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2 results on '"Giuseppe Cannino"'

1. HIF1α-dependent induction of the mitochondrial chaperone TRAP1 regulates bioenergetic adaptations to hypoxia

Author

Claudio Laquatra, Carlos Sanchez-Martin, Alberto Dinarello, Giuseppe Cannino, Giovanni Minervini, Elisabetta Moroni, Marco Schiavone, Silvio Tosatto, Francesco Argenton, Giorgio Colombo, Paolo Bernardi, Ionica Masgras, and Andrea Rasola

Subjects
Cytology, QH573-671
Abstract

Abstract The mitochondrial paralog of the Hsp90 chaperone family TRAP1 is often induced in tumors, but the mechanisms controlling its expression, as well as its physiological functions remain poorly understood. Here, we find that TRAP1 is highly expressed in the early stages of Zebrafish development, and its ablation delays embryogenesis while increasing mitochondrial respiration of fish larvae. TRAP1 expression is enhanced by hypoxic conditions both in developing embryos and in cancer models of Zebrafish and mammals. The TRAP1 promoter contains evolutionary conserved hypoxic responsive elements, and HIF1α stabilization increases TRAP1 levels. TRAP1 inhibition by selective compounds or by genetic knock-out maintains a high level of respiration in Zebrafish embryos after exposure to hypoxia. Our data identify TRAP1 as a primary regulator of mitochondrial bioenergetics in highly proliferating cells following reduction in oxygen tension and HIF1α stabilization.

Published
2021
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2. Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies

Author

Pierre Rustin, Eric Dufour, Praveen K. Dhandapani, Ana Andjelković, Marten Szibor, Marcos T. Oliveira, Giuseppe Cannino, Howard T. Jacobs, Cagri Yalgin, Institute of Biotechnology, Research Programme for Molecular Neurology, BioMediTech - BioMediTech, University of Tampere, Tampere Univ, Universidade Estadual Paulista (Unesp), Univ Helsinki, INSERM, and Universidade de São Paulo (USP)

Subjects
0301 basic medicine, Male, Models, Molecular, Mitochondrion, medicine.disease_cause, Protein Structure, Secondary, Animals, Genetically Modified, chemistry.chemical_compound, MITOCHONDRIA, Lääketieteen bioteknologia - Medical biotechnology, Drosophila Proteins, LIFE-SPAN, Plant Proteins, Mutation, Multidisciplinary, biology, RESPIRATORY PATHWAY, DEFECTS, Ciona intestinalis, DROSOPHILA, Drosophila melanogaster, Biochemistry, Gene Knockdown Techniques, Female, Oxidoreductases, EXPRESSION, Alternative oxidase, Ubiquinol, Transgene, Iron, Molecular Sequence Data, Article, Cell Line, Electron Transport Complex IV, Mitochondrial Proteins, 03 medical and health sciences, Oxygen Consumption, REVEALS, medicine, Cytochrome c oxidase, Animals, Humans, Amino Acid Sequence, Sequence Homology, Amino Acid, HUMAN-CELLS, fungi, biology.organism_classification, Protein Structure, Tertiary, Ciona, 030104 developmental biology, HEK293 Cells, chemistry, biology.protein, 1182 Biochemistry, cell and molecular biology, UNDERSTAND
Abstract

Made available in DSpace on 2018-11-26T16:18:57Z (GMT). No. of bitstreams: 0 Previous issue date: 2015-12-17 Academy of Finland (CoE grant) European Research Council EU (Marie Curie International Incoming Fellowship) Tampere University Hospital Medical Research Fund Sigrid Juselius Foundation The mitochondrial alternative oxidase, AOX, carries out the non proton-motive re-oxidation of ubiquinol by oxygen in lower eukaryotes, plants and some animals. Here we created a modified version of AOX from Ciona instestinalis, carrying mutations at conserved residues predicted to be required for chelation of the diiron prosthetic group. The modified protein was stably expressed in mammalian cells or flies, but lacked enzymatic activity and was unable to rescue the phenotypes of flies knocked down for a subunit of cytochrome oxidase. The mutated AOX transgene is thus a potentially useful tool in studies of the physiological effects of AOX expression. Tampere Univ, BioMediTech, FI-33014 Tampere, Finland Tampere Univ, Tampere Univ Hosp, FI-33014 Tampere, Finland Univ Estadual Paulista, Fac Ciencias Agr & Vet, Dept Tecnol, BR-14884900 Jaboticabal, SP, Brazil Univ Helsinki, Inst Biotechnol, FI-00014 Helsinki, Finland INSERM, UMR 1141, F-75019 Paris, France Univ Paris 07, Fac Med Denis Diderot, Hop Robert Debre, F-75019 Paris, France Univ Estadual Paulista, Fac Ciencias Agr & Vet, Dept Tecnol, BR-14884900 Jaboticabal, SP, Brazil Academy of Finland (CoE grant): 272376 European Research Council: 232738 EU (Marie Curie International Incoming Fellowship): 328988

Published
2015

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