ParkinsonFranceV1, Main, Exploration, bibRecord, 001159

Delaying aging and the aging-associated decline in protein homeostasis by inhibition of tryptophan degradation

Identifieur interne : 001159 ( Main/Exploration ); précédent : 001158; suivant : 001160

Delaying aging and the aging-associated decline in protein homeostasis by inhibition of tryptophan degradation

Auteurs : Annemieke T. Van Der Goot ; Wentao Zhu [Allemagne] ; Rafael P. Vázquez-Manrique [France] ; Renée I. Seinstra ; Katja Dettmer [Allemagne] ; Helen Michels ; Francesca Farina [France] ; Jasper Krijnen [Pays-Bas] ; Ronald Melki [France] ; Rogier C. Buijsman [Pays-Bas] ; Mariana Ruiz Silva ; Karen L. Thijssen ; Ido P. Kema [Pays-Bas] ; Christian Neri [France] ; Peter J. Oefner [Allemagne] ; Ellen A. A. Nollen [Pays-Bas]

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2012.

RBID : PMC:3443121

Abstract

Toxicity of aggregation-prone proteins is thought to play an important role in aging and age-related neurological diseases like Parkinson and Alzheimer’s diseases. Here, we identify tryptophan 2,3-dioxygenase (tdo-2), the first enzyme in the kynurenine pathway of tryptophan degradation, as a metabolic regulator of age-related α-synuclein toxicity in a Caenorhabditis elegans model. Depletion of tdo-2 also suppresses toxicity of other heterologous aggregation-prone proteins, including amyloid-β and polyglutamine proteins, and endogenous metastable proteins that are sensors of normal protein homeostasis. This finding suggests that tdo-2 functions as a general regulator of protein homeostasis. Analysis of metabolite levels in C. elegans strains with mutations in enzymes that act downstream of tdo-2 indicates that this suppression of toxicity is independent of downstream metabolites in the kynurenine pathway. Depletion of tdo-2 increases tryptophan levels, and feeding worms with extra l-tryptophan also suppresses toxicity, suggesting that tdo-2 regulates proteotoxicity through tryptophan. Depletion of tdo-2 extends lifespan in these worms. Together, these results implicate tdo-2 as a metabolic switch of age-related protein homeostasis and lifespan. With TDO and Indoleamine 2,3-dioxygenase as evolutionarily conserved human orthologs of TDO-2, intervening with tryptophan metabolism may offer avenues to reducing proteotoxicity in aging and age-related diseases.

Url:

DOI: 10.1073/pnas.1203083109
PubMed: 22927396
PubMed Central: 3443121

Affiliations:

Allemagne, France, Pays-Bas

Le document en format XML

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<front><div type="abstract" xml:lang="en"><p>Toxicity of aggregation-prone proteins is thought to play an important role in aging and age-related neurological diseases like Parkinson and Alzheimer’s diseases. Here, we identify tryptophan 2,3-dioxygenase (<italic>tdo-2</italic>
), the first enzyme in the kynurenine pathway of tryptophan degradation, as a metabolic regulator of age-related α-synuclein toxicity in a <italic>Caenorhabditis elegans</italic>
 model. Depletion of <italic>tdo-2</italic>
 also suppresses toxicity of other heterologous aggregation-prone proteins, including amyloid-β and polyglutamine proteins, and endogenous metastable proteins that are sensors of normal protein homeostasis. This finding suggests that <italic>tdo-2</italic>
 functions as a general regulator of protein homeostasis. Analysis of metabolite levels in <italic>C. elegans</italic>
 strains with mutations in enzymes that act downstream of <italic>tdo-2</italic>
 indicates that this suppression of toxicity is independent of downstream metabolites in the kynurenine pathway. Depletion of <italic>tdo-2</italic>
 increases tryptophan levels, and feeding worms with extra <sc>l</sc>
-tryptophan also suppresses toxicity, suggesting that <italic>tdo-2</italic>
 regulates proteotoxicity through tryptophan. Depletion of <italic>tdo-2</italic>
 extends lifespan in these worms. Together, these results implicate <italic>tdo-2</italic>
 as a metabolic switch of age-related protein homeostasis and lifespan. With TDO and Indoleamine 2,3-dioxygenase as evolutionarily conserved human orthologs of TDO-2, intervening with tryptophan metabolism may offer avenues to reducing proteotoxicity in aging and age-related diseases.</p>
</div>
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:22927396" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a ParkinsonFranceV1

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Data generation: Wed May 17 19:46:39 2017. Site generation: Mon Mar 4 15:48:15 2024

La maladie de Parkinson en France (serveur d'exploration)

Delaying aging and the aging-associated decline in protein homeostasis by inhibition of tryptophan degradation

Delaying aging and the aging-associated decline in protein homeostasis by inhibition of tryptophan degradation

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	La maladie de Parkinson en France (serveur d'exploration)
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.