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Article ; Online: An environmental measurement for a dynamic and endogenous global environmental Kuznets curve in the global context.

Pincheira, Roxana / Zúñiga, Felipe / Valencia, Francisco

Environmental science and pollution research international

2021 Volume 28, Issue 46, Page(s) 65573–65594

Abstract: Planetary boundaries (PB) is a novel conceptual framework that assesses the state of processes fundamental to the stability of the Earth system. Studies argue a non-linear relationship between economy and environmental degradation, known as the ... ...

Abstract	Planetary boundaries (PB) is a novel conceptual framework that assesses the state of processes fundamental to the stability of the Earth system. Studies argue a non-linear relationship between economy and environmental degradation, known as the environmental Kuznets curve (EKC). We postulate this inverted-U association between PB and economic output in a worldwide sample. This paper, therefore, examines the correlation between changes in environmental conditions and global economic growth, incorporating the growth rate of key control variables (population, financial development, merchandise trade and regulations). Thus, we intend to identify and address the main gaps in these EKC studies and analyse the impacts of worldwide economic growth on global environmental change. PB variables are identified as the more integrated perspective with regard to this change. These planetary boundaries include various proxies: global CO
MeSH term(s)	Carbon Dioxide ; Economic Development ; Hydrogen-Ion Concentration ; Investments ; Seawater
Chemical Substances	Carbon Dioxide (142M471B3J)
Language	English
Publishing date	2021-07-28
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1178791-0
ISSN	1614-7499 ; 0944-1344
ISSN (online)	1614-7499
ISSN	0944-1344
DOI	10.1007/s11356-021-14795-5
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Article: An environmental measurement for a dynamic and endogenous global environmental Kuznets curve in the global context

Pincheira, Roxana / Zúñiga, Felipe / Valencia, Francisco

Environmental science and pollution research. 2021 Dec., v. 28, no. 46

2021

Abstract	Planetary boundaries (PB) is a novel conceptual framework that assesses the state of processes fundamental to the stability of the Earth system. Studies argue a non-linear relationship between economy and environmental degradation, known as the environmental Kuznets curve (EKC). We postulate this inverted-U association between PB and economic output in a worldwide sample. This paper, therefore, examines the correlation between changes in environmental conditions and global economic growth, incorporating the growth rate of key control variables (population, financial development, merchandise trade and regulations). Thus, we intend to identify and address the main gaps in these EKC studies and analyse the impacts of worldwide economic growth on global environmental change. PB variables are identified as the more integrated perspective with regard to this change. These planetary boundaries include various proxies: global CO₂ concentration as a climate change proxy, threatened species for biodiversity loss, the total ozone for ozone depletion, mean surface ocean hydrogen ion concentration for ocean acidification and global fertiliser consumption for biochemical cycles. Under this integrated perspective, the EKC hypothesis is supported for climate change and ocean acidification panels using a dynamic system generalized method of moments (GMM) approach. Meanwhile, biochemical cycles, ozone depletion and freshwater use, land change and biodiversity loss boundaries do not support the existence of the EKC shape using the same methodology. The results provide an additional and novel view to be factored into the decisions of policymaker and investment institutions to contribute to sustainable development in all countries.
Keywords	biodiversity ; carbon dioxide ; climate change ; environmental Kuznets curve ; freshwater ; ocean acidification ; ozone ; ozone depletion ; pH ; pollution ; research ; sustainable development ; trade
Language	English
Dates of publication	2021-12
Size	p. 65573-65594.
Publishing place	Springer Berlin Heidelberg
Document type	Article
ZDB-ID	1178791-0
ISSN	1614-7499 ; 0944-1344
ISSN (online)	1614-7499
ISSN	0944-1344
DOI	10.1007/s11356-021-14795-5
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Article: SALL Proteins; Common and Antagonistic Roles in Cancer.

Álvarez, Claudia / Quiroz, Aracelly / Benítez-Riquelme, Diego / Riffo, Elizabeth / Castro, Ariel F / Pincheira, Roxana

Cancers

2021 Volume 13, Issue 24

Abstract: SALL proteins are a family of four conserved C2H2 zinc finger transcription factors that play critical roles in organogenesis during embryonic development. They regulate cell proliferation, survival, migration, and stemness; consequently, they are ... ...

Abstract	SALL proteins are a family of four conserved C2H2 zinc finger transcription factors that play critical roles in organogenesis during embryonic development. They regulate cell proliferation, survival, migration, and stemness; consequently, they are involved in various human genetic disorders and cancer. SALL4 is a well-recognized oncogene; however, SALL1-3 play dual roles depending on the cancer context and stage of the disease. Current reviews of SALLs have focused only on SALL2 or SALL4, lacking an integrated view of the SALL family members in cancer. Here, we update the recent advances of the SALL members in tumor development, cancer progression, and therapy, highlighting the synergistic and/or antagonistic functions they perform in similar cancer contexts. We identified common regulatory mechanisms, targets, and signaling pathways in breast, brain, liver, colon, blood, and HPV-related cancers. In addition, we discuss the potential of the SALL family members as cancer biomarkers and in the cancer cells' response to therapies. Understanding SALL proteins' function and relationship will open new cancer biology, clinical research, and therapy perspectives.
Language	English
Publishing date	2021-12-15
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers13246292
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Article: The Sall2 transcription factor promotes cell migration regulating focal adhesion turnover and integrin β1 expression.

Riffo, Elizabeth / Palma, Mario / Hepp, Matías I / Benítez-Riquelme, Diego / Torres, Vicente A / Castro, Ariel F / Pincheira, Roxana

Frontiers in cell and developmental biology

2022 Volume 10, Page(s) 1031262

Abstract: SALL2/Sall2 is a transcription factor associated with development, neuronal differentiation, and cancer. Interestingly, ...

Abstract	SALL2/Sall2 is a transcription factor associated with development, neuronal differentiation, and cancer. Interestingly,
Language	English
Publishing date	2022-11-09
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2022.1031262
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Article: Blocking the Farnesyl Pocket of PDEδ Reduces Rheb-Dependent mTORC1 Activation and Survival of

Armijo, Marisol Estrella / Escalona, Emilia / Peña, Daniela / Farias, Alejandro / Morin, Violeta / Baumann, Matthias / Klebl, Bert Matthias / Pincheira, Roxana / Castro, Ariel Fernando

Frontiers in pharmacology

2022 Volume 13, Page(s) 912688

Abstract: Rheb is a small GTPase member of the Ras superfamily and an activator of mTORC1, a protein complex master regulator of cell metabolism, growth, and proliferation. Rheb/mTORC1 pathway is hyperactivated in proliferative diseases, such as Tuberous Sclerosis ...

Abstract	Rheb is a small GTPase member of the Ras superfamily and an activator of mTORC1, a protein complex master regulator of cell metabolism, growth, and proliferation. Rheb/mTORC1 pathway is hyperactivated in proliferative diseases, such as Tuberous Sclerosis Complex syndrome and cancer. Therefore, targeting Rheb-dependent signaling is a rational strategy for developing new drug therapies. Rheb activates mTORC1 in the cytosolic surface of lysosomal membranes. Rheb's farnesylation allows its anchorage on membranes, while its proper localization depends on the prenyl-binding chaperone PDEδ. Recently, the use of PDEδ inhibitors has been proposed as anticancer agents because they interrupted KRas signaling leading to antiproliferative effects in KRas-dependent pancreatic cancer cells. However, the effect of PDEδ inhibition on the Rheb/mTORC1 pathway has been poorly investigated. Here, we evaluated the impact of a new PDEδ inhibitor, called Deltasonamide 1, in
Language	English
Publishing date	2022-06-23
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587355-6
ISSN	1663-9812
ISSN	1663-9812
DOI	10.3389/fphar.2022.912688
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Article: Cytosolic NUAK1 Enhances ATP Production by Maintaining Proper Glycolysis and Mitochondrial Function in Cancer Cells.

Escalona, Emilia / Muñoz, Marcelo / Pincheira, Roxana / Elorza, Álvaro A / Castro, Ariel F

Frontiers in oncology

2020 Volume 10, Page(s) 1123

Abstract: NUAK1 is an AMPK-related kinase located in the cytosol and the nucleus, whose expression associates with tumor malignancy and poor patient prognosis in several cancers. Accordingly, NUAK1 was associated with metastasis because it promotes cell migration ... ...

Abstract	NUAK1 is an AMPK-related kinase located in the cytosol and the nucleus, whose expression associates with tumor malignancy and poor patient prognosis in several cancers. Accordingly, NUAK1 was associated with metastasis because it promotes cell migration and invasion in different cancer cells. Besides, NUAK1 supports cancer cell survival under metabolic stress and maintains ATP levels in hepatocarcinoma cells, suggesting a role in energy metabolism in cancer. However, the underlying mechanism for this metabolic function, as well as its link to NUAK1 subcellular localization, is unclear. We demonstrated that cytosolic NUAK1 increases ATP levels, which associates with increased mitochondrial respiration, supporting that cytosolic NUAK1 is involved in mitochondrial function regulation in cancer cells. NUAK1 inhibition led to the formation of "donut-like" structures, providing evidence of NUAK1-dependent mitochondrial morphology regulation. Additionally, our results indicated that cytosolic NUAK1 increases the glycolytic capacity of cancer cells under mitochondrial inhibition. Nuclear NUAK1 seems to be involved in the metabolic switch to glycolysis. Altogether, our results suggest that cytosolic NUAK1 participates in mitochondrial ATP production and the maintenance of proper glycolysis in cancer cells. Our current studies support the role of NUAK1 in bioenergetics, mitochondrial homeostasis, glycolysis and metabolic capacities. They suggest different metabolic outcomes depending on its subcellular localization. The identified roles of NUAK1 in cancer metabolism provide a potential mechanism relevant for tumor progression and its association with poor patient prognosis in several cancers. Further studies could shed light on the molecular mechanisms involved in the identified metabolic NUAK1 functions.
Language	English
Publishing date	2020-07-10
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2649216-7
ISSN	2234-943X
ISSN	2234-943X
DOI	10.3389/fonc.2020.01123
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Article: NUAK1 coordinates growth factor-dependent activation of mTORC2 and Akt signaling.

Palma, Mario / Riffo, Elizabeth / Farias, Alejandro / Coliboro-Dannich, Viviana / Espinoza-Francine, Luis / Escalona, Emilia / Amigo, Roberto / Gutiérrez, José L / Pincheira, Roxana / Castro, Ariel F

Cell & bioscience

2023 Volume 13, Issue 1, Page(s) 232

Abstract: Background: mTORC2 is a critical regulator of cytoskeleton organization, cell proliferation, and cancer cell survival. Activated mTORC2 induces maximal activation of Akt by phosphorylation of Ser-473, but regulation of Akt activity and signaling ... ...

Abstract	Background: mTORC2 is a critical regulator of cytoskeleton organization, cell proliferation, and cancer cell survival. Activated mTORC2 induces maximal activation of Akt by phosphorylation of Ser-473, but regulation of Akt activity and signaling crosstalk upon growth factor stimulation are still unclear. Results: We identified that NUAK1 regulates growth factor-dependent activation of Akt by two mechanisms. NUAK1 interacts with mTORC2 components and regulates mTORC2-dependent activation of Akt by controlling lysosome positioning and mTOR association with this organelle. A second mechanism involves NUAK1 directly phosphorylating Akt at Ser-473. The effect of NUAK1 correlated with a growth factor-dependent activation of specific Akt substrates. NUAK1 induced the Akt-dependent phosphorylation of FOXO1/3a (Thr-24/Thr-32) but not of TSC2 (Thr-1462). According to a subcellular compartmentalization that could explain NUAK1's differential effect on the Akt substrates, we found that NUAK1 is associated with early endosomes but not with plasma membrane, late endosomes, or lysosomes. NUAK1 was required for the Akt/FOXO1/3a axis, regulating p21CIP1, p27KIP1, and FoxM1 expression and cancer cell survival upon EGFR stimulation. Pharmacological inhibition of NUAK1 potentiated the cell death effect induced by Akt or mTOR pharmacological blockage. Analysis of human tissue data revealed that NUAK1 expression positively correlates with EGFR expression and Akt Ser-473 phosphorylation in several human cancers. Conclusions: Our results showed that NUAK1 kinase controls mTOR subcellular localization and induces Akt phosphorylation, demonstrating that NUAK1 regulates the growth factor-dependent activation of Akt signaling. Therefore, targeting NUAK1, or co-targeting it with Akt or mTOR inhibitors, may be effective in cancers with hyperactivated Akt signaling.
Language	English
Publishing date	2023-12-22
Publishing country	England
Document type	Journal Article
ZDB-ID	2593367-X
ISSN	2045-3701
ISSN	2045-3701
DOI	10.1186/s13578-023-01185-2
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Article: Characterization of

Farkas, Carlos / Quiroz, Aracelly / Alvarez, Claudia / Hermosilla, Viviana / Aylwin, Carlos F / Lomniczi, Alejandro / Castro, Ariel F / Hepp, Matias I / Pincheira, Roxana

Frontiers in genetics

2021 Volume 12, Page(s) 613808

Abstract: The SALL2 transcription factor, an evolutionarily conserved gene through vertebrates, is involved in normal development and neuronal differentiation. In disease, SALL2 is associated with eye, kidney, and brain disorders, but mainly is related to cancer. ... ...

Abstract	The SALL2 transcription factor, an evolutionarily conserved gene through vertebrates, is involved in normal development and neuronal differentiation. In disease, SALL2 is associated with eye, kidney, and brain disorders, but mainly is related to cancer. Some studies support a tumor suppressor role and others an oncogenic role for SALL2, which seems to depend on the cancer type. An additional consideration is tissue-dependent expression of different SALL2 isoforms. Human and mouse
Language	English
Publishing date	2021-02-22
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2606823-0
ISSN	1664-8021
ISSN	1664-8021
DOI	10.3389/fgene.2021.613808
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Article ; Online: DISC1 promotes translation maintenance during sodium arsenite-induced oxidative stress.

Fuentes-Villalobos, Francisco / Farkas, Carlos / Riquelme-Barrios, Sebastián / Armijo, Marisol E / Soto-Rifo, Ricardo / Pincheira, Roxana / Castro, Ariel F

Biochimica et biophysica acta. Gene regulatory mechanisms

2019 Volume 1862, Issue 6, Page(s) 657–669

Abstract: Variation in Disrupted-in-Schizophrenia 1 (DISC1) increases the risk for neurodegenerative diseases, schizophrenia, and other mental disorders. However, the functions of DISC1 associated with the development of these diseases remain unclear. DISC1 has ... ...

Abstract	Variation in Disrupted-in-Schizophrenia 1 (DISC1) increases the risk for neurodegenerative diseases, schizophrenia, and other mental disorders. However, the functions of DISC1 associated with the development of these diseases remain unclear. DISC1 has been reported to inhibit Akt/mTORC1 signaling, a major regulator of translation, and recent studies indicate that DISC1 could exert a direct role in translational regulation. Here, we present evidence of a novel role of DISC1 in the maintenance of protein synthesis during oxidative stress. In order to investigate DISC1 function independently of Akt/mTORC1, we used Tsc2-/- cells, where mTORC1 activation is independent of Akt. DISC1 knockdown enhanced inhibition of protein synthesis in cells treated with sodium arsenite (SA), an oxidative agent used for studying stress granules (SGs) dynamics and translational control. N-acetyl-cysteine inhibited the effect of DISC1, suggesting that DISC1 affects translation in response to oxidative stress. DISC1 decreased SGs number in SA-treated cells, but resided outside SGs and maintained protein synthesis independently of a proper SG nucleation. DISC1-dependent stimulation of translation in SA-treated cells was supported by its interaction with eIF3h, a component of the canonical translation initiation machinery. Consistent with a role in the homeostatic maintenance of translation, DISC1 knockdown or overexpression decreased cell viability after SA exposure. Our data suggest that DISC1 is a relevant component of the cellular response to stress, maintaining certain levels of translation and preserving cell integrity. This novel function of DISC1 might be involved in its association with pathologies affecting tissues frequently exposed to oxidative stress.
MeSH term(s)	Animals ; Arsenites/pharmacology ; Cell Survival/drug effects ; Cytoplasmic Granules/metabolism ; DNA Helicases/metabolism ; Eukaryotic Initiation Factor-3/metabolism ; Gene Expression Regulation ; Gene Knockdown Techniques ; HEK293 Cells ; Humans ; Mechanistic Target of Rapamycin Complex 1 ; Mice ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Oncogene Protein v-akt ; Oxidative Stress/drug effects ; Poly-ADP-Ribose Binding Proteins/metabolism ; RNA Helicases/metabolism ; RNA Recognition Motif Proteins/metabolism ; Sodium Compounds/pharmacology ; Transcriptome ; Tuberous Sclerosis Complex 2 Protein/genetics
Chemical Substances	Arsenites ; DISC1 protein, human ; Eukaryotic Initiation Factor-3 ; Nerve Tissue Proteins ; Poly-ADP-Ribose Binding Proteins ; RNA Recognition Motif Proteins ; Sodium Compounds ; TSC2 protein, human ; Tuberous Sclerosis Complex 2 Protein ; sodium arsenite (48OVY2OC72) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Oncogene Protein v-akt (EC 2.7.11.1) ; DNA Helicases (EC 3.6.4.-) ; G3BP1 protein, human (EC 3.6.4.12) ; RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2019-05-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2918786-2
ISSN	1876-4320 ; 1874-9399
ISSN (online)	1876-4320
ISSN	1874-9399
DOI	10.1016/j.bbagrm.2019.05.001
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Article ; Online: Identification of a nuclear localization signal and importin beta members mediating NUAK1 nuclear import inhibited by oxidative stress.

Palma, Mario / Riffo, Elizabeth N / Suganuma, Tamaki / Washburn, Michael P / Workman, Jerry L / Pincheira, Roxana / Castro, Ariel F

Journal of cellular biochemistry

2019 Volume 120, Issue 9, Page(s) 16088–16107

Abstract: NUAK1 is a serine/threonine kinase member of the AMPK-α family. NUAK1 regulates several processes in tumorigenesis; however, its regulation and molecular targets are still poorly understood. Bioinformatics analysis predicted that the majority of NUAK1 ... ...

Abstract	NUAK1 is a serine/threonine kinase member of the AMPK-α family. NUAK1 regulates several processes in tumorigenesis; however, its regulation and molecular targets are still poorly understood. Bioinformatics analysis predicted that the majority of NUAK1 localizes in the nucleus. However, there are no studies about the regulation of NUAK1 subcellular distribution. Here, we analyzed NUAK1 localization in several human cell lines, mouse embryo fibroblasts, and normal mouse tissues. We found that NUAK1 is located in the nucleus and also in the cytoplasm. Through bioinformatics analysis and studies comparing subcellular localization of wild type and NUAK1 mutants, we identified a conserved bipartite nuclear localization signal at the N-terminal domain of NUAK1. Based on mass spectrometry analysis, we found that NUAK1 interacts with importin-β members including importin-β1 (KPNB1), importin-7 (IPO7), and importin-9 (IPO9). We confirmed that importin-β members are responsible for NUAK1 nuclear import through the inhibition of importin-β by Importazole and the knockdown of either IPO7 or IPO9. In addition, we found that oxidative stress induces NUAK1 cytoplasmic accumulation, indicating that oxidative stress affects NUAK1 nuclear transport. Thus, our study is the first evidence of an active nuclear transport mechanism regulating NUAK1 subcellular localization. These data will lead to investigations of the molecular targets of NUAK1 according to its subcellular distribution, which could be new biomarkers or targets for cancer therapies.
MeSH term(s)	Active Transport, Cell Nucleus ; Animals ; Cell Line ; Cytoplasm/metabolism ; HCT116 Cells ; HEK293 Cells ; HeLa Cells ; Humans ; MCF-7 Cells ; Mice ; Nuclear Localization Signals/metabolism ; Oxidative Stress ; Protein Kinases/genetics ; Protein Kinases/metabolism ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; beta Karyopherins/metabolism
Chemical Substances	Nuclear Localization Signals ; Repressor Proteins ; beta Karyopherins ; Protein Kinases (EC 2.7.-) ; NUAK1 protein, human (EC 2.7.1.-) ; NUAK1 protein, mouse (EC 2.7.1.-)
Language	English
Publishing date	2019-05-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	392402-6
ISSN	1097-4644 ; 0730-2312
ISSN (online)	1097-4644
ISSN	0730-2312
DOI	10.1002/jcb.28890
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