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2. Editorial: Autophagy in endocrine-metabolic diseases associated with aging: Volume II.

Author

Vaccaro, Maria Ines, De Tata, Vincenzo, and Gonzalez, Claudio Daniel

Subjects
BONE resorption, MESENCHYMAL stem cells, AUTOPHAGY, BREAST
Abstract

This document is an editorial published in the journal Frontiers in Endocrinology, discussing the role of autophagy in endocrine-metabolic diseases associated with aging. It explores the complex relationship between autophagy and diseases such as type 2 diabetes, thyroid dysfunctions, non-alcoholic fatty liver disease, endocrine cancer, and age-related degenerative diseases. The editorial also discusses the potential therapeutic implications of targeting autophagy in these conditions. Additionally, the document provides a list of references for two articles related to the role of sirtuins in osteoporosis and myocardial ischemia-reperfusion, offering valuable insights into mitochondrial quality control and autophagy regulation. [Extracted from the article]

Published
2024
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7. Efecto antitumoral de compuestos glicoconjugados sobre cultivos primarios de células de cáncer de páncreas obtenidas por ecoendoscopía

Author

Molejon, Maria Ines, Weiz, Gisela, Tellechea, Juan Ignacio, Breccia, Javier Dario, and Vaccaro, Maria Ines

Subjects
purl.org/becyt/ford/1 [https], Ciencias Biológicas, Biología Celular, Microbiología, FINE NEEDLE ASPIRATE, HYDROQUINONE, BIOPSY, VACUOLE-MEMBRANE PROTEIN 1, ADENOCARCINOMA, PANCREATIC, purl.org/becyt/ford/1.6 [https], CIENCIAS NATURALES Y EXACTAS
Abstract

El adenocarcinoma pancreático (PDAC), que constituye el 90% de los cánceres de páncreas, es la cuarta causa mundial de muertes relacionadas al cáncer. Debido a sus características moleculares y genéticas, PDAC pertenece al grupo de tumores con más resistencia al tratamiento quimioterápico. En la actualidad, las opciones terapéuticas disponibles incluyen la cirugía, la radiación, la quimioterapia, la inmunoterapia y drogas dirigidas. Sin embargo, la mayoría de los tratamientos son paliativos, con el objeto de disminuir los síntomas relacionados con la enfermedad. Por lo tanto, nuestro objetivo es evaluar el efecto de un compuesto glicosilado, la hidroquinona-rutinósido, sobre células tumorales pancreáticas primarias con el fin de buscar mayor efectividad de los tratamientos quimioterápicos actuales. Encontramos que la utilización de glicocompuestos como segunda línea de terapia mejora significativamente el efecto antitumoral de la gemcitabina. Estos resultados sugieren un potencial interés en la utilización de compuestos glicoconjugados como terapias complementarias a los tratamientos estándares contra el cáncer. Pancreatic ductal adenocarcinoma (PDAC), which constitutes 90% of pancreatic cancers, is the fourth leading cause of cancer-related deaths in the world. PDAC belongs to one of the most chemo resistant cancers, in part due to its molecularand genetics features. Currently, available therapeutic options are surgery, radiation, chemotherapy, and immunotherapy. Most of the available treatments are palliative, with the objective of relieving disease-related symptoms. Our aim was to evaluate the antitumoral effect as a second line therapy, of enzymatically glycosylated compounds, hydroquinone-rutinoside, on primary pancreatic tumoral cells. We found that glycoconjugates combined with antitumor agents, such as gemcitabine, improved single-treatment effects. These findings suggest that emerging trends towards glycoconjugates could be a promising approach for cancer therapies. Fil: Molejon, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina Fil: Weiz, Gisela. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina Fil: Tellechea, Juan Ignacio. Institución Médica Profensa; Argentina Fil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina Fil: Vaccaro, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina

Published
2019

9. The VMP1-Beclin 1 interaction regulates autophagy induction

Author

Molejon, Maria Ines, Ropolo, Alejandro Javier, Lo Ré, Andrea Emilia, Boggio, Veronica Ines, and Vaccaro, Maria Ines

Subjects
Medicina Básica, CIENCIAS MÉDICAS Y DE LA SALUD, Autophagy, Patología, purl.org/becyt/ford/3 [https], purl.org/becyt/ford/3.1 [https], VMP1, Beclin 1, Vps34
Abstract

Fil: Molejon, Maria Ines. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular; Argentina; Fil: Ropolo, Alejandro Javier. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular; Argentina; Fil: Lo Ré, Andrea Emilia. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular; Argentina; Fil: Boggio, Veronica Ines. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular; Argentina; Fil: Vaccaro, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular; Argentina

Published
2013

10. Autophagy, physiology and cell pathology

Author

Vaccaro, Maria Ines

Subjects
Medicina Básica, CIENCIAS MÉDICAS Y DE LA SALUD, Ciencias Médicas, Autophagy, mTOR, Patología, purl.org/becyt/ford/3 [https], purl.org/becyt/ford/3.1 [https], VMP1, Zymophagy
Abstract

Autophagy plays an important role in human pathologies, such as miopathies and neurodegenerative diseases. Moreover, metabolic disease processes such as diabetes and pancreatitis, as well as tumor cells and cancer chemotherapy, activate autophagy. Furthermore, a selective type of autophagy of pancreatic zymogen granules has been discovered and characterized as a protective cellular process triggered by acute pancreatitis. In this review we describe the physiological bases and molecular mechanisms in the autophagic process and the possible role of autophagy in human disease. Understanding the events and molecular mechanisms of this complex cellular process will help in the design of new strategies for more effective diagnosis and treatment., Sociedad Argentina de Fisiología

Published
2013

11. Beclin 1

Author

Molejon, Maria Ines, Ropolo, Alejandro Javier, and Vaccaro, Maria Ines

Subjects
Otras Ciencias de la Salud, PANCREAS, purl.org/becyt/ford/3.3 [https], CIENCIAS MÉDICAS Y DE LA SALUD, Ciencias de la Salud, BECLIN 1, AUTOPHAGY, purl.org/becyt/ford/3 [https]
Abstract

Beclin 1/ATG6/Vps30 (UniProtKB/Swiss-Prot Q14457) is a 450 amino-acids length protein, with three domains; BH3 (aminoacid 114 to 123), Coiled Coil domain (CCD; aminoacid 144 to 269) and the Evolutionarily Conserved Domain (ECD; aminoacid 244 to 337). BH3 proteins are part of the Bcl-2 family; they are pro-apoptotic damage sensors that play an important role in protecting against cancer (1). The BH3-only domain of Beclin 1 can interact with Bcl-2 and Bcl-XL (2;3). Both cellular and viral Bcl-2 (vBcl-2), or more specifically ER-targeted Bcl-2, inhibit Beclin 1-dependent autophagy by interfering with the Beclin 1-PtdIns 3-kinase interaction (PI3K) and the Beclin 1-associated PI3K activity (3,4). The interaction between Bcl-2 and Beclin 1 is greatly reduced upon starvation, which suggests that the dissociation of Bcl-2 from Beclin1 is important for activating autophagy. We demonstrated that, VMP1 (Vacuole Membrane Protein 1) displaces Bcl-2 from Beclin 1, partitioning Beclin 1 to the autophagic pathway (Molejon et al., Sci Rep. 2012; In press). Fil: Molejon, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; Argentina Fil: Ropolo, Alejandro Javier. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; Argentina Fil: Vaccaro, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; Argentina

Published
2012

12. Role of lncRNAs in Cellular Aging.

Author

Degirmenci, Ufuk, Sun Lei, Vaccaro, Maria Ines, and Stampfer, Martha Ruskin

Subjects
CELLULAR aging, NON-coding RNA, CELLULAR signal transduction
Abstract

Aging is a universal, intrinsic, and time-dependent biological decay that is linked to intricate cellular processes including cellular senescence, telomere shortening, stem cell exhaustion, mitochondrial dysfunction, and deregulated metabolism. Cellular senescence is accepted as one of the core processes of aging at the organism level. Understanding the molecular mechanism underlying senescence could facilitate the development of potential therapeutics for aging and age-related diseases. Recently, the discovery of long non-coding RNAs (lncRNA) provided insights into a novel regulatory layer that can intervene with cellular senescence. Increasing evidence indicates that targeting lncRNAs may impact on senescence pathways. In this review, we will focus on lncRNAs involved in mechanistic pathways governing cellular senescence. [ABSTRACT FROM AUTHOR]

Published
2016
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13. The HMG-I/Y-related Protein p8 Binds to p300 and Pax2trans-Activation Domain-interacting Protein to Regulate thetrans-Activation Activity of the Pax2A and Pax2B Transcription Factors on the Glucagon Gene Promoter

Author

Hoffmeister, Albrecht, primary, Ropolo, Alejandro, additional, Vasseur, Sophie, additional, Mallo, Gustavo V., additional, Bodeker, Hans, additional, Ritz-Laser, Beate, additional, Dressler, Gregory R., additional, Vaccaro, Maria Ines, additional, Dagorn, Jean-Charles, additional, Moreno, Silvia, additional, and Iovanna, Juan Lucio, additional

Published
2002
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14. Autophagy researchers.

Author

Juhász G, Puertollano R, Shimizu S, and Vaccaro MI

Subjects
Animals, Argentina, History, 20th Century, History, 21st Century, Humans, Hungary, Japan, Autophagy, Biology history, Research Personnel
Published
2013
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15. The HMG-I/Y-related protein p8 binds to p300 and Pax2 trans-activation domain-interacting protein to regulate the trans-activation activity of the Pax2A and Pax2B transcription factors on the glucagon gene promoter.

Author

Hoffmeister A, Ropolo A, Vasseur S, Mallo GV, Bodeker H, Ritz-Laser B, Dressler GR, Vaccaro MI, Dagorn JC, Moreno S, and Iovanna JL

Subjects
3T3 Cells, Amino Acid Sequence, Animals, Basic Helix-Loop-Helix Transcription Factors, COS Cells, Carrier Proteins metabolism, DNA-Binding Proteins chemistry, E1A-Associated p300 Protein, Growth Substances chemistry, HMGA1a Protein metabolism, HeLa Cells, Histidine chemistry, Humans, Mice, Models, Biological, Molecular Sequence Data, PAX2 Transcription Factor, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Trans-Activators chemistry, Transcription Factors chemistry, Transfection, Carrier Proteins chemistry, DNA-Binding Proteins metabolism, Glucagon genetics, Growth Substances metabolism, HMGA1a Protein chemistry, Neoplasm Proteins, Nuclear Proteins chemistry, Nuclear Proteins metabolism, Promoter Regions, Genetic, Trans-Activators metabolism, Transcription Factors metabolism, Transcriptional Activation
Abstract

p8 is a nuclear DNA-binding protein, which was identified because its expression is strongly activated in response to several stresses. Biochemical and biophysical studies revealed that despite a weak sequence homology p8 is an HMG-I/Y-like protein, suggesting that p8 may be involved in transcription regulation. Results reported here strongly support this hypothesis. Using a pull-down approach, we found that p8 interacts with the general co-activator p300. We also found that, similar to the HMG proteins, p300 was able to acetylate recombinant p8 in vitro, although the significance of such modification remains to be determined. Then a screening by the two-hybrid system, using p8 as bait, allowed us to identify the Pax2 trans-activation domain-interacting protein (PTIP) as another partner of p8. Transient transfection studies revealed that PTIP is a strong inhibitor of the trans-activation activities of Pax2A and Pax2B on the glucagon gene promoter, which was chosen as a model because it is a target of the Pax2A and Pax2B transcription factors. This effect is completely abolished by co-transfection of p8 in glucagon-producing InRIG9 cells, indicating that p8 binding to PTIP prevents inhibition of the glucagon gene promoter. This was not observed in NIH3T3 fibroblasts that do not express glucagon. Finally, expression of p8 enhances the effect of p300 on Pax2A and Pax2B trans-activation of the glucagon gene promoter. These observations suggest that in glucagon-producing cells p8 is a positive cofactor of the activation of the glucagon gene promoter by Pax2A and Pax2B, both by recruiting the p300 cofactor to increase the Pax2A and Pax2B activities and by binding the Pax2-interacting protein PTIP to suppress its inhibition.

Published
2002
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