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7. 8D.02

Author

Satoh, F., primary, Morimoto, R., additional, Ono, Y., additional, Iwakura, Y., additional, Omata, K., additional, Kudo, M., additional, Tkase, K., additional, Seiji, K., additional, Gomez-Sanchez, C., additional, Rainey, W., additional, Nakamura, Y., additional, Sasano, H., additional, and Ito, S., additional

Published
2015
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8. Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β

Author

Echeverría, P.C., Mazaira, G., Erlejman, A., Gomez-Sanchez, C., Pilipuk, G.P., and Galigniana, M.D.

Subjects
glycoprotein, radicicol, glycoprotein nup62, Active Transport, Cell Nucleus, animal cell, protein binding, Cell Line, Tacrolimus Binding Proteins, Mice, Receptors, Glucocorticoid, nuclear pore complex, protein cross linking, tetratricopeptide repeat, glucocorticoid receptor, Animals, Humans, heat shock protein 70, tetratricopeptide repeat protein, controlled study, HSP70 Heat-Shock Proteins, human, HSP90 Heat-Shock Proteins, heat shock protein 90, protein expression, mouse, Glycoproteins, cell membrane permeability, protein pp5, nonhuman, protein Fkbp52, human cell, protein p23, steroid, digitonin, article, protein function, beta Karyopherins, nuclear import, structure analysis, unclassified drug, Intramolecular Oxidoreductases, Nuclear Pore Complex Proteins, nuclear pore, priority journal, karyopherin beta, protein protein interaction, Multiprotein Complexes
Abstract

Glucocorticoid receptor (GR) is cytoplasmic in the absence of ligand and localizes to the nucleus after steroid binding. Previous evidence demonstrated that the hsp90-based heterocomplex bound to GR is required for the efficient retrotransport of the receptor to the nuclear compartment. We examined the putative association of GR and its associated chaperone heterocomplex with structures of the nuclear pore. We found that importin β and the integral nuclear pore glycoprotein Nup62 interact with hsp90, hsp70, p23, and the TPR domain proteins FKBP52 and PP5. Nup62 and GR were able to interact in a more efficient manner when chaperoned by the hsp90-based heterocomplex. Interestingly, the binding of hsp70 and p23 to Nup62 does not require the presence of hsp90, whereas the association of FKBP52 and PP5 is hsp90 dependent, as indicated by the results of experiments where the hsp90 function was disrupted with radicicol. The ability of both FKBP52 and PP5 to interact with Nup62 was abrogated in cells overexpressing the TPR peptide. Importantly, GR cross-linked to the hsp90 heterocomplex was able to translocate to the nucleus in digitonin-permeabilized cells treated with steroid, suggesting that GR could pass through the pore in its untransformed state. Copyright © 2009, American Society for Microbiology. All Rights Reserved. Fil:Echeverría, P.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.

Published
2009

13. Aldosterone does not Modify Gene Expression in Human Endothelial Cells

Author

Verhovez, A., additional, Williams, T., additional, Morello, F., additional, Monticone, S., additional, Brizzi, M., additional, Dentelli, P., additional, Fallo, F., additional, Fabris, B., additional, Amenta, F., additional, Gomez-Sanchez, C., additional, Veglio, F., additional, and Mulatero, P., additional

Published
2011
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14. ALDOSTERONE DOES NOT MODIFY GENE EXPRESSION IN HUMAN ENDOTHELIAL CELLS

Author

Verhovez, A., primary, Williams, T. A., additional, Crudo, V., additional, Burrello, J., additional, Covella, M., additional, Leone, D., additional, Berra, E., additional, Fallo, F., additional, Fabris, B., additional, Amenta, F., additional, Gomez-Sanchez, C. E., additional, Veglio, F., additional, and Mulatero, P., additional

Published
2011
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17. Early cardiovascular adaptation to simulated zero gravity

Author

Nixon, J. V, Murray, R. G, Bryant, C, Johnson, R. L., Jr, Mitchell, J. H, Holland, O. B, Gomez-Sanchez, C, Vergne-Marini, P, and Blomqvist, C. G

Subjects
Aerospace Medicine
Abstract

A study was conducted on five normal male volunteers (23-29 yr), under controlled conditions, to evaluate early adaptive responses to zero gravity. Specific objectives are (1) to characterize the hemodynamic, renal and hormonal responses to a central fluid shift, and (2) to compare data obtained during and after head-down tilt with corresponding data from actual space flight to validate tilt as a physiological model for simulation of zero gravity. Zero gravity is simulated by a 24-hr period of head-down tilt at 5 deg. The results suggest that hemodynamic adaptation occurs rapidly and is essentially accomplished by 6 hr, and that adaptation includes diuresis and reduction in blood volume. The validity of head-down tilt at 5 deg as an experimental model is established by comparing the results obtained with data from Apollo and Skylab astronauts on body fluid distributions and postflight responses to orthostatic and exercise stress.

Published
1979

27. Electrospinning of poly(lactic acid)/polyhedral oligomeric silsesquioxane nanocomposites and their potential in ehondrogenic tissue regeneration.

Author

Gomez-Sanchez, C., Kowalczyk, T., Ruiz De Eguino, G., Lopez-Arraiza, A., Infante, A., Rodriguez, C.I., Kowalewski, T.A., Sarrionandia, M., and Aurrekoetxea, J.

Subjects
*ELECTROSPINNING, *POLYLACTIC acid, *POLYHEDRAL functions, *OLIGOMERS, *SILICONES, *NANOCOMPOSITE materials, *REGENERATION (Biology), *BIODEGRADATION
Abstract

The study was conducted to evaluate the cytocompatibility and hydrolytic degradability of the new poly(lactic acid)/polyethylene glycol-polyhedral oligomerie silsesquioxane (peg-POSS/PLLA) nanocomposite as potenfial material for cartilage regeneration. PLLA scaffolds containing 0 to 5% of peg-POSS were fabricated by electrospinning. Human mesenchymal stem cells (hMSC's) were cultured in vitro to evaluate the cytocompafibility of the new nanocomposite material. Hydrolytic degradation studies were also carried out to analyze the mass loss rate of the nanoeomposites through time. The addition of the peg-POSS to the PLLA did not affect the processability of the nanocomposite by electrospinning. It was also observed that peg-POSS did not show any relevant change in fibers morphology, concluding that it was well dispersed. However, addifion of peg-POSS caused noticeable decrease in mean fiber diameter, which made the specific surface area of the scaffold to rise. hMSC's were able to attach, to proliferate, and to differenfiate into chondrocytes in a similar way onto the different types of electrospun peg-POSS/PLLA and pure PLLA scaffolds, showing that the peg-POSS as nano-additive does not exhibit any cytotoxicity. The hydrolytic degradation rate of the material was lower when peg- POSS was added, showing a higher durability of the nanocomposites through time. Results demonstrate that the addition of peg-POSS to the PLLA scaffolds does not affect its cytocompatibility to obtain hyaline cartilage from hMSC's. [ABSTRACT FROM AUTHOR]

Published
2014
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42. Aldosterone does not Modify Gene Expression in Human Endothelial Cells.

Author

Verhovez, A., Williams, T. A., Morello, F., Monticone, S., Brizzi, M. F., Dentelli, P., Fallo, F., Fabris, B., Amenta, F., Gomez-Sanchez, C., Veglio, F., and Mulatero, P.

Subjects
ALDOSTERONE, LUCIFERASES, ENDOTHELIAL seeding, GENE expression, CORONARY arteries, MINERALOCORTICOIDS
Abstract

The toxic effects of aldosterone on the vasculature, and in particular on the endothelial layer, have been proposed as having an important role in the cardiovascular pathology observed in mineralocorticoid-excess states. In order to characterize the genomic molecular mechanisms driving the aldosterone-induced endothelial dysfunction, we performed an expression microarray on transcripts obtained from both human umbilical vein endothelial cells and human coronary artery endothelial cells stimulated with 10-7M aldosterone for 18 h. The results were then subjected to qRT-PCR confirmation, also including a group of genes known to be involved in the control of the endothelial function or previously described as regulated by aldosterone. The state of activation of the mineralocorticoid receptor was investigated by means of a luciferase-reporter assay using a plasmid encoding a mineralocorticoid and glucocorticoid-sensitive promoter. Aldosterone did not determine any significant change in gene expression in either cell type both in the microarray and in the qRT-PCR analysis. The luciferase-reporter assay showed no activation of the mineralocorticoid receptor following aldosterone stimulation. The status of nonfunctionality of the mineralocorticoid receptor expressed in cultured human umbilical and coronary artery endothelial cells does not allow aldosterone to modify gene expression and provides evidence against either a beneficial or harmful genomic effect of aldosterone on healthy endothelial cells. [ABSTRACT FROM AUTHOR]

Published
2012
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