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Article: Stressed to death: Mitochondrial stress responses connect respiration and apoptosis in cancer

Winter, Jacob M. / Yadav, Tarun / Rutter, Jared

Molecular cell. 2022 Sept. 15, v. 82, no. 18

2022

Abstract: Mitochondrial energetics and respiration have emerged as important factors in how cancer cells respond to or evade apoptotic signals. The study of the functional connection between these two processes may provide insight into following questions old and ... ...

Abstract	Mitochondrial energetics and respiration have emerged as important factors in how cancer cells respond to or evade apoptotic signals. The study of the functional connection between these two processes may provide insight into following questions old and new: how might we target respiration or downstream signaling pathways to amplify apoptotic stress in the context of cancer therapy? Why are respiration and apoptotic regulation housed in the same organelle? Here, we briefly review mitochondrial respiration and apoptosis and then focus on how the intersection of these two processes is regulated by cytoplasmic signaling pathways such as the integrated stress response.
Keywords	apoptosis ; cancer therapy ; death ; mitochondria ; stress response
Language	English
Dates of publication	2022-0915
Size	p. 3321-3332.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2022.07.012
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Stressed to death: Mitochondrial stress responses connect respiration and apoptosis in cancer.

Winter, Jacob M / Yadav, Tarun / Rutter, Jared

Molecular cell

2022 Volume 82, Issue 18, Page(s) 3321–3332

Abstract	Mitochondrial energetics and respiration have emerged as important factors in how cancer cells respond to or evade apoptotic signals. The study of the functional connection between these two processes may provide insight into following questions old and new: how might we target respiration or downstream signaling pathways to amplify apoptotic stress in the context of cancer therapy? Why are respiration and apoptotic regulation housed in the same organelle? Here, we briefly review mitochondrial respiration and apoptosis and then focus on how the intersection of these two processes is regulated by cytoplasmic signaling pathways such as the integrated stress response.
MeSH term(s)	Apoptosis ; Humans ; Mitochondria/metabolism ; Neoplasms/genetics ; Neoplasms/metabolism ; Oxidative Stress ; Respiration ; Signal Transduction
Language	English
Publishing date	2022-08-11
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2022.07.012
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Article ; Online: Phosphate starvation signaling increases mitochondrial membrane potential through respiration-independent mechanisms.

eLife

2024 Volume 13

Abstract: Mitochondrial membrane potential directly powers many critical functions of mitochondria, including ATP production, mitochondrial protein import, and metabolite transport. Its loss is a cardinal feature of aging and mitochondrial diseases, and cells ... ...

Abstract	Mitochondrial membrane potential directly powers many critical functions of mitochondria, including ATP production, mitochondrial protein import, and metabolite transport. Its loss is a cardinal feature of aging and mitochondrial diseases, and cells closely monitor membrane potential as an indicator of mitochondrial health. Given its central importance, it is logical that cells would modulate mitochondrial membrane potential in response to demand and environmental cues, but there has been little exploration of this question. We report that loss of the Sit4 protein phosphatase in yeast increases mitochondrial membrane potential, both by inducing the electron transport chain and the phosphate starvation response. Indeed, a similarly elevated mitochondrial membrane potential is also elicited simply by phosphate starvation or by abrogation of the Pho85-dependent phosphate sensing pathway. This enhanced membrane potential is primarily driven by an unexpected activity of the ADP/ATP carrier. We also demonstrate that this connection between phosphate limitation and enhancement of mitochondrial membrane potential is observed in primary and immortalized mammalian cells as well as in
MeSH term(s)	Animals ; Membrane Potential, Mitochondrial ; Phosphates/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Adenosine Triphosphate/metabolism ; Respiration ; Mammals/metabolism
Chemical Substances	Phosphates ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2024-01-22
Publishing country	England
Document type	Journal Article
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.84282
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Article ; Online: Collateral deletion of the mitochondrial AAA+ ATPase ATAD1 sensitizes cancer cells to proteasome dysfunction.

Winter, Jacob M / Fresenius, Heidi L / Cunningham, Corey N / Wei, Peng / Keys, Heather R / Berg, Jordan / Bott, Alex / Yadav, Tarun / Ryan, Jeremy / Sirohi, Deepika / Tripp, Sheryl R / Barta, Paige / Agarwal, Neeraj / Letai, Anthony / Sabatini, David M / Wohlever, Matthew L / Rutter, Jared

eLife

2022 Volume 11

Abstract: The tumor suppressor ... ...

Abstract	The tumor suppressor gene
MeSH term(s)	Humans ; Animals ; Mice ; Proteasome Endopeptidase Complex/metabolism ; ATPases Associated with Diverse Cellular Activities/genetics ; ATPases Associated with Diverse Cellular Activities/metabolism ; PTEN Phosphohydrolase/metabolism ; Mitochondria/metabolism ; Neoplasms/genetics
Chemical Substances	Proteasome Endopeptidase Complex (EC 3.4.25.1) ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-) ; PTEN Phosphohydrolase (EC 3.1.3.67) ; ATAD1 protein, mouse (EC 3.6.1.3)
Language	English
Publishing date	2022-11-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.82860
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Article ; Online: Neuroinflammatory disease disrupts the blood-CNS barrier via crosstalk between proinflammatory and endothelial-to-mesenchymal-transition signaling.

Neuron

2022 Volume 110, Issue 19, Page(s) 3106–3120.e7

Abstract: Breakdown of the blood-central nervous system barrier (BCNSB) is a hallmark of many neuroinflammatory disorders, such as multiple sclerosis (MS). Using a mouse model of MS, experimental autoimmune encephalomyelitis (EAE), we show that endothelial-to- ... ...

Abstract	Breakdown of the blood-central nervous system barrier (BCNSB) is a hallmark of many neuroinflammatory disorders, such as multiple sclerosis (MS). Using a mouse model of MS, experimental autoimmune encephalomyelitis (EAE), we show that endothelial-to-mesenchymal transition (EndoMT) occurs in the CNS before the onset of clinical symptoms and plays a major role in the breakdown of BCNSB function. EndoMT can be induced by an IL-1β-stimulated signaling pathway in which activation of the small GTPase ADP ribosylation factor 6 (ARF6) leads to crosstalk with the activin receptor-like kinase (ALK)-SMAD1/5 pathway. Inhibiting the activation of ARF6 both prevents and reverses EndoMT, stabilizes BCNSB function, reduces demyelination, and attenuates symptoms even after the establishment of severe EAE, without immunocompromising the host. Pan-inhibition of ALKs also reduces disease severity in the EAE model. Therefore, multiple components of the IL-1β-ARF6-ALK-SMAD1/5 pathway could be targeted for the treatment of a variety of neuroinflammatory disorders.
MeSH term(s)	Activin Receptors/metabolism ; Animals ; Central Nervous System/metabolism ; Encephalomyelitis, Autoimmune, Experimental ; Mice ; Mice, Inbred C57BL ; Monomeric GTP-Binding Proteins/metabolism ; Multiple Sclerosis ; Neuroinflammatory Diseases ; Receptor Protein-Tyrosine Kinases/metabolism ; Signal Transduction
Chemical Substances	Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; Activin Receptors (EC 2.7.11.30) ; Monomeric GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2022-08-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	808167-0
ISSN	1097-4199 ; 0896-6273
ISSN (online)	1097-4199
ISSN	0896-6273
DOI	10.1016/j.neuron.2022.07.015
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Zs.A 2496: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Calcium influx through TRPV4 channels modulates the adherens contacts between retinal microvascular endothelial cells.

Phuong, Tam T T / Redmon, Sarah N / Yarishkin, Oleg / Winter, Jacob M / Li, Dean Y / Križaj, David

The Journal of physiology

2017 Volume 595, Issue 22, Page(s) 6869–6885

Abstract: Key points: Endothelial cells employ transient receptor potential isoform 4 (TRPV4) channels to sense ambient mechanical and chemical stimuli. In retinal microvascular endothelial cells, TRPV4 channels regulate calcium homeostasis, cytoskeletal ... ...

Abstract	Key points: Endothelial cells employ transient receptor potential isoform 4 (TRPV4) channels to sense ambient mechanical and chemical stimuli. In retinal microvascular endothelial cells, TRPV4 channels regulate calcium homeostasis, cytoskeletal signalling and the organization of adherens junctional contacts. Intracellular calcium increases induced by TRPV4 agonists include a significant contribution from calcium release from internal stores. Activation of TRPV4 channels regulates retinal endothelial barriers in vitro and in vivo. TRPV4 sensing may provide a feedback mechanism between sensing shear flow and eicosanoid modulators, vascular permeability and contractility at the inner retinal endothelial barrier. Abstract: The identity of microvascular endothelial (MVE) mechanosensors that sense blood flow in response to mechanical and chemical stimuli and regulate vascular permeability in the retina is unknown. Using immunohistochemistry, calcium imaging, electrophysiology, impedance measurements and vascular permeability assays, we show that the transient receptor potential isoform 4 (TRPV4) plays a major role in Ca
MeSH term(s)	Action Potentials ; Adherens Junctions/metabolism ; Animals ; Blood-Retinal Barrier/metabolism ; Calcium/metabolism ; Calcium Signaling ; Cells, Cultured ; Endothelial Cells/cytology ; Endothelial Cells/metabolism ; Feedback, Physiological ; Humans ; Leucine/analogs & derivatives ; Mice ; Mice, Inbred C57BL ; Morpholines/pharmacology ; Occludin/genetics ; Occludin/metabolism ; Pyrroles/pharmacology ; Retinal Vessels/cytology ; Retinal Vessels/metabolism ; Sulfonamides ; TRPV Cation Channels/agonists ; TRPV Cation Channels/antagonists & inhibitors ; TRPV Cation Channels/metabolism
Chemical Substances	HC-067047 ; Morpholines ; N-(1-((4-(2-(((2,4-dichlorophenyl)sulfonyl)amino)-3-hydroxypropanoyl)-1-piperazinyl)carbonyl)-3-methylbutyl)-1-benzothiophene-2-carboxamide ; Occludin ; Pyrroles ; Sulfonamides ; TRPV Cation Channels ; TRPV4 protein, human ; Leucine (GMW67QNF9C) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2017-10-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	3115-x
ISSN	1469-7793 ; 0022-3751
ISSN (online)	1469-7793
ISSN	0022-3751
DOI	10.1113/JP275052
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Article ; Online: Long-term effects of cryopreservation on clinically prepared hematopoietic progenitor cell products.

Winter, Jacob M / Jacobson, Pam / Bullough, Brandon / Christensen, Austin P / Boyer, Michael / Reems, Jo-Anna

Cytotherapy

2014 Volume 16, Issue 7, Page(s) 965–975

Abstract: Background aims: The question of how long hematopoietic progenitor cells (HPCs) destined for clinical applications withstand long-term cryopreservation remains unanswered. To increase our basic understanding about the stability of HPC products over time, ...

Abstract	Background aims: The question of how long hematopoietic progenitor cells (HPCs) destined for clinical applications withstand long-term cryopreservation remains unanswered. To increase our basic understanding about the stability of HPC products over time, this study focused on characterizing long-term effects of cryopreservation on clinically prepared HPC products. Methods: Cryovials (n = 233) frozen for an average of 6.3 ± 14.2 years (range, 0.003-14.6 years) from HPC products (n = 170) representing 75 individual patients were thawed and evaluated for total nucleated cells (TNCs), cell viability, viable CD34+ (vCD34+) cells and colony-forming cells (CFCs). TNCs were determined by use of an automated cell counter, and cell viability was measured with the use of trypan blue exclusion. Viable CD34 analysis was performed by means of flow cytometry and function by a CFC assay. Results: Significant losses in TNCs, cell viability, vCD34+ cells and CFC occurred on cryopreservation. However, once frozen, viable TNCs, vCD34+ cells and CFC recoveries did not significantly change over time. The only parameter demonstrating a change over time was cell viability, which decreased as the length of time that an HPC product was stored frozen increased. A significant negative correlation (correlation coefficient = -0.165) was determined between pre-freeze percent granulocyte content and post-thaw percent viability (n = 170; P = 0.032). However, a significant positive correlation was observed between percent viability at thaw and pre-freeze lymphocyte concentration. Conclusions: Once frozen, HPC products were stable for up to 14.6 years at <-150°C. Post-thaw viability was found to correlate negatively with pre-freeze granulocyte content and positively with pre-freeze lymphocyte content.
MeSH term(s)	Blood Preservation/methods ; Cell Survival/drug effects ; Cell Survival/genetics ; Cryopreservation/methods ; Flow Cytometry ; Freezing ; Hematopoietic Stem Cell Transplantation/methods ; Hematopoietic Stem Cells/cytology ; Hematopoietic Stem Cells/metabolism ; Humans ; Stem Cells
Language	English
Publishing date	2014-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2039821-9
ISSN	1477-2566 ; 1465-3249
ISSN (online)	1477-2566
ISSN	1465-3249
DOI	10.1016/j.jcyt.2014.02.005
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Article ; Online: The biochemical basis of mitochondrial dysfunction in Zellweger Spectrum Disorder.

Nuebel, Esther / Morgan, Jeffrey T / Fogarty, Sarah / Winter, Jacob M / Lettlova, Sandra / Berg, Jordan A / Chen, Yu-Chan / Kidwell, Chelsea U / Maschek, J Alan / Clowers, Katie J / Argyriou, Catherine / Chen, Lingxiao / Wittig, Ilka / Cox, James E / Roh-Johnson, Minna / Braverman, Nancy / Bonkowsky, Joshua / Gygi, Steven P / Rutter, Jared

EMBO reports

2021 Volume 22, Issue 10, Page(s) e51991

Abstract: Peroxisomal biogenesis disorders (PBDs) are genetic disorders of peroxisome biogenesis and metabolism that are characterized by profound developmental and neurological phenotypes. The most severe class of PBDs-Zellweger spectrum disorder (ZSD)-is caused ... ...

Abstract	Peroxisomal biogenesis disorders (PBDs) are genetic disorders of peroxisome biogenesis and metabolism that are characterized by profound developmental and neurological phenotypes. The most severe class of PBDs-Zellweger spectrum disorder (ZSD)-is caused by mutations in peroxin genes that result in both non-functional peroxisomes and mitochondrial dysfunction. It is unclear, however, how defective peroxisomes contribute to mitochondrial impairment. In order to understand the molecular basis of this inter-organellar relationship, we investigated the fate of peroxisomal mRNAs and proteins in ZSD model systems. We found that peroxins were still expressed and a subset of them accumulated on the mitochondrial membrane, which resulted in gross mitochondrial abnormalities and impaired mitochondrial metabolic function. We showed that overexpression of ATAD1, a mitochondrial quality control factor, was sufficient to rescue several aspects of mitochondrial function in human ZSD fibroblasts. Together, these data suggest that aberrant peroxisomal protein localization is necessary and sufficient for the devastating mitochondrial morphological and metabolic phenotypes in ZSDs.
MeSH term(s)	Humans ; Mitochondria/genetics ; Peroxins/metabolism ; Peroxisomal Disorders/genetics ; Peroxisomal Disorders/metabolism ; Peroxisomes/metabolism ; Zellweger Syndrome/genetics ; Zellweger Syndrome/metabolism
Chemical Substances	Peroxins
Language	English
Publishing date	2021-08-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.202051991
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Zs.A 5433: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Protein-metabolite interactomics of carbohydrate metabolism reveal regulation of lactate dehydrogenase.

Hicks, Kevin G / Cluntun, Ahmad A / Schubert, Heidi L / Hackett, Sean R / Berg, Jordan A / Leonard, Paul G / Ajalla Aleixo, Mariana A / Zhou, Youjia / Bott, Alex J / Salvatore, Sonia R / Chang, Fei / Blevins, Aubrie / Barta, Paige / Tilley, Samantha / Leifer, Aaron / Guzman, Andrea / Arok, Ajak / Fogarty, Sarah / Winter, Jacob M /

Ahn, Hee-Chul / Allen, Karen N / Block, Samuel / Cardoso, Iara A / Ding, Jianping / Dreveny, Ingrid / Gasper, William C / Ho, Quinn / Matsuura, Atsushi / Palladino, Michael J / Prajapati, Sabin / Sun, Pengkai / Tittmann, Kai / Tolan, Dean R / Unterlass, Judith / VanDemark, Andrew P / Vander Heiden, Matthew G / Webb, Bradley A / Yun, Cai-Hong / Zhao, Pengkai / Wang, Bei / Schopfer, Francisco J / Hill, Christopher P / Nonato, Maria Cristina / Muller, Florian L / Cox, James E / Rutter, Jared

Science (New York, N.Y.)

2023 Volume 379, Issue 6636, Page(s) 996–1003

Abstract: Metabolic networks are interconnected and influence diverse cellular processes. The protein-metabolite interactions that mediate these networks are frequently low affinity and challenging to systematically discover. We developed mass spectrometry ... ...

Abstract	Metabolic networks are interconnected and influence diverse cellular processes. The protein-metabolite interactions that mediate these networks are frequently low affinity and challenging to systematically discover. We developed mass spectrometry integrated with equilibrium dialysis for the discovery of allostery systematically (MIDAS) to identify such interactions. Analysis of 33 enzymes from human carbohydrate metabolism identified 830 protein-metabolite interactions, including known regulators, substrates, and products as well as previously unreported interactions. We functionally validated a subset of interactions, including the isoform-specific inhibition of lactate dehydrogenase by long-chain acyl-coenzyme A. Cell treatment with fatty acids caused a loss of pyruvate-lactate interconversion dependent on lactate dehydrogenase isoform expression. These protein-metabolite interactions may contribute to the dynamic, tissue-specific metabolic flexibility that enables growth and survival in an ever-changing nutrient environment.
MeSH term(s)	Humans ; Carbohydrate Metabolism ; Fatty Acids/metabolism ; L-Lactate Dehydrogenase/metabolism ; Organ Specificity ; Metabolome ; Mass Spectrometry/methods ; Allosteric Regulation
Chemical Substances	Fatty Acids ; L-Lactate Dehydrogenase (EC 1.1.1.27)
Language	English
Publishing date	2023-03-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.abm3452
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Article ; Online: The small GTPase ARF6 regulates protein trafficking to control cellular function during development and in disease.

Grossmann, Allie H / Zhao, Helong / Jenkins, Noah / Zhu, Weiquan / Richards, Jackson R / Yoo, Jae Hyuk / Winter, Jacob M / Rich, Bianca / Mleynek, Tara M / Li, Dean Y / Odelberg, Shannon J

Small GTPases

2016 Volume 10, Issue 1, Page(s) 1–12

Abstract: The activation of the small GTPase ARF6 has been implicated in promoting several pathological processes related to vascular instability and tumor formation, growth, and metastasis. ARF6 also plays a vital role during embryonic development. Recent studies ...

Abstract	The activation of the small GTPase ARF6 has been implicated in promoting several pathological processes related to vascular instability and tumor formation, growth, and metastasis. ARF6 also plays a vital role during embryonic development. Recent studies have suggested that ARF6 carries out these disparate functions primarily by controlling protein trafficking within the cell. ARF6 helps direct proteins to intracellular or extracellular locations where they function in normal cellular responses during development and in pathological processes later in life. This transport of proteins is accomplished through a variety of mechanisms, including endocytosis and recycling, microvesicle release, and as yet uncharacterized processes. This Commentary will explore the functions of ARF6, while focusing on the role of this small GTPase in development and postnatal physiology, regulating barrier function and diseases associated with its loss, and tumor formation, growth, and metastasis.
MeSH term(s)	ADP-Ribosylation Factors/physiology ; Animals ; Embryonic Development ; Endothelium, Vascular/physiology ; Humans ; Neoplasms/enzymology ; Neoplasms/pathology ; Protein Transport
Chemical Substances	ADP-Ribosylation Factors (EC 3.6.5.2) ; ADP-ribosylation factor 6 (EC 3.6.5.2)
Language	English
Publishing date	2016-12-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2682247-7
ISSN	2154-1256 ; 2154-1248
ISSN (online)	2154-1256
ISSN	2154-1248
DOI	10.1080/21541248.2016.1259710
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