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Article ; Online: TMEM106B Puncta Is Increased in Multiple Sclerosis Plaques, and Reduced Protein in Mice Results in Delayed Lipid Clearance Following CNS Injury.

Shafit-Zagardo, Bridget / Sidoli, Simone / Goldman, James E / DuBois, Juwen C / Corboy, John R / Strittmatter, Stephen M / Guzik, Hillary / Edema, Ukuemi / Arackal, Anita G / Botbol, Yair M / Merheb, Emilio / Nagra, Rashed M / Graff, Sarah

Cells

2023 Volume 12, Issue 13

Abstract: During inflammatory, demyelinating diseases such as multiple sclerosis (MS), inflammation and axonal damage are prevalent early in the course. Axonal damage includes swelling, defects in transport, and failure to clear damaged intracellular proteins, all ...

Abstract	During inflammatory, demyelinating diseases such as multiple sclerosis (MS), inflammation and axonal damage are prevalent early in the course. Axonal damage includes swelling, defects in transport, and failure to clear damaged intracellular proteins, all of which affect recovery and compromise neuronal integrity. The clearance of damaged cell components is important to maintain normal turnover and restore homeostasis. In this study, we used mass spectrometry to identify insoluble proteins within high-speed/mercaptoethanol/sarcosyl-insoluble pellets from purified white matter plaques isolated from the brains of individuals with relapsing-remitting MS (RRMS). We determined that the transmembrane protein 106B (TMEM106B), normally lysosome-associated, is insoluble in RRMS plaques relative to normal-appearing white matter from individuals with Alzheimer's disease and non-neurologic controls. Relative to wild-type mice, hypomorphic mice with a reduction in TMEM106B have increased axonal damage and lipid droplet accumulation in the spinal cord following myelin-oligodendrocyte-glycoprotein-induced experimental autoimmune encephalomyelitis. Additionally, the corpora callosa from cuprizone-challenged hypomorphic mice fail to clear lipid droplets efficiently during remyelination, suggesting that when TMEM106B is compromised, protein and lipid clearance by the lysosome is delayed. As TMEM106B contains putative lipid- and LC3-binding sites, further exploration of these sites is warranted.
MeSH term(s)	Mice ; Animals ; Multiple Sclerosis ; Encephalomyelitis, Autoimmune, Experimental ; Spinal Cord/metabolism ; Myelin-Oligodendrocyte Glycoprotein/metabolism ; Lipids/adverse effects
Chemical Substances	Myelin-Oligodendrocyte Glycoprotein ; Lipids
Language	English
Publishing date	2023-06-27
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells12131734
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Article ; Online: Assays for Monitoring Macroautophagy Activity in T cells.

Botbol, Yair / Macian, Fernando

Methods in molecular biology (Clifton, N.J.)

2015 Volume 1343, Page(s) 143–153

Abstract: Autophagy is an essential catabolic process that regulates a diverse array of functions by targeting cellular components for degradation by lysosomes. Studies in mammalian cells have shown that the regulation of autophagy is highly complex and ... ...

Abstract	Autophagy is an essential catabolic process that regulates a diverse array of functions by targeting cellular components for degradation by lysosomes. Studies in mammalian cells have shown that the regulation of autophagy is highly complex and optimization of experimental approaches to analyze this process needs to be developed for each model studied. This chapter provides an overview of two of the most commonly used ways to monitor autophagy activity in T cell. It involves description of common techniques, namely Western blot and cell immunostaining, giving specific recommendations for working with T cells and monitoring macroautophagy. We also discuss the analysis required for correct interpretation of the results and quantification of macroautophagy activity.
MeSH term(s)	Animals ; Autophagy/physiology ; Cell Separation/methods ; Fluorescent Antibody Technique ; Lymphocyte Activation/immunology ; Mice ; Microtubule-Associated Proteins/metabolism ; T-Lymphocyte Subsets/metabolism ; T-Lymphocytes/metabolism
Chemical Substances	Map1lc3b protein, mouse ; Microtubule-Associated Proteins
Language	English
Publishing date	2015-09-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-2963-4_12
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Article ; Online: Key roles of autophagy in regulating T-cell function.

Botbol, Yair / Guerrero-Ros, Ignacio / Macian, Fernando

European journal of immunology

2016 Volume 46, Issue 6, Page(s) 1326–1334

Abstract: In the past 10 years, autophagy has emerged as a crucial regulator of T-cell homeostasis, activation, and differentiation. Through the ability to adjust the cell's proteome in response to different stimuli, different forms of autophagy have been shown to ...

Abstract	In the past 10 years, autophagy has emerged as a crucial regulator of T-cell homeostasis, activation, and differentiation. Through the ability to adjust the cell's proteome in response to different stimuli, different forms of autophagy have been shown to control T-cell homeostasis and survival. Autophagic processes can also determine the magnitude of the T-cell response to TCR engagement, by regulating the cellular levels of specific signaling intermediates and modulating the metabolic output in activated T cells. In this review we will examine the mechanisms that control autophagy activity in T cells, such as ROS signaling and signaling through common gamma-chain cytokine receptors, and the different aspect of T-cell biology, including T-cell survival, effector cell function, and generation of memory, which can be regulated by autophagy.
MeSH term(s)	Animals ; Autoimmune Diseases/genetics ; Autoimmune Diseases/immunology ; Autoimmune Diseases/metabolism ; Autoimmunity ; Autophagy/genetics ; Autophagy/immunology ; Cell Survival/genetics ; Cell Survival/immunology ; Energy Metabolism ; Homeostasis ; Host-Pathogen Interactions/genetics ; Host-Pathogen Interactions/immunology ; Humans ; Immunologic Memory ; Immunosenescence ; Lymphocyte Activation/genetics ; Lymphocyte Activation/immunology ; Molecular Chaperones/metabolism ; Organelles/immunology ; Organelles/metabolism ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; T-Lymphocytes/immunology ; T-Lymphocytes/metabolism
Chemical Substances	Molecular Chaperones ; Receptors, Antigen, T-Cell
Language	English
Publishing date	2016-06
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	120108-6
ISSN	1521-4141 ; 0014-2980
ISSN (online)	1521-4141
ISSN	0014-2980
DOI	10.1002/eji.201545955
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Article ; Online: TMEM106B Puncta Is Increased in Multiple Sclerosis Plaques, and Reduced Protein in Mice Results in Delayed Lipid Clearance Following CNS Injury

Bridget Shafit-Zagardo / Simone Sidoli / James E. Goldman / Juwen C. DuBois / John R. Corboy / Stephen M. Strittmatter / Hillary Guzik / Ukuemi Edema / Anita G. Arackal / Yair M. Botbol / Emilio Merheb / Rashed M. Nagra / Sarah Graff

Cells, Vol 12, Iss 1734, p

2023 Volume 1734

Abstract	During inflammatory, demyelinating diseases such as multiple sclerosis (MS), inflammation and axonal damage are prevalent early in the course. Axonal damage includes swelling, defects in transport, and failure to clear damaged intracellular proteins, all of which affect recovery and compromise neuronal integrity. The clearance of damaged cell components is important to maintain normal turnover and restore homeostasis. In this study, we used mass spectrometry to identify insoluble proteins within high-speed/mercaptoethanol/sarcosyl-insoluble pellets from purified white matter plaques isolated from the brains of individuals with relapsing–remitting MS (RRMS). We determined that the transmembrane protein 106B (TMEM106B), normally lysosome-associated, is insoluble in RRMS plaques relative to normal-appearing white matter from individuals with Alzheimer’s disease and non-neurologic controls. Relative to wild-type mice, hypomorphic mice with a reduction in TMEM106B have increased axonal damage and lipid droplet accumulation in the spinal cord following myelin-oligodendrocyte-glycoprotein-induced experimental autoimmune encephalomyelitis. Additionally, the corpora callosa from cuprizone-challenged hypomorphic mice fail to clear lipid droplets efficiently during remyelination, suggesting that when TMEM106B is compromised, protein and lipid clearance by the lysosome is delayed. As TMEM106B contains putative lipid- and LC3-binding sites, further exploration of these sites is warranted.
Keywords	multiple sclerosis (MS) ; TMEM106B ; myelin oligodendrocyte glycoprotein (MOG)-induced EAE ; demyelination ; lipids ; Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2023-06-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Common γ-chain cytokine signaling is required for macroautophagy induction during CD4+ T-cell activation.

Botbol, Yair / Patel, Bindi / Macian, Fernando

Autophagy

2015 Volume 11, Issue 10, Page(s) 1864–1877

Abstract: Macroautophagy is a cellular process that mediates degradation in the lysosome of cytoplasmic components including proteins and organelles. Previous studies have shown that macroautophagy is induced in activated T cells to regulate organelle homeostasis ... ...

Abstract	Macroautophagy is a cellular process that mediates degradation in the lysosome of cytoplasmic components including proteins and organelles. Previous studies have shown that macroautophagy is induced in activated T cells to regulate organelle homeostasis and the cell's energy metabolism. However, the signaling pathways that initiate and regulate activation-induced macroautophagy in T cells have not been identified. Here, we show that activation-induced macroautophagy in T cells depends on signaling from common γ-chain cytokines. Consequently, inhibition of signaling through JAK3, induced downstream of cytokine receptors containing the common γ-chain, prevents full induction of macroautophagy in activated T cells. Moreover, we found that common γ-chain cytokines are not only required for macroautophagy upregulation during T cell activation but can themselves induce macroautophagy. Our data also show that macroautophagy induction in T cells is associated with an increase of LC3 expression that is mediated by a post-transcriptional mechanism. Overall, our findings unveiled a new role for common γ-chain cytokines as a molecular link between autophagy induction and T-cell activation.
MeSH term(s)	Animals ; Autophagy/immunology ; CD4-Positive T-Lymphocytes/immunology ; Cell Communication/immunology ; Cytokines/metabolism ; Female ; Lymphocyte Activation/immunology ; Mice, Inbred C57BL ; Phosphorylation ; Signal Transduction
Chemical Substances	Cytokines
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2015.1089374
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Article ; Online: Autophagy Is a Tolerance-Avoidance Mechanism that Modulates TCR-Mediated Signaling and Cell Metabolism to Prevent Induction of T Cell Anergy.

Mocholi, Enric / Dowling, Samuel D / Botbol, Yair / Gruber, Ross C / Ray, Alex K / Vastert, Sebastiaan / Shafit-Zagardo, Bridget / Coffer, Paul J / Macian, Fernando

Cell reports

2018 Volume 24, Issue 5, Page(s) 1136–1150

Abstract: In response to activation, ... ...

Abstract	In response to activation, CD4
MeSH term(s)	Animals ; Autophagy ; CD4-Positive T-Lymphocytes/immunology ; Cells, Cultured ; Clonal Anergy ; Encephalomyelitis, Autoimmune, Experimental/immunology ; Female ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Mitochondria/metabolism ; Protein Tyrosine Phosphatase, Non-Receptor Type 1/metabolism ; Receptors, Antigen, T-Cell/metabolism
Chemical Substances	Receptors, Antigen, T-Cell ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 (EC 3.1.3.48) ; Ptpn1 protein, mouse (EC 3.1.3.48)
Language	English
Publishing date	2018-11-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2018.06.065
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Article ; Online: Autophagy and disease: always two sides to a problem.

Sridhar, Sunandini / Botbol, Yair / Macian, Fernando / Cuervo, Ana Maria

The Journal of pathology

2011 Volume 226, Issue 2, Page(s) 255–273

Abstract: Autophagy is a process traditionally known to contribute to cellular cleaning through the removal of intracellular components in lysosomes. In recent years, intensive scrutiny at the molecular level to which autophagy has been subjected has also ... ...

Abstract	Autophagy is a process traditionally known to contribute to cellular cleaning through the removal of intracellular components in lysosomes. In recent years, intensive scrutiny at the molecular level to which autophagy has been subjected has also contributed to expanding our understanding of the physiological role of this pathway. Added to the well-characterized role in quality control, autophagy has proved to be important in the maintenance of cellular homeostasis and of the energetic balance, in cellular and tissue remodelling, and cellular defence against extracellular insults and pathogens. It is not a surprise that, in light of this growing number of physiological functions, connections between autophagic malfunction and human pathologies have also been strengthened. In this review, we focus on several pathological conditions associated with primary or secondary defects in autophagy and comment on a recurring theme for many of them, ie the fact that autophagy can often exert both beneficial and aggravating effects on the progression of disease. Elucidating the factors that determine the switch between these dual functions of autophagy in disease has become a priority when considering the potential therapeutic implications of the pharmacological modulation of autophagy in many of these pathological conditions.
MeSH term(s)	Autoimmune Diseases/pathology ; Autophagy/physiology ; Cell Differentiation ; Cell Survival ; Disease Progression ; Energy Metabolism ; Heart Failure/pathology ; Humans ; Infections/pathology ; Lysosomes/physiology ; Molecular Chaperones/physiology ; Neoplasms/pathology ; Neurodegenerative Diseases/pathology
Chemical Substances	Molecular Chaperones
Language	English
Publishing date	2011-11-23
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	3119-7
ISSN	1096-9896 ; 0022-3417
ISSN (online)	1096-9896
ISSN	0022-3417
DOI	10.1002/path.3025
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Article ; Online: Chaperone-mediated autophagy regulates T cell responses through targeted degradation of negative regulators of T cell activation.

Valdor, Rut / Mocholi, Enric / Botbol, Yair / Guerrero-Ros, Ignacio / Chandra, Dinesh / Koga, Hiroshi / Gravekamp, Claudia / Cuervo, Ana Maria / Macian, Fernando

Nature immunology

2014 Volume 15, Issue 11, Page(s) 1046–1054

Abstract: Chaperone-mediated autophagy (CMA) targets soluble proteins for lysosomal degradation. Here we found that CMA was activated in T cells in response to engagement of the T cell antigen receptor (TCR), which induced expression of the CMA-related lysosomal ... ...

Abstract	Chaperone-mediated autophagy (CMA) targets soluble proteins for lysosomal degradation. Here we found that CMA was activated in T cells in response to engagement of the T cell antigen receptor (TCR), which induced expression of the CMA-related lysosomal receptor LAMP-2A. In activated T cells, CMA targeted the ubiquitin ligase Itch and the calcineurin inhibitor RCAN1 for degradation to maintain activation-induced responses. Consequently, deletion of the gene encoding LAMP-2A in T cells caused deficient in vivo responses to immunization or infection with Listeria monocytogenes. Impaired CMA activity also occurred in T cells with age, which negatively affected their function. Restoration of LAMP-2A in T cells from old mice resulted in enhancement of activation-induced responses. Our findings define a role for CMA in regulating T cell activation through the targeted degradation of negative regulators of T cell activation.
MeSH term(s)	Aging/immunology ; Animals ; Autophagy/immunology ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/biosynthesis ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/genetics ; Calcineurin Inhibitors/metabolism ; Calcium-Binding Proteins ; Cells, Cultured ; Dual Oxidases ; Female ; Humans ; Immunization ; Intracellular Signaling Peptides and Proteins/metabolism ; Listeria monocytogenes/immunology ; Listeriosis/immunology ; Lymphocyte Activation/immunology ; Lysosomal-Associated Membrane Protein 2/biosynthesis ; Lysosomal-Associated Membrane Protein 2/genetics ; Lysosomal-Associated Membrane Protein 2/immunology ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Molecular Chaperones/immunology ; Muscle Proteins/metabolism ; NADPH Oxidases/genetics ; Oxidative Stress/immunology ; RNA Interference ; RNA, Messenger/biosynthesis ; RNA, Small Interfering ; Reactive Oxygen Species/metabolism ; Receptors, Antigen, T-Cell/immunology ; Th1 Cells/immunology ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Calcineurin Inhibitors ; Calcium-Binding Proteins ; DSCR1 protein, mouse ; Intracellular Signaling Peptides and Proteins ; Lysosomal-Associated Membrane Protein 2 ; Molecular Chaperones ; Muscle Proteins ; RNA, Messenger ; RNA, Small Interfering ; Reactive Oxygen Species ; Receptors, Antigen, T-Cell ; Tcfeb protein, mouse ; Dual Oxidases (EC 1.11.1.-) ; NADPH Oxidases (EC 1.6.3.-) ; Duox1 protein, mouse (EC 1.6.3.1) ; Itch protein, mouse (EC 2.3.2.26) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2014-09-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2016987-5
ISSN	1529-2916 ; 1529-2908
ISSN (online)	1529-2916
ISSN	1529-2908
DOI	10.1038/ni.3003
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Zs.A 5294: 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: H1 histones control the epigenetic landscape by local chromatin compaction.

Willcockson, Michael A / Healton, Sean E / Weiss, Cary N / Bartholdy, Boris A / Botbol, Yair / Mishra, Laxmi N / Sidhwani, Dhruv S / Wilson, Tommy J / Pinto, Hugo B / Maron, Maxim I / Skalina, Karin A / Toro, Laura Norwood / Zhao, Jie / Lee, Chul-Hwan / Hou, Harry / Yusufova, Nevin / Meydan, Cem / Osunsade, Adewola / David, Yael /

Cesarman, Ethel / Melnick, Ari M / Sidoli, Simone / Garcia, Benjamin A / Edelmann, Winfried / Macian, Fernando / Skoultchi, Arthur I

Nature

2020 Volume 589, Issue 7841, Page(s) 293–298

Abstract: H1 linker histones are the most abundant chromatin-binding ... ...

Abstract	H1 linker histones are the most abundant chromatin-binding proteins
MeSH term(s)	Animals ; CD8-Positive T-Lymphocytes/metabolism ; Cell Differentiation/genetics ; Chromatin/chemistry ; Chromatin/genetics ; Chromatin/metabolism ; Chromatin Assembly and Disassembly ; Enhancer of Zeste Homolog 2 Protein/metabolism ; Epigenesis, Genetic ; Female ; Gene Silencing ; Histones/chemistry ; Histones/metabolism ; Lymphocyte Activation/genetics ; Male ; Methylation ; Mice ; Mice, Knockout
Chemical Substances	Chromatin ; Histones ; Enhancer of Zeste Homolog 2 Protein (EC 2.1.1.43) ; Ezh2 protein, mouse (EC 2.1.1.43)
Language	English
Publishing date	2020-12-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-020-3032-z
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Article ; Online: A PDGFRα-Mediated Switch toward CD9

Marcelin, Geneviève / Ferreira, Adaliene / Liu, Yuejun / Atlan, Michael / Aron-Wisnewsky, Judith / Pelloux, Véronique / Botbol, Yair / Ambrosini, Marc / Fradet, Magali / Rouault, Christine / Hénégar, Corneliu / Hulot, Jean-Sébastien / Poitou, Christine / Torcivia, Adriana / Nail-Barthelemy, Raphael / Bichet, Jean-Christophe / Gautier, Emmanuel L / Clément, Karine

Cell metabolism

2017 Volume 25, Issue 3, Page(s) 673–685

Abstract: Obesity-induced white adipose tissue (WAT) fibrosis is believed to accelerate WAT dysfunction. However, the cellular origin of WAT fibrosis remains unclear. Here, we show that adipocyte platelet-derived growth factor receptor-α-positive ( ... ...

Abstract	Obesity-induced white adipose tissue (WAT) fibrosis is believed to accelerate WAT dysfunction. However, the cellular origin of WAT fibrosis remains unclear. Here, we show that adipocyte platelet-derived growth factor receptor-α-positive (PDGFRα
MeSH term(s)	Adipocytes/pathology ; Adipogenesis ; Adipose Tissue/pathology ; Adipose Tissue, White/metabolism ; Adipose Tissue, White/pathology ; Adult ; Animals ; Body Weight ; Epididymis/metabolism ; Fibrosis ; Homeostasis ; Humans ; Insulin Resistance ; Male ; Mice, Inbred C57BL ; Obesity/metabolism ; Obesity/pathology ; Obesity/physiopathology ; Platelet-Derived Growth Factor/metabolism ; Receptor, Platelet-Derived Growth Factor alpha/metabolism ; Signal Transduction ; Stem Cells/metabolism ; Tetraspanin-29/metabolism
Chemical Substances	Platelet-Derived Growth Factor ; Tetraspanin-29 ; Receptor, Platelet-Derived Growth Factor alpha (EC 2.7.10.1)
Language	English
Publishing date	2017-02-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2176834-1
ISSN	1932-7420 ; 1550-4131
ISSN (online)	1932-7420
ISSN	1550-4131
DOI	10.1016/j.cmet.2017.01.010
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