Browsing by Author "Marzolo Canales, María Paz"
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- ItemA cytoplasmic PPPSP motif determines Megalin's phosphorylation and regulates receptor's recycling and surface expression(2007) Yuseff Sepúlveda, María Isabel; Marzolo Canales, María Paz
- ItemA RhoA Signaling Pathway Regulates Dendritic Golgi Outpost Formation(2015) Marzolo Canales, María Paz
- ItemA Sorting Nexin 17-Binding Domain Within the LRP1 Cytoplasmic Tail Mediates Receptor Recycling Through the Basolateral Sorting Endosome(2013) Farfán González, Pamela Soledad; Larios Yarur, Jorge Alberto; Marzolo Canales, María Paz
- ItemAdaptor protein sorting nexin 17 regulates amyloid precursor protein trafficking and processing in the early endosomes(2008) Lee, J.; Marzolo Canales, María Paz
- Itemalpha-Secretase-derived Fragment of Cellular Prion, N1, Protects against Monomeric and Oligomeric Amyloid beta (A beta)-associated Cell Death(2012) Guillot, M.; Marzolo Canales, María Paz
- ItemApical sorting of hepatitis B surface antigen (HBsAg) is independent of N-glycosylation and glycosylphosphatidylinositol-anchored protein segregation(1997) Marzolo Canales, María Paz; Bull Simpfendorfer, Paulina; González de la Rosa, Alfonso; Marzolo Canales, María Paz; Bull Simpfendorfer, Paulina; González de la Rosa, Alfonso
- ItemApoER2 and Reelin are expressed in regenerating peripheral nerve and regulate Schwann cell migration by activating the Rac1 GEF protein, Tiam1(2015) Pasten, C.; Cerda, J.; Jausoro, I.; Court G., Felipe; Caceres, A.; Marzolo Canales, María Paz
- ItemApoER2 expression increases Aβ production while decreasing Amyloid Precursor Protein (APP) endocytosis: Possible role in the partitioning of APP into lipid rafts and in the regulation of γ-secretase activity(2007) Fuentealba Alday, Rodrigo Esteban; Barría, M. I.; Lee, J.; Cam, J.; Araya, C.; Escudero, C. A.; Inestrosa Cantín, Nibaldo; Bronfman C., Francisca; Bu, G.; Marzolo Canales, María Paz
- ItemApoer2 Is Endocytosed by a Clathrin-Mediated Process Involving the Adaptor Protein Dab2 Independent of Its Rafts' Association(2005) Cuitino, Loreto.; Inestrosa Cantín, Nibaldo; Marzolo Canales, María Paz
- ItemEMBO Workshop al fin del mundo: a meeting on membrane trafficking and its implication for polarity and diseases(2015) Marzolo Canales, María Paz
- ItemExpression of α2-macroglobulin receptor/low density lipoprotein receptor-related protein (LRP) in rat microglial cells(2000) Marzolo Canales, María Paz; Bernhardi Montgomery, Rommy von; Inestrosa Cantín, Nibaldo
- ItemFunctional characterization of Lipophorin Receptors in the mushroom body of Drosophila melanogaster(2022) Rojo Cortés, Francisca Rayén; Marzolo Canales, María Paz; Campusano Astorga, Jorge Mauricio; Pontificia Universidad Católica de Chile. Facultad de Ciencias BiológicasLos receptores de lipoforina de Drosophila melanogaster (LpRs), LpR1 y LpR2, median la captación de lípidos. Los ortólogos de estos receptores en vertebrados, ApoER2 y VLDL-R, se unen a Reelina, la que no está presente en las moscas. Estas proteínas están asociadas con el desarrollo y función del hipocampo y la corteza cerebral. Actualmente se desconoce si los LpRs desempeñan funciones similares en el cerebro de Drosophila. Informamos que las moscas deficientes en LpRs exhiben una memoria olfativa y patrones de sueño alterados, los que parecen reflejar los defectos anatómicos encontrados en un área de asociación cerebral crítica, el cuerpo fungiforme (MB). Además, las neuronas del MB respondieron a Reelina aumentando su árbol neurítico. Este efecto depende de LpRs y Dab, el ortólogo en Drosophila de la proteína adaptadora del la señalización de Reelina Dab1. In vitro, dos isoformas largas de LpRs permitieron la internalización de Reelina. Además, se estudió la proteína no caracterizada anteriormente, la que dada su similitud con F-spondina y Reelina llamaremos Drospondina, como un posible ligando endógeno para los LpRs. Drospondina es expresada por una población de glía a lo largo del desarrollo. Dado que se encontró Drospondina rodeando los lóbulos del MB, estudiamos el MB de moscas deficientes para Drospondin, encontrándose defectos en su desarrollo. Además, la falta de Drospondina alteró la homeostasis del sueño. También encontramos que Drospondina interactúa genéticamente con los LpRs. Estos hallazgos demuestran que LpRs, Dab y Drospondina contribuyen al desarrollo y la función de MB, lo que respalda la existencia de señalización dependiente de estas proteínas en Drosophila.
- ItemInterfering of the Reelin/ApoER2/PSD95 Signaling Axis Reactivates Dendritogenesis of Mature Hippocampal Neurons(2017) Ampuero, E.; Jury, N.; Hartel, S.; Marzolo Canales, María Paz; Van Zundert, B.
- ItemLipophorin receptors regulate mushroom body development and complex behaviors in Drosophila(2022) Rojo Cortés, Francisca Rayén; Fuenzalida-Uribe, Nicolás; Tapia Valladares, Victoria; Roa, Candy B.; Hidalgo Sotelo, Sergio Ignacio; González Ramírez, María Constanza; Oliva Olave, Carlos Andrés; Campusano Astorga, Jorge Mauricio; Marzolo Canales, María PazBackground: Drosophila melanogaster lipophorin receptors (LpRs), LpR1 and LpR2, are members of the LDLR family known to mediate lipid uptake in a range of organisms from Drosophila to humans. The vertebrate orthologs of LpRs, ApoER2 and VLDL-R, function as receptors of a glycoprotein involved in development of the central nervous system, Reelin, which is not present in flies. ApoER2 and VLDL-R are associated with the development and function of the hippocampus and cerebral cortex, important association areas in the mammalian brain, as well as with neurodevelopmental and neurodegenerative disorders linked to those regions. It is currently unknown whether LpRs play similar roles in the Drosophila brain. Results: We report that LpR-deficient flies exhibit impaired olfactory memory and sleep patterns, which seem to reflect anatomical defects found in a critical brain association area, the mushroom bodies (MB). Moreover, cultured MB neurons respond to mammalian Reelin by increasing the complexity of their neurite arborization. This effect depends on LpRs and Dab, the Drosophila ortholog of the Reelin signaling adaptor protein Dab1. In vitro, two of the long isoforms of LpRs allow the internalization of Reelin, suggesting that Drosophila LpRs interact with human Reelin to induce downstream cellular events. Conclusions: These findings demonstrate that LpRs contribute to MB development and function, supporting the existence of a LpR-dependent signaling in Drosophila, and advance our understanding of the molecular factors functioning in neural systems to generate complex behaviors in this model. Our results further emphasize the importance of Drosophila as a model to investigate the alterations in specific genes contributing to neural disorders.
- ItemLipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease(2009) Marzolo Canales, María Paz
- ItemMannose receptor is present in a functional state in rat microglial cells(1999) Marzolo Canales, María Paz; Bernhardi Montgomery, Rommy von; Inestrosa Cantín, Nibaldo
- ItemMegalin and Cubilin Expression in Gallblandder Epithelium and Regulation by Bile Acids(2004) Erranz, Benjamín.; Miquel P., Juan Francisco; Marzolo Canales, María Paz
- ItemMorphogens, New Passengers on Lipoprotein Particles(2006) Marzolo Canales, María Paz
- ItemNew Insights into the Roles of Megalin/LRP2 and the Regulation of its Functional Expression(2011) Marzolo Canales, María Paz