediction, which has not yet been fully demonstrated, does not explain the localization of carnosine-related dipeptides in other cell types, such as glial and ependymal cells. A recent demonstration of high carnosine-like immunoreactivity in the subependymal layer of rodents, an area of the forebrain which shares with the olfactory neuroepithelium the occurrence of continuous neurogenesis during adulthood, supports the hypothesis that carnosine-related dipeptides could be implicated in some forms of structural plasticity. However, the particular distribution of these molecules in the subependymal layer, along with their expression in glial/ependymal cell populations, suggests that they are not directly linked to cell migration or cell renewal. In the absence of a unified theory about the role of carnosine-related dipeptides in the nervous system, some common features shared by different cell populations of the mammalian brain which contain these molecules are discussed.

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“…An involvement in neurotransmission within the olfactory system has been proposed in the past [23]. Nevertheless, the distribution of carnosine-LI in the central nervous system (CNS), prevalently associated to glial/ependymal cells [3,7,26] along with the identification of several effects displayed by these molecules in vitro [4,5,13,18,24], strongly suggest that they could subserve other functions [7]. In the mammalian brain, carnosine has been detected almost exclusively in astrocytes, oligodendrocytes, ependymal cells and tanycytes [3,10,26; for review see Ref.…”

Section: Introductionmentioning

confidence: 99%

Aminoacyl-histidine dipeptides in the glial cells of the adult rabbit forebrain☆,1

et al. 2000

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The mammalian nervous system contains high amounts of the aminoacylhistidine dipeptides carnosine and homocarnosine. In the brain, they prevalently occur mainly in glial and ependymal cells, their role(s) still remaining obscure. In vitro studies indicate that these molecules exert diverse protective effects, and in vivo they are frequently associated with extracellular fluid compartments. Recently, carnosine-like immunoreactivity has been found in the subependymal layer (SEL) of adult rodents, a region endowed with persistent cell proliferation and migration. Unlike rodents, the SEL of the rabbit has a persistent olfactory ventricle. We show here that the morphologic organization of the SEL is different in these species, with particular reference to the glial/non glial cell compartments. The distribution of carnosine-like immunoreactivity in the rabbit displays some differences only within the SEL, which could be linked to its arrangement and compartmentalization.

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Advanced glycation endproducts in ageing and Alzheimer's disease

Cited by 264 publications

References 67 publications

Alpha-lipoic acid as a new treatment option for Azheimer type dementia

Alpha-lipoic acid as a new treatment option for Azheimer type dementia

Carnosine-related dipeptides in the mammalian brain

Aminoacyl-histidine dipeptides in the glial cells of the adult rabbit forebrain☆,1

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