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27 results on '"Nicolás, Francisco J."'

1. Expert Revision of Key Elements for Clinical-Grade Production and Qualification of Perinatal Derivatives

Author

Gramignoli, Roberto, primary, Hofmann, Nicola, additional, Agudo-Barriuso, Marta, additional, Antica, Mariastefania, additional, Flores, Ana I, additional, Girandon, Lenart, additional, Kerdjoudj, Halima, additional, Navakauskiene, Ruta, additional, Schiavi, Jessica, additional, Scholz, Hanne, additional, Shablii, Volodymyr, additional, Lafarge, Xavier, additional, Nicolás, Francisco J, additional, and Gindraux, Florelle, additional

Published
2023
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5. Expert Consideration on Regulatory Aspects for Perinatal Derivatives in Clinical Settings

Author

Hofmann, Nicola, primary, Lafarge, Xavier, additional, Antica, Mariastefania, additional, Ferry, Nicolas, additional, Girandon, Lenart, additional, Gramignoli, Roberto, additional, Jurga, Marcin, additional, Kerdjoudj, Halima, additional, Navakauskiene, Ruta, additional, Schiavi, Jessica, additional, Shablii, Volodymyr, additional, Nicolás, Francisco J, additional, and Gindraux, Florelle, additional

Published
2023
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7. Perinatal derivatives application: Identifying possibilities for clinical use

Author

Gindraux, Florelle, primary, Hofmann, Nicola, additional, Agudo-Barriuso, Marta, additional, Antica, Mariastefania, additional, Couto, Pedro Silva, additional, Dubus, Marie, additional, Forostyak, Serhiy, additional, Girandon, Lenart, additional, Gramignoli, Roberto, additional, Jurga, Marcin, additional, Liarte, Sergio, additional, Navakauskiene, Ruta, additional, Shablii, Volodymyr, additional, Lafarge, Xavier, additional, and Nicolás, Francisco J., additional

Published
2022
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10. GMAI

Author

Alejandro J. Calderón, Leonidas Kosmidis, Carlos F. Nicolás, Francisco J. Cazorla, Peio Onaindia

Published
2020
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15. Cryopreserved amniotic membrane in the treatment of diabetic foot ulcers: a case series

Author

Valiente, Mónica Rodríguez, primary, Nicolás, Francisco J., additional, García-Hernández, Ana M., additional, Mora, Cristina Fuente, additional, Blanquer, Miguel, additional, Alcaraz, Patricio J., additional, Almansa, Sonia, additional, Merino, Guadalupe Ruiz, additional, Lucas, Ma Dolores López, additional, Algueró, María C., additional, Insausti, Carmen L., additional, Piñero, Antonio, additional, Moraleda, José M., additional, and Castellanos, Gregorio, additional

Published
2018
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18. Isolation and Characterization of Mesenchymal Stem Cells from the Fat Layer on the Density Gradient Separated Bone Marrow

Author

Insausti, Carmen L., primary, Blanquer Blanquer, Miguel, additional, Meseguer Olmo, Luis, additional, López-Martínez, María C., additional, Férez Ruiz, Xavier, additional, Rodríguez Lozano, Francisco J., additional, Cabañas Perianes, Valentín, additional, Funes, Consuelo, additional, Nicolás, Francisco J., additional, Majado, María J., additional, and Moraleda Jiménez, José M., additional

Published
2012
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19. Amniotic membrane induces epithelialization in massive posttraumatic wounds

Author

Insausti, Carmen L., primary, Alcaraz, Antonia, additional, García-Vizcaíno, Eva M., additional, Mrowiec, Anna, additional, López-Martínez, María C., additional, Blanquer, Miguel, additional, Piñero, Antonio, additional, Majado, María J., additional, Moraleda, José M., additional, Castellanos, Gregorio, additional, and Nicolás, Francisco J., additional

Published
2010
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25. Epithelial to mesenchymal transition in Madin-Darby canine kidney cells is accompanied by down-regulation of Smad3 expression, leading to resistance to transforming growth factor-beta-induced growth arrest.

Author

Nicolás, Francisco J, Lehmann, Kerstin, Warne, Patricia H, Hill, Caroline S, and Downward, Julian

Abstract

In normal epithelial cells, transforming growth factor-beta (TGF-beta) typically causes growth arrest in the G(1) phase of the cell cycle and may eventually lead to apoptosis. However, transformed cells lose these inhibitory responses and often instead show an increase in malignant character following TGF-beta treatment. In the canine kidney-derived epithelial cell line, MDCK, synergism between activation of the Raf/MAPK pathway and the resulting autocrine production of TGF-beta triggers transition from an epithelial to a mesenchymal phenotype. During this process, these cells become refractive to TGF-beta-induced cell cycle arrest and apoptosis. TGF-beta signals are primarily transduced to the nucleus through complexes of receptor-regulated Smads, Smad2 and Smad3 with the common mediator Smad, Smad4. Here we show that the transition from an epithelial to mesenchymal phenotype is accompanied by gradual down-regulation of expression of Smad3. Restoration of Smad3 to previous levels of expression restores the cell cycle arrest induced by TGF-beta without reverting the cells to an epithelial phenotype or impacting on the MAPK pathway. Regulation of apoptosis is not affected by Smad3 levels. These data attribute to Smad3 a critical role in the control of cell proliferation by TGF-beta, which is lost following an epithelial to mesenchymal transition.

Published
2003
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26. Xenopus Ran-binding protein 1: Molecular interactions and effects on nuclear assembly in Xenopus egg extracts

Author

Nicolás, Francisco J., Zhang, Chuanmao, Hughes, Mike, Goldberg, Martin W., Watton, Sandra J., and Clarke, Paul R.

Abstract

Ran is a nuclear GTPase implicated in nucleocytoplasmic transport, the maintenance of nuclear structure, mRNA processing, and cell cycle regulation. By two-hybrid interaction in yeast, we have identified a Xenopus homologue of Ran-binding protein 1 (RanBP1). Xenopus RanBP1 interacts specifically with the GTP-bound form of Ran and forms complexes in Xenopus egg extracts with Ran, importin-β/karyopherin-β and importin-α/karyopherin-α, but not p10, p120/RanBP7, RanBP2 or other nucleoporins. These complexes may play roles in the recycling of Ran and importins/karyopherins during nucleocytoplasmic transport. Increased concentrations of RanBP1 stabilise an interaction between Ran and RCC1 in egg extracts, inhibiting the exchange activity of RCC1 towards Ran. Under these conditions, the assembly of nuclei from chromatin is dramatically affected: the nuclei do not assemble a lamina and become very small with homogeneously condensed chromatin. They fail to actively import proteins and do not undergo DNA replication. By field emission in-lens scanning electron microscopy, we show that these nuclei have an intact nuclear envelope containing pore complexes, but the envelope is highly convoluted. However, RanBP1 does not directly inhibit nuclear protein import in assembled nuclei. These results suggest that RCC1 and/or Ran have a function early in nuclear assembly that is disrupted by RanBP1.

Published
1997
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27. SB-431542 is a potent and specific inhibitor of transforming growth factor-beta superfamily type I activin receptor-like kinase (ALK) receptors ALK4, ALK5, and ALK7.

Author

Inman GJ, Nicolás FJ, Callahan JF, Harling JD, Gaster LM, Reith AD, Laping NJ, and Hill CS

Subjects
3T3 Cells, Activating Transcription Factor 2, Activins pharmacology, Animals, Bone Morphogenetic Protein 4, Bone Morphogenetic Proteins pharmacology, Cells, Cultured, Cyclic AMP Response Element-Binding Protein metabolism, DNA-Binding Proteins metabolism, Drug Interactions, Enzyme Activation, Humans, JNK Mitogen-Activated Protein Kinases, Mice, Mitogen-Activated Protein Kinases metabolism, Osmotic Pressure drug effects, Phosphorylation drug effects, Protein Serine-Threonine Kinases, Rats, Receptor, Transforming Growth Factor-beta Type I, Signal Transduction drug effects, Smad Proteins, Trans-Activators metabolism, Transcription Factors metabolism, Transforming Growth Factor beta pharmacology, p38 Mitogen-Activated Protein Kinases, Activin Receptors, Type I antagonists & inhibitors, Enzyme Inhibitors pharmacology, Proteins, Receptors, Transforming Growth Factor beta antagonists & inhibitors, Transcription, Genetic drug effects
Abstract

Small molecule inhibitors have proven extremely useful for investigating signal transduction pathways and have the potential for development into therapeutics for inhibiting signal transduction pathways whose activities contribute to human diseases. Transforming growth factor beta (TGF-beta) is a member of a large family of pleiotropic cytokines that are involved in many biological processes, including growth control, differentiation, migration, cell survival, adhesion, and specification of developmental fate, in both normal and diseased states. TGF-beta superfamily members signal through a receptor complex comprising a type II and type I receptor, both serine/threonine kinases. Here, we characterize a small molecule inhibitor (SB-431542) that was identified as an inhibitor of activin receptor-like kinase (ALK)5 (the TGF-beta type I receptor). We demonstrate that it inhibits ALK5 and also the activin type I receptor ALK4 and the nodal type I receptor ALK7, which are very highly related to ALK5 in their kinase domains. It has no effect on the other, more divergent ALK family members that recognize bone morphogenetic proteins (BMPs). Consistent with this, we demonstrate that SB-431542 is a selective inhibitor of endogenous activin and TGF-beta signaling but has no effect on BMP signaling. To demonstrate the specificity of SB-431542, we tested its effect on several other signal transduction pathways whose activities depend on the concerted activation of multiple kinases. SB-431542 has no effect on components of the ERK, JNK, or p38 MAP kinase pathways or on components of the signaling pathways activated in response to serum.

Published
2002
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