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Iv Joint Meeting of the Biology Societies of Argentina BIOCELL, Vol. 45, Suppl. 3, 2021 ABSTRACTS ISSN 0327- 9545 A1 / A261 ISSN 1667-5746 (online version) Abstracts from the IV JOINT MEETING OF THE BIOLOGY SOCIETIES OF ARGENTINA (Cuarta Reunión Conjunta de Sociedades de Biología de la República Argentina) XXXVII Annual Scientific Meeting of the Tucumán Biology Association XXIII Annual Scientific Meeting of the Córdoba Biology Society XXXVIII Annual Scientific Meeting of the Cuyo Biology Society Argentine Biology Society Rosario Biology Society Chilean Society of Reproduction and Development September 9–15, 2020 Online edition The abstracts have been revised and evaluated by a Scientific Committee prior to publication 1 BIOCELL, Vol. 45, Suppl. 3, 2021 ABSTRACTS ISSN 0327- 9545 A1 / A261 ISSN 1667-5746 (online version) SCIENTIFIC COMMITTEE ASOCIACIÓN DE BIOLOGÍA DE TUCUMÁN Dra. María Teresa Ajmat Dra. Patricia L. Albornoz Dr. Mario Fortuna Dr. Carlos Gamarra-Luques Dra. Lucrecia Iruzubieta Villagra Vet. Paula Ginevro Mag. Analía Salvatore Dr. Diego Grilli Dr. Federico Bonilla Dr. Eduardo Koch Dra. Liliana I. Zelarayán Dra. Myriam Laconi Dra. María Eugenia Pérez Dr. Luis López Dra. Elisa Ofelia Vintiñi Dra. Alejandra Mampel Dr. Walter Manucha Dr. Ricardo Masuelli SOCIEDAD DE BIOLOGÍA DE Dra. Marcela Michaut Dra. Adriana Telechea CÓRDOBA Dr. Roberto Yunes Dra. Graciela Borioli Dra. Paola Boeris Dra. Cecilia Conde SAN LUIS Dra. Marta Dardanelli Dra. Silvina Álvarez Dra. Elena Fernández Dra. Cristina Barcia Dr. Leonardo Fruttero Dra. María Eugenia Ciminari Dra. Susana Genti-Raimondi Dr. Juan Gabriel Chediack Dr. Alejandro Guidobaldi Dr. Fabricio Cid Dr. Edgardo Jofré Dra. Gladys Ciuffo Dra. Melina Musri Lic. Óscar Córdoba Mascali Dra. Graciela Panzetta-Dutari Dra. María Esther Escudero Dr. Germán Robert Dra. Susana Ferrari Dra. Luciana Torre Dra. Lucia Fuentes Dra. Cristina Torres Esp. Mónica Laurentina Gatica Dra. Nidia Noemí Gomez Dra. Marta Moglia Esp. Facundo Morales SOCIEDAD DE BIOLOGÍA DE Dra. Edith Pérez CUYO Dra. María Verónica Pérez Chaca Dra. Hilda Elizabeth Pedranzani MENDOZA Dra. Graciela Wendel Dra. Nora Arenas Dra. Alba Edith Vega Dra. Silvia Belmonte Dra. Liliana Villegas Dra. Alejandra Camargo Dr. Diego Cargnelutti SAN JUAN Dra. María Teresa Damiani Dra. Gabriela Feresín Dra. María Inés Echeverría 2 BIOCELL, Vol. 45, Suppl. 3, 2021 ABSTRACTS ISSN 0327- 9545 A1 / A261 ISSN 1667-5746 (online version) SOCIEDAD DE BIOLOGÍA DE ROSARIO Dra. Ariana Diaz Méd. Vet. Melina Gay Dra. Graciela Klekailo Dra. Milagros López Hiriart Dra. Stella Mattaloni Dra. Nidia Montechiarini Dra. Alejandra Peruzzo Dr. Claudio Luis Pidone Dra. Marta Posadas Dra. Mariana Raviola Dra. María Elena Tosello Dra. Silvina Villar SOCIEDAD ARGENTINA DE BIOLOGÍA Dra. Fernanda Parborell Dra. Débora Cohen Dra. Griselda Irusta Dra. Isabel María Lacau Dra. Silvina Pérez Martínez Dra. Evelin Elia Dra. Clara I. Marín Briggiler Dr. Leandro Miranda Dr. Pablo Cetica 3 BIOCELL, Vol. 45, Suppl. 3, 2021 ABSTRACTS ISSN 0327- 9545 A1 / A261 ISSN 1667-5746 (online version) LECTURES Opening Lecture (Cuyo Biology Society) A1 MELATONIN IN MITOCHONDRIA: PROTECTING AGAINST CLEAR AND PRESENT DANGERS Reiter RJ UT Health San Antonio, San Antonio, Texas USA. The circadian melatonin rhythm plays an essential role in reducing the development of diseases such as solid tumors which adopt cytosolic aerobic glycolysis (Warburg effect) to support their enhanced metabolism. Experimental data shows that solid mammary tumors depend on aerobic glycolysis during the day but likely revert to mitochondrial oxidative phosphorylation at night for ATP production. This conversion of diseased cells during the day to a healthier phenotype at night occurs under control of the circulating melatonin rhythm. When the nocturnal melatonin rise is inhibited by light exposure at night, cancer cells function in the diseased state 24/7. The ability of melatonin to switch cancer cells as well as other diseased cells, e.g., Alzheimer disease, fibrosis, hyperactivation of macrophages, etc., from aerobic glycolysis to mitochondrial oxidative phosphorylation may be a basic protective mechanism to reduce several different pathologies. When diseased cells prevent the product of glucose metabolism, pyruvate, from entering the mitochondria, it deprives the mitochondria of the ability to generate acetyl Co-A, which normally feeds the citric acid cycle and supports oxidative phosphorylation. Since acetyl Co-A is also a necessary co-factor for the synthesis of melatonin, which occurs in the mitochondria of normal cells, cancer cells also cannot synthesize melatonin, a molecule with significant anticancer activity. Lecture (Tucumán Biology Association) A2 REGULATION OF EXTRACELLULAR VESICLES RELEASE BY AUTOPHAGY Posse de Chaves E, Viveiros A Department of Pharmacology and Neuroscience and Mental Health Institute, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Canada. E-mail: [email protected] Autophagy and extracellular vesicles (EVs) are components of the cellular proteostasis network that keeps misfolded proteins in check and ensures they do not accumulate in the cell or trigger deleterious effects. In the Central Nervous System, all cell types release EVs that are taken up by neighboring cells or are released into the cerebrospinal fluid and blood. EVs carry amyloidogenic proteins and potentially spread the disease from one cell to another. There is growing evidence of intense crosstalk between autophagy and EVs. Our lab has studied the regulation of EV secretion by autophagy in the context of cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases, specifically the transmission of amyloid beta peptide (A). We developed a protocol to label EVs in vivo in cultured cells using the fluorescent lipid DiI, and we analysed cell-derived EV preparations, virtually unprocessed, by Imaging Flow Cytometry (IFC) and nanoparticle tracking analysis (NTA) as reliable methods to understand EV secretion regulation. We demonstrated that blockade of autophagic flux causes a significant increase in EV release. Extensive autophagic- lysosomal pathology in Alzheimer’s disease (AD) brain contributes to disease pathogenesis, although the underlying mechanisms are not well understood. Using the reporter mcherry-GFP-LC3 we found that A42 blocks autophagic flux in cultured cells and mice in vivo. Thus, we examined if A42 increases EV secretion and promotes its own cell-to-cell transfer. Our data, using IFC and NTA analysis indicate that A-induced autophagy blockade increases EV secretion and favors cell-to-cell transfer of EVs, however we could not detect any significant increase of A spreading. Our results are important in the general context of EV release regulation and in neurodegenerative diseases since reversing autophagy dysfunction in AD is considered a valuable innovative therapeutic strategy. Lecture (Cuyo Biology Society) A3 COVID-19: MELATONIN AS A SOLE OR ADJUVANT TREATMENT Reiter RJ UT Health San Antonio, San Antonio, Texas USA. Regulation of the melatonergic pathways, both pineal and systemic, may be an important aspect in how viruses drive the cellular changes that underpin their control of cellular function. Viral, or preexistent, suppression of pineal melatonin disinhibits neutrophil attraction, thereby contributing to an initial "cytokine storm", as well as the regulation of other immune cells. Melatonin induces the circadian gene, Bmal1, which disinhibits the 4 BIOCELL, Vol. 45, Suppl. 3, 2021 ABSTRACTS ISSN 0327- 9545 A1 / A261 ISSN 1667-5746 (online version) pyruvate dehydrogenase complex (PDC), countering viral inhibition of Bmal1/PDC. PDC drives mitochondrial conversion of pyruvate to acetyl- coenzyme A (acetyl-CoA), thereby increasing the citric acid cycle, oxidative phosphorylation, and ATP production. Pineal melatonin suppression attenuates this, preventing the circadian "resetting" of mitochondrial metabolism. This is especially relevant in immune cells, where shifting metabolism from glycolytic to oxidative phosphorylation switches cells from reactive to quiescent phenotypes. Acetyl-CoA is a necessary cosubstrate for arylalkylamine N-acetyltransferase, providing an acetyl group to serotonin, and thereby initiating the melatonergic pathway. Virus- and cytokine- storm-driven control of the pineal and mitochondrial melatonergic pathway therefore regulates immune responses. The focus of this presentation will be the role of melatonin, an immune regulator, and its treatment implications for COVID-19 and other viral infections Lecture (Argentinean Biology Society) A4 MOLECULAR MECHANISMS OF ADAPTATION TO HYPOXIA IN Drosophila melanogaster Wappner P Instituto Leloir y FBMC, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires. E-mail: [email protected] Animal cells have the capacity to adapt to low oxygen levels (hypoxia), through several different mechanisms that depend on changes in their transcription profile. The Hypoxia Inducible Factor (HIF) is the master regulator of transcriptional responses to hypoxia conserved throughout the animal kingdom. It is a heterodimer composed of two subunits that belong to the bHLH-PAS family of transcription factors, where the beta-subunit is constitutive, and the alpha-subunit is regulated by oxygen levels. In normoxia, one or more HIF prolyl residues are hydroxylated in a reaction catalyzed by specific prolyl-4-hydroxylases. Hydroxylated HIF prolyl residues can be then recognized by the Von Hippel Lindau (VHL) tumor suppressor factor, which is part of an E3
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