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dc.contributor.author
Chacon Cabrera, Alba
dc.contributor.author
Fermoselle, Clara
dc.contributor.author
Urtreger, Alejandro Jorge
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dc.contributor.author
Mateu Jimenez, Mercè
dc.contributor.author
Diament, Miriam
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dc.contributor.author
Bal, Elisa Dora
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dc.contributor.author
Sandri, Marco
dc.contributor.author
Barreiro, Eshter
dc.date.available
2017-12-12T21:09:39Z
dc.date.issued
2014-07
dc.identifier.citation
Chacon Cabrera, Alba; Fermoselle, Clara; Urtreger, Alejandro Jorge; Mateu Jimenez, Mercè; Diament, Miriam; et al.; Pharmacological strategies in lung cancer-induced cachexia: effects on muscle proteolysis, autophagy, structure, and weakness; Wiley; Journal of Cellular Physiology; 229; 11; 7-2014; 1660-1672
dc.identifier.issn
0021-9541
dc.identifier.uri
http://hdl.handle.net/11336/30354
dc.description.abstract
Muscle wasting and cachexia are important systemic manifestations of highly prevalent conditions including cancer. Inflammation, oxidative stress, autophagy, ubiquitin-proteasome system, nuclear factor (NF)-kB, and mitogen activated protein kinases (MAPK) are involved in the pathophysiology of cancer cachexia. Currently available treatment is limited and data demonstrating effectiveness in in vivo models are lacking. Our objectives were to explore in respiratory and limb muscles of lung cancer (LC) cachectic mice whether proteasome, NF-kB, and MAPK inhibitors improve muscle mass and function loss through several molecular mechanisms. Body and muscle weights, limb muscle force, protein degradation and the ubiquitin-proteasome system, signaling pathways, oxidative stress and inflammation, autophagy, contractile and functional proteins, myostatin and myogenin, and muscle structure were evaluated in the diaphragm and gastrocnemius of LC (LP07 adenocarcinoma) bearing cachectic mice (BALB/c), with and without concomitant treatment with NF-kB (sulfasalazine), MAPK (U0126), and proteasome (bortezomib) inhibitors. Compared to control animals, in both respiratory and limb muscles of LC cachectic mice: muscle proteolysis, ubiquitinated proteins, autophagy, myostatin, protein oxidation, FoxO-1, NF-kB and MAPK signaling pathways, and muscle abnormalities were increased, while myosin, creatine kinase, myogenin, and slow- and fast-twitch muscle fiber size were decreased. Pharmacological inhibition of NF-kB and MAPK, but not the proteasome system, induced in cancer-induced cachectic animals, a substantial restoration of muscle mass and force through a decrease in muscle protein oxidation and catabolism, myostatin, and autophagy, together with a greater content of myogenin, and contractile and functional proteins. These findings may offer new therapeutic strategies in cancer-induced cachexia.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Lung Cancer
dc.subject
Cachexia
dc.subject
Pharmacology
dc.subject
Autophagy
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Medicina Básica
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dc.subject.classification
CIENCIAS MÉDICAS Y DE LA SALUD
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dc.title
Pharmacological strategies in lung cancer-induced cachexia: effects on muscle proteolysis, autophagy, structure, and weakness
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-12-12T18:29:07Z
dc.identifier.eissn
1097-4652
dc.journal.volume
229
dc.journal.number
11
dc.journal.pagination
1660-1672
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Hoboken
dc.description.fil
Fil: Chacon Cabrera, Alba. Universitat Pompeu Fabra; España. Universidad Carlos III de Madrid. Instituto de Salud; España
dc.description.fil
Fil: Fermoselle, Clara. Universitat Pompeu Fabra; España. Universidad Carlos III de Madrid. Instituto de Salud; España
dc.description.fil
Fil: Urtreger, Alejandro Jorge. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Oncología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina
dc.description.fil
Fil: Mateu Jimenez, Mercè. Universidad Carlos III de Madrid. Instituto de Salud; España. Universitat Pompeu Fabra; España
dc.description.fil
Fil: Diament, Miriam. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Oncología; Argentina
dc.description.fil
Fil: Bal, Elisa Dora. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Oncología "Ángel H. Roffo"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina
dc.description.fil
Fil: Sandri, Marco. Università di Padova; Italia
dc.description.fil
Fil: Barreiro, Eshter. Universitat Pompeu Fabra; España. Universidad Carlos III de Madrid. Instituto de Salud; España
dc.journal.title
Journal of Cellular Physiology
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/jcp.24611
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