Interferon‐γ stimulates p11‐dependent surface expression of annexin A2 in lung epithelial cells to enhance phagocytosis
Identifieur interne : 001409 ( Main/Merge ); précédent : 001408; suivant : 001410Interferon‐γ stimulates p11‐dependent surface expression of annexin A2 in lung epithelial cells to enhance phagocytosis
Auteurs : Yi-Ting Fang [Taïwan] ; Chiou-Feng Lin [Taïwan] ; Chi-Yun Wang [Taïwan] ; Robert Anderson [Canada] ; Yee-Shin Lin [Taïwan]Source :
- Journal of Cellular Physiology [ 0021-9541 ] ; 2012-06.
English descriptors
- Teeft :
- Alexa, Annexin, Apoptotic, Apoptotic cells, Apoptotic eosinophils, Biol, Calnexin, Cell surface, Cellular physiology, Cheng, Confocal, Confocal microscopy, Culture medium, Cytometry, Dapi, Different time periods, Egta, Eluate, Endothelial, Endothelial cells, Epithelial, Epithelial cells, Exosomal, Exosomal fraction, Exosome, Exosomes, Extracellular, Fang, Hajjar, Immunol, Intracellular, Jak2, Lung epithelial cells, Mediates, National cheng kung university, Paraformaldehyde, Pathway, Permeabilized, Phagocytosis, Phosphorylation, Plasma membrane, Pretreated, Primary antibodies, Protein expression, Receptor, Room temperature, Saponin, Supernatant, Surface annexin, Surface expression, Surface translocation, Total cell lysates, Transfected, Translocation, Upregulation.
Abstract
Annexin A2 (p36) is usually present together with its natural ligand p11 as a heterotetramer complex, which has multiple biological functions depending on its cellular localization. However, the detailed mechanism of annexin A2 translocation and its physiological role in inflammation remain unclear. Here, we show that IFN‐γ stimulation enhances surface translocation of annexin A2 on lung epithelial cells. While total annexin A2 protein remains unchanged, the expression of p11 is upregulated via the IFN‐γ‐activated JAK2/STAT1 signal pathway. Notably, IFN‐γ‐induced p11 expression is required for annexin A2 translocation to the cell surface. Since annexin A2 lacks a signal peptide for surface translocation by the classical endoplasmic reticulum‐Golgi route, its mode of trafficking remains unclear. We observed that p11‐dependent surface translocation of annexin A2 is associated with the exosomal secretion pathway. The IFN‐γ‐induced increase of annexin A2 in the exosomes is blocked in p11‐silenced cells. Furthermore, IFN‐γ‐induced surface expression of annexin A2 mediates phagocytosis of apoptotic cells by lung epithelial cells. These findings provide insights into the surface translocation mechanism of annexin A2 and illustrate a pivotal function of surface annexin A2 in the phagocytic response to IFN‐γ. J. Cell. Physiol. 227: 2775–2787, 2012. © 2011 Wiley Periodicals, Inc.
Url:
DOI: 10.1002/jcp.23026
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first="Yi-Ting" last="Fang">Yi-Ting Fang</name><affiliation wicri:level="1"><country xml:lang="fr">Taïwan</country><wicri:regionArea>Institute of Basic Medical Sciences, National Cheng Kung University Medical College, Tainan</wicri:regionArea><wicri:noRegion>Tainan</wicri:noRegion></affiliation></author><author><name sortKey="Lin, Chiou Eng" sort="Lin, Chiou Eng" uniqKey="Lin C" first="Chiou-Feng" last="Lin">Chiou-Feng Lin</name><affiliation wicri:level="1"><country xml:lang="fr">Taïwan</country><wicri:regionArea>Institute of Basic Medical Sciences, National Cheng Kung University Medical College, Tainan</wicri:regionArea><wicri:noRegion>Tainan</wicri:noRegion></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Taïwan</country><wicri:regionArea>Institute of Clinical Medicine, National Cheng Kung University Medical College, Tainan</wicri:regionArea><wicri:noRegion>Tainan</wicri:noRegion></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Taïwan</country><wicri:regionArea>Department of Microbiology and Immunology, National Cheng Kung University Medical College, Tainan</wicri:regionArea><wicri:noRegion>Tainan</wicri:noRegion></affiliation></author><author><name sortKey="Wang, Chi Un" sort="Wang, Chi Un" uniqKey="Wang C" first="Chi-Yun" last="Wang">Chi-Yun Wang</name><affiliation wicri:level="1"><country xml:lang="fr">Taïwan</country><wicri:regionArea>Institute of Basic Medical Sciences, National Cheng Kung University Medical College, Tainan</wicri:regionArea><wicri:noRegion>Tainan</wicri:noRegion></affiliation></author><author><name sortKey="Anderson, Robert" sort="Anderson, Robert" uniqKey="Anderson R" first="Robert" last="Anderson">Robert Anderson</name><affiliation wicri:level="1"><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia</wicri:regionArea><wicri:noRegion>Nova Scotia</wicri:noRegion></affiliation></author><author><name sortKey="Lin, Yee Hin" sort="Lin, Yee Hin" uniqKey="Lin Y" first="Yee-Shin" last="Lin">Yee-Shin Lin</name><affiliation wicri:level="1"><country xml:lang="fr">Taïwan</country><wicri:regionArea>Institute of Basic Medical Sciences, National Cheng Kung University Medical College, Tainan</wicri:regionArea><wicri:noRegion>Tainan</wicri:noRegion></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Taïwan</country><wicri:regionArea>Department of Microbiology and Immunology, National Cheng Kung University Medical College, Tainan</wicri:regionArea><wicri:noRegion>Tainan</wicri:noRegion></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Taïwan</country><wicri:regionArea>Center of Infectious Disease and Signaling Research, National Cheng Kung University, Tainan</wicri:regionArea><wicri:noRegion>Tainan</wicri:noRegion></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Taïwan</country></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Taïwan</country><wicri:regionArea>Correspondence address: Department of Microbiology and Immunology, National Cheng Kung University Medical College, 1 University Road, Tainan 701</wicri:regionArea><wicri:noRegion>Tainan 701</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of Cellular Physiology</title><title level="j" type="alt">JOURNAL OF CELLULAR PHYSIOLOGY</title><idno type="ISSN">0021-9541</idno><idno type="eISSN">1097-4652</idno><imprint><biblScope unit="vol">227</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="2775">2775</biblScope><biblScope unit="page" to="2787">2787</biblScope><biblScope unit="page-count">13</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2012-06">2012-06</date></imprint><idno type="ISSN">0021-9541</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-9541</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Alexa</term><term>Annexin</term><term>Apoptotic</term><term>Apoptotic cells</term><term>Apoptotic eosinophils</term><term>Biol</term><term>Calnexin</term><term>Cell surface</term><term>Cellular physiology</term><term>Cheng</term><term>Confocal</term><term>Confocal microscopy</term><term>Culture medium</term><term>Cytometry</term><term>Dapi</term><term>Different time periods</term><term>Egta</term><term>Eluate</term><term>Endothelial</term><term>Endothelial cells</term><term>Epithelial</term><term>Epithelial cells</term><term>Exosomal</term><term>Exosomal fraction</term><term>Exosome</term><term>Exosomes</term><term>Extracellular</term><term>Fang</term><term>Hajjar</term><term>Immunol</term><term>Intracellular</term><term>Jak2</term><term>Lung epithelial cells</term><term>Mediates</term><term>National cheng kung university</term><term>Paraformaldehyde</term><term>Pathway</term><term>Permeabilized</term><term>Phagocytosis</term><term>Phosphorylation</term><term>Plasma membrane</term><term>Pretreated</term><term>Primary antibodies</term><term>Protein expression</term><term>Receptor</term><term>Room temperature</term><term>Saponin</term><term>Supernatant</term><term>Surface annexin</term><term>Surface expression</term><term>Surface translocation</term><term>Total cell lysates</term><term>Transfected</term><term>Translocation</term><term>Upregulation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Annexin A2 (p36) is usually present together with its natural ligand p11 as a heterotetramer complex, which has multiple biological functions depending on its cellular localization. However, the detailed mechanism of annexin A2 translocation and its physiological role in inflammation remain unclear. Here, we show that IFN‐γ stimulation enhances surface translocation of annexin A2 on lung epithelial cells. While total annexin A2 protein remains unchanged, the expression of p11 is upregulated via the IFN‐γ‐activated JAK2/STAT1 signal pathway. Notably, IFN‐γ‐induced p11 expression is required for annexin A2 translocation to the cell surface. Since annexin A2 lacks a signal peptide for surface translocation by the classical endoplasmic reticulum‐Golgi route, its mode of trafficking remains unclear. We observed that p11‐dependent surface translocation of annexin A2 is associated with the exosomal secretion pathway. The IFN‐γ‐induced increase of annexin A2 in the exosomes is blocked in p11‐silenced cells. Furthermore, IFN‐γ‐induced surface expression of annexin A2 mediates phagocytosis of apoptotic cells by lung epithelial cells. These findings provide insights into the surface translocation mechanism of annexin A2 and illustrate a pivotal function of surface annexin A2 in the phagocytic response to IFN‐γ. J. Cell. Physiol. 227: 2775–2787, 2012. © 2011 Wiley Periodicals, Inc.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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