1,720,995 research outputs found
Cell bioenergetics: Simple logics, complex solution
Full text linkCells are open systems that exchange energy and molecules with their environment. As any material system, they perform all the complex activities required for homeostasis and reproduction, obeying the thermodynamic laws. This viewpoint will argue that the basic logic governing the energy flux required to preserve cell organization and function is simple: to decrease the activation energy (Ea) of specific processes. Almost none of the possible chemical reactions and energy transformations inside a cell occur at a measurable speed at room or body temperature. Enzymes or other macromolecular structures speed up particular transformations by decreasing the corresponding energetic barriers. However, to maintain the systems in a homeostatic state, capable of sophisticated functions based on this simple strategy requires an inconceivably complex solution. The conclusion will point to the challenging and intricate problems that cells have solved to carve the highly regulated channel through which the energy flows, fueling the work of these nanoscale machines.Fil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentin
The Secret Ballet Inside Multivesicular Bodies
No full textLipid bilayers possess the capacity for self-assembly due to the amphipathic nature of lipid molecules, which have both hydrophobic and hydrophilic regions. When confined, lipid bilayers exhibit astonishing versatility in their forms, adopting diverse shapes that are challenging to observe through experimental means. Exploiting this adaptability, lipid structures motivate the development of bio-inspired mechanomaterials and integrated nanobio-interfaces that could seamlessly merge with biological entities, ultimately bridging the gap between synthetic and biological systems. In this work, we demonstrate how, in numerical simulations of multivesicular bodies, a fascinating evolution unfolds from an initial semblance of order toward states of higher entropy over time. We observe dynamic rearrangements in confined vesicles that reveal unexpected limit shapes of distinct geometric patterns. We identify five structures as the basic building blocks that systematically repeat under various conditions of size and composition. Moreover, we observe more complex and less frequent shapes that emerge in confined spaces. Our results provide insights into the dynamics of multivesicular systems, offering a richer understanding of how confined lipid bodies spontaneously self-organize.Fil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Masone, Diego Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentin
Molecular thermodynamics for cell biology as taught with boxes
Full text linkThermodynamic principles are basic to an understanding of the complex fluxes of energy and information required to keep cells alive. These microscopic machines are nonequilibrium systems at the micron scale that are maintained in pseudo-steady-state conditions by very sophisticated processes. Therefore, several nonstandard concepts need to be taught to rationalize why these very ordered systems proliferate actively all over our planet in seeming contradiction to the second law of thermodynamics. We propose a model consisting of boxes with different shapes that contain small balls that are in constant motion due to a stream of air blowing from below. This is a simple macroscopic system that can be easily visualized by students and that can be understood as mimicking the behavior of a set of molecules exchanging energy.With such boxes, the basic concepts of entropy, enthalpy, and free energy can be taught while reinforcing a molecular understanding of the concepts and stressing the stochastic nature of the thermodynamic laws. In addition, time-related concepts, such as reaction rates and activation energy, can be readily visualized. Moreover, the boxes provide an intuitive way to introduce the role in cellular organization of "information" and Maxwell's demons operating under nonequilibrium conditions.Fil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: López, María José. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas; ArgentinaFil: Becker, Wayne M.. Department of Botany; Estados Unido
A TEM-traceable physiologically functional gold nanoprobe that permeates non-endocytic cells
Full text linkBackground: Nanoparticles’ intracellular fate requires proper internalization. Most cells make use of a battery of internalization pathways, but some are practically sealed, as they lack the biochemical machinery for cellular intake. Non-endocytic cells, such as mammals’ spermatozoa, challenge standard drug-delivery strategies. Purpose: In this article, we present a gold nanoprobe that permeates the external and internal membranes of human sperm. Methods: Our design makes use of a gold nanoparticle functionalized with a membranepermeable cysteine-rich recombinant protein. The chimeric protein contains two units of physiologically active metallothioneins (MT) that also provide binding motifs to gold and a cell-penetrating-peptide sequence (CPP) that confers cell permeability to the nanoparticle. Results: Transmission electron microscopy, indirect immunofluorescence, and functional assays show that the nanoprobe is readily internalized in sperm, without compromising cell integrity, while preserving MT’s physiological activity. Our findings highlight the potential of CPP-functionalized nanogold for investigating the physiology of otherwise impermeable non-endocytic cells. Keywords: human sperm, metallothionein, gold nanoparticles functionalization, cell-penetrating peptides, transmission electron microscopyFil: Berberian, Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Pocognoni, Cristián Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentin
Flow cytometry protocol for GLUT4-myc detection on cell surfaces
No full textInsulin and muscle contraction trigger GLUT4 translocation to the plasma membrane, which increases glucose uptake by muscle cells. Insulin resistance and type 2 diabetes are the result of impaired GLUT4 translocation. Quantifying GLUT4 translocation is essential for comprehending the intricacies of both physiological and pathophysiological processes involved in glucose metabolism. The most commonly used methods for measuring GLUT4 translocation are the ELISA-type assay and the immunofluorescence assay. While some reports suggest that flow cytometry could be useful in quantifying GLUT4 translocation, this technique is not frequently used. Much of our current understanding of the regulation of GLUT4 has been based on experiments using the rat myoblast cell line (L6 cell) which expresses GLUT4 with a myc epitope on the exofacial loop. In the present study, we use the L6-GLUT4myc cell line to develop a flow cytometry-based approach to detect GLUT4 translocation. Flow cytometry offers the advantages of both immunofluorescence and ELISA-based assays. It allows easy identification of separate cell populations in the sample, similar to immunofluorescence, while providing results based on a population-level analysis of multiple individual cells, like an ELISA-based assay. Our results demonstrate a 0.6-fold increase with insulin stimulation compared to basal conditions. Finally, flow cytometry consistently yielded results across different experiments and exhibited sensitivity under the tested conditions.Fil: Zanni Ruiz, Emilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Histología y Embriología D/mend Dr.m.burgos; ArgentinaFil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Histología y Embriología D/mend Dr.m.burgos; ArgentinaFil: Pavarotti, Martin Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Histología y Embriología D/mend Dr.m.burgos; Argentin
Efecto de los anticuerpos monoclonales anti proteínas variable de superficie sobre el proceso de variación antigénica en Giardia Lamblia
Full text linkTesis (Doctor en Ciencias Químicas) - - Universidad Nacional de Córdoba. Facultad de Ciencias Químicas, 2016Fil: Torri, Alessandro. Universidad Católica de Córdoba. Facultad de Medicina. Cátedra de Química; Argentina.Fil: Torri, Alessandro. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas; Argentina.Fil: Luján, Hugo Daniel. Universidad Católica de Córdoba. Facultad de Medicina. Cátedra de Química; Argentina.Fil: Luján, Hugo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigación y Desarrollo en Inmunología y Enfermedades Infecciosas; Argentina.Fil: Barra, José Luis Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina.Fil: Barra, José Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina.Fil: Sotomayor, Claudia Elena. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Bioquímica Clínica; Argentina.Fil: Sotomayor, Claudia Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina.Fil: Rivero, Virginia Elena. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Bioquímica Clínica; Argentina.Fil: Rivero, Virginia Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina.Fil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina.Giardia lamblia es un parásito intestinal considerado como uno de los eucariotas más primitivos. Vive en el duodeno de los humanos y otros mamíferos y es el agente causante la giardiasis, una enfermedad que puede manifestarse clínicamente con diarrea aguda o crónica así como puede causar infecciones asintomáticas. Giardia está recubierto por proteínas de superficie que constituyen una interfase entre el parásito y el medio ambiente y que pertenecen a la familia de proteínas llamadas Proteínas Variables de Superficie (Variant-specific Surface Proteins - VSPs). Su genoma contiene aproximadamente entre 150 y 200 genes codificantes para estas proteínas, pero sólo una VSP es expresada sobre la superficie de cada parásito en un dado momento y puede ser recambiada por otra mediante un mecanismo de regulación post transcripcional. Los estímulos que inducen este recambio son aún desconocidos. Varios estudios han sugerido que anticuerpos monoclonales contra una VSP específica podrían tener efectos citotóxicos sobre Giardia. En el presente trabajo de tesis se demuestra no sólo que los anticuerpos monoclonales contra VSPs no tiene efecto citotóxico sobre el parásito, sino también que son un estímulo que induce variación antigénica in vitro, sugiriendo que la presión del sistema inmunitario podría ser la principal causa de la variación antigénica in vivo.Giardia lamblia is an intestinal protozoan considered one of the most primitive eukaryotes. It lives in the small intestine of humans and other mammals and is the causative agent of giardiasis. This disorder is characterized by clinical manifestations ranging from asymptomatic infection to acute or chronic diarrhea, and closely related to malabsorption. Giardia is covered with a specific surface protein, which is a true interface between the parasite and the environment, and belong to a family of proteins called Variant-specific surface proteins (VSPs). Its genome contains a repertoire from 150 to 200 genes encoding these proteins, but only one VSP is expressed on the surface of each parasite at a particular time and can switches to a different VSP by unknown stimuli through a post transcriptional regulation. Several studies have suggested that monoclonal antibodies against a specific VSP may have cytotoxic effect on Giardia. Through this work it is demonstrated not only that • inmunoglobulins do not have a cytotoxic effect but also induce antigenic variation in vitro, suggesting that the inimune system pression can be a major cause of antigenic switching in vivo.Fil: Torri, Alessandro. Universidad Católica de Córdoba. Facultad de Medicina. Cátedra de Química; Argentina.Fil: Torri, Alessandro. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas; Argentina.Fil: Luján, Hugo Daniel. Universidad Católica de Córdoba. Facultad de Medicina. Cátedra de Química; Argentina.Fil: Luján, Hugo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigación y Desarrollo en Inmunología y Enfermedades Infecciosas; Argentina.Fil: Barra, José Luis Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina.Fil: Barra, José Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina.Fil: Sotomayor, Claudia Elena. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Bioquímica Clínica; Argentina.Fil: Sotomayor, Claudia Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina.Fil: Rivero, Virginia Elena. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Bioquímica Clínica; Argentina.Fil: Rivero, Virginia Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina.Fil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
In silico testing the fundamental mechanisms and logic of intracellular traffic
Full text linkIntracellular traffic is a central process in cellular physiology. Numerous macromolecules must be transported in the endocytic and exocytic pathways for the correct function of eukaryotic cells. However, the way by which macromolecules are transported between compartments is still a matter of intense debate. Our group has developed a simulation platform, based on a combination of agent-based modeling and ordinary differential equations, for processes that occur in dynamic organelles that merge, divide, and change position and shape, while altering their composition by complex networks of molecular interactions and chemical reactions. We have already described how this modeling strategy successfully reproduces transport in the endocytic pathway. Our next objective is to apply this modeling approach to the trafficking within the Golgi apparatus. It is worth mentioning that several hypotheses regarding this issue are still in conflict, despite the abundance of experimental results and the development of ingenious probes to assess transport. Interestingly, our modeling strategy is flexible enough to simulate all these hypotheses and test the agreement between the different models and experimental data. At present, we have successfully modeled the transport of small and large membrane-associated cargos using the “cisternal progression/maturation” hypothesis. We expect that the active dialogue between simulations and experimental results will foster our understanding of the logic underlying the transport mechanisms that efficiently sort a large number of macromolecules to their final destination inside and outside the cell.Fil: Cebrián, José Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Pavarotti, Martin Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaLV Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; XIV Congreso de la Asociación Panamericana de Bioquímica y Biología MolecularSaltaArgentinaSociedad Argentina de Investigación en Bioquímica y BiologíaAsociación Panamericana de Bioquímica y Biología Molecula
ESCRT (endosomal sorting complex required for transport) machinery is essential for acrosomal exocytosis in human sperm
Full text linkThe sperm acrosome reaction is a unique, regulated exocytosis characterized by the secretion of the acrosomal content and the release of hybrid vesicles formed by patches of the outer acrosomal and plasma membranes. In previous reports, we have shown that inward invaginations of the acrosomal membrane delineate ring-shaped membrane microdomains that contact the plasma membrane. We have postulated that the opening and expansion of fusion pores along these rings trigger acrosomal exocytosis. The invaginations of the acrosomal membrane topologically resemble the deformations of the endosomal membrane leading to the assembly of luminal vesicles in multivesicular bodies. In fact, intra-acrosomal vesicles are also formed during acrosomal exocytosis. Endosomal sorting complex required for transport (ESCRT) participates in the organization of membrane microdomains that are invaginated and released as intraluminal vesicles in endosomes. We report here that members of ESCRT I (TSG101), ESCRT III (CHMP4), and the AAA ATPase VPS4 are present in the acrosomal region of the human sperm. Perturbing the function of these factors with antibodies or recombinant proteins inhibited acrosomal exocytosis in permeabilized cells. A similar effect was observed with a dominant-negative mutant of VPS4A cross-linked to a cell-penetrating peptide in nonpermeabilized sperm stimulated with a calcium ionophore. When the function of ESCRTs was inhibited, acrosomes showed abnormal deformation of the acrosomal membrane, and SNARE proteins that participate in acrosomal exocytosis failed to be stabilized in neurotoxin-resistant complexes. However, the growing of membrane invaginations was not blocked, and numerous intra-acrosomal vesicles were observed. These observations indicate that ESCRT-mediated processes are essential for acrosomal secretion, implicating these multifunctional complexes in an exocytic event crucial for sperm-egg fusion.Fil: Pocognoni, Cristián Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Berberian, Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentin
Differential requirement of Rab22a for the recruitment of ER-derived proteins to phagosomes and endosomes in dendritic cells
Full text linkThe recruitment of endoplasmic reticulum (ER) components to dendritic cell (DC) phagosomes and endosomes is a crucial event to achieve efficient cross-presentation of exogenous antigens. We have previously identified the small GTPase Rab22a as a key regulator of MHC-I trafficking and antigen cross-presentation by DCs. In this study we show that low expression of Rab22a does not prevent the normal delivery of ER-derived proteins to DC phagosomes. In contrast, the presence of these proteins was diminished in endosomes labelled with a fluid phase marker. These observations were confirmed by a functional assay that assesses the translocation of a soluble protein to the cytosol. Interestingly, we also demonstrate that early endosomal maturation is altered in Rab22a deficient DCs. Our results indicate that Rab22a plays a major role in endosomal function and highlight the importance of studying the endocytic and phagocytic pathways separately in DCs.Fil: Croce, Cristina Celeste. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Cebrián, José Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentin
The Synaptotagmin-1 C2B Domain Is a Key Regulator in the Stabilization of the Fusion Pore
Full text linkFusion pores serve as an effective mechanism to connect intracellular organelles and release vesicle contents during exocytosis. A complex lipid rearrangement takes place as membranes approximate, bend, fuse, and establish a traversing water channel to define the fusion pore, linking initially isolated chambers. Thermodynamically, the process is unfavorable and thought to be mediated by specialized proteins. In this work, we have developed a reaction coordinate to induce fusion pores from initially flat and parallel lipid bilayers and we have used it to describe the effects of the synaptotagmin-1 C2B domain during the process. We have obtained free-energy profiles of the whole lipid reorganization in biologically realistic membranes, going from planar and parallel bilayers through stalk hemifusion to water channel formation. Our results point to a lysine-rich polybasic region on synaptotagmin-1 C2B as the key to lipid reorganization control through the formation of phosphatidylinositol bisphosphate clusters that stabilize the fusion pore.Fil: Caparotta, Marcelo Rubén. Universidad Nacional de Cuyo; ArgentinaFil: Tomes, Claudia Nora. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Masone, Diego Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentin
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