Understanding the role of key amino acids in regulation of proline dehydrogenase/proline oxidase (prodh/pox)-dependent apoptosis/autophagy as an approach to targeted cancer therapy.
Apoptosis
Autophagy
Glutamine
Proline
Proline dehydrogenase/proline oxidase
Journal
Molecular and cellular biochemistry
ISSN: 1573-4919
Titre abrégé: Mol Cell Biochem
Pays: Netherlands
ID NLM: 0364456
Informations de publication
Date de publication:
Mar 2020
Mar 2020
Historique:
received:
30
08
2019
accepted:
04
01
2020
pubmed:
15
1
2020
medline:
8
10
2020
entrez:
15
1
2020
Statut:
ppublish
Résumé
In stress conditions, as neoplastic transformation, amino acids serve not only as nutrients to maintain the cell survival but also as mediators of several regulatory pathways which are involved in apoptosis and autophagy. Especially, under glucose deprivation, in order to maintain the cell survival, proline and glutamine together with other glutamine-derived products such as glutamate, alpha-ketoglutarate, and ornithine serve as alternative sources of energy. They are substrates for production of pyrroline-5-carboxylate which is the product of conversion of proline by proline dehydrogenase/ proline oxidase (PRODH/POX) to produce ATP for protective autophagy or reactive oxygen species for apoptosis. Interconversion of proline, ornithine, and glutamate may therefore regulate PRODH/POX-dependent apoptosis/autophagy. The key amino acid is proline, circulating between mitochondria and cytoplasm in the proline cycle. This shuttle is known as proline cycle. It is coupled to pentose phosphate pathway producing nucleotides for DNA biosynthesis. PRODH/POX is also linked to p53 and AMP-activated protein kinase (AMPK)-dependent pathways. Proline availability for PRODH/POX-dependent apoptosis/autophagy is regulated at the level of collagen biosynthesis (proline utilizing process) and prolidase activity (proline supporting process). In this review, we suggest that amino acid metabolism linking TCA and Urea cycles affect PRODH/POX-dependent apoptosis/autophagy and the knowledge might be useful to targeted cancer therapy.
Identifiants
pubmed: 31933109
doi: 10.1007/s11010-020-03685-y
pii: 10.1007/s11010-020-03685-y
pmc: PMC7028810
doi:
Substances chimiques
Neoplasm Proteins
0
Proline
9DLQ4CIU6V
Proline Oxidase
EC 1.5.3.-
PRODH protein, human
EC 1.5.5.2
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
35-44Subventions
Organisme : Polish National Science Center
ID : 2017/25/B/NZ7/02183
Organisme : H2020 Marie Skłodowska-Curie Actions
ID : 754432
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