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Article ; Online: The laminin-binding integrins regulate nuclear factor κB-dependent epithelial cell polarity and inflammation.

Yazlovitskaya, Eugenia M / Plosa, Erin / Bock, Fabian / Viquez, Olga M / Mernaugh, Glenda / Gewin, Leslie S / De Arcangelis, Adele / Georges-Labouesse, Elisabeth / Sonnenberg, Arnoud / Blackwell, Timothy S / Pozzi, Ambra / Zent, Roy

Journal of cell science

2021 Volume 134, Issue 24

Abstract: The main laminin-binding integrins α3β1, α6β1 and α6β4 are co-expressed in the developing kidney collecting duct system. We previously showed that deleting the integrin α3 or α6 subunit in the ureteric bud, which gives rise to the kidney collecting ... ...

Abstract	The main laminin-binding integrins α3β1, α6β1 and α6β4 are co-expressed in the developing kidney collecting duct system. We previously showed that deleting the integrin α3 or α6 subunit in the ureteric bud, which gives rise to the kidney collecting system, caused either a mild or no branching morphogenesis phenotype, respectively. To determine whether these two integrin subunits cooperate in kidney collecting duct development, we deleted α3 and α6 in the developing ureteric bud. The collecting system of the double knockout phenocopied the α3 integrin conditional knockout. However, with age, the mice developed severe inflammation and fibrosis around the collecting ducts, resulting in kidney failure. Integrin α3α6-null collecting duct epithelial cells showed increased secretion of pro-inflammatory cytokines and displayed mesenchymal characteristics, causing loss of barrier function. These features resulted from increased nuclear factor kappa-B (NF-κB) activity, which regulated the Snail and Slug (also known as Snai1 and Snai2, respectively) transcription factors and their downstream targets. These data suggest that laminin-binding integrins play a key role in the maintenance of kidney tubule epithelial cell polarity and decrease pro-inflammatory cytokine secretion by regulating NF-κB-dependent signaling.
MeSH term(s)	Animals ; Epithelial Cells ; Inflammation/genetics ; Integrin alpha3beta1 ; Integrins/genetics ; Kidney Tubules, Collecting ; Laminin/genetics ; Mice ; NF-kappa B/genetics
Chemical Substances	Integrin alpha3beta1 ; Integrins ; Laminin ; NF-kappa B
Language	English
Publishing date	2021-12-22
Publishing country	England
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	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.259161
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Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 14: Show issues

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Article ; Online: The laminin binding α3 and α6 integrins cooperate to promote epithelial cell adhesion and growth.

Yazlovitskaya, Eugenia M / Viquez, Olga M / Tu, Tianxiang / De Arcangelis, Adele / Georges-Labouesse, Elisabeth / Sonnenberg, Arnoud / Pozzi, Ambra / Zent, Roy

Matrix biology : journal of the International Society for Matrix Biology

2018 Volume 77, Page(s) 101–116

Abstract: Integrins, the major receptors for cell-extracellular matrix (ECM) interactions, regulate multiple cell biological processes including adhesion, migration, proliferation and growth factor-dependent signaling. The principal laminin (LM) binding integrins ... ...

Abstract	Integrins, the major receptors for cell-extracellular matrix (ECM) interactions, regulate multiple cell biological processes including adhesion, migration, proliferation and growth factor-dependent signaling. The principal laminin (LM) binding integrins α3β1, α6β1 and α6β4 are usually co-expressed in cells and bind to multiple laminins with different affinities making it difficult to define their specific function. In this study, we generated kidney epithelial collecting duct (CD) cells that lack both the α3 and α6 integrin subunits. This deletion impaired cell adhesion and migration to LM-332 and LM-511 more than deleting α3 or α6 alone. Cell adhesion mediated by both α3β1 and α6 integrins was PI3K independent, but required K63-linked polyubiquitination of Akt by the ubiquitin-modifying enzyme TRAF6. Moreover, we provide evidence that glial-derived neurotrophic factor (GDNF) and fibroblast growth factor 10 (FGF10)- mediated cell signaling, spreading and proliferation were severely compromised in double integrin α3/α6- but not single α3- or α6-null CD cells. Interestingly, these growth factor-dependent cell functions required both PI3K- and TRAF6-dependent Akt activation. These data suggest that expression of the integrin α3 or α6 subunit is sufficient to mediate GDNF- and FGF10-dependent spreading, proliferation and signaling on LM-511. Thus, our study shows that α3 and α6 containing integrins promote distinct functions and signaling by CD cells on laminin substrata.
MeSH term(s)	Animals ; Cell Adhesion/drug effects ; Cell Adhesion Molecules/chemistry ; Cell Adhesion Molecules/metabolism ; Cell Movement/drug effects ; Cell Proliferation/drug effects ; Epithelial Cells/cytology ; Epithelial Cells/drug effects ; Epithelial Cells/metabolism ; Extracellular Matrix/chemistry ; Extracellular Matrix/drug effects ; Extracellular Matrix/metabolism ; Fibroblast Growth Factor 10/pharmacology ; Gene Deletion ; Gene Expression Regulation ; Glial Cell Line-Derived Neurotrophic Factor/pharmacology ; Humans ; Integrin alpha3/genetics ; Integrin alpha3/metabolism ; Integrin alpha3beta1/genetics ; Integrin alpha3beta1/metabolism ; Integrin alpha6/genetics ; Integrin alpha6/metabolism ; Integrin alpha6beta1/genetics ; Integrin alpha6beta1/metabolism ; Integrin alpha6beta4/genetics ; Integrin alpha6beta4/metabolism ; Intracellular Signaling Peptides and Proteins ; Kidney Tubules, Collecting/cytology ; Kidney Tubules, Collecting/metabolism ; Laminin/chemistry ; Laminin/metabolism ; Mice ; Mice, Knockout ; Phosphatidylinositol 3-Kinases/genetics ; Phosphatidylinositol 3-Kinases/metabolism ; Primary Cell Culture ; Protein Binding ; Proto-Oncogene Proteins c-akt/genetics ; Proto-Oncogene Proteins c-akt/metabolism ; Signal Transduction ; TNF Receptor-Associated Factor 6/genetics ; TNF Receptor-Associated Factor 6/metabolism ; Kalinin
Chemical Substances	Cell Adhesion Molecules ; FGF10 protein, human ; Fibroblast Growth Factor 10 ; Glial Cell Line-Derived Neurotrophic Factor ; Integrin alpha3 ; Integrin alpha3beta1 ; Integrin alpha6 ; Integrin alpha6beta1 ; Integrin alpha6beta4 ; Intracellular Signaling Peptides and Proteins ; Laminin ; TNF Receptor-Associated Factor 6 ; Tifab protein, human ; laminin 10 ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
Language	English
Publishing date	2018-09-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1183793-7
ISSN	1569-1802 ; 0945-053X
ISSN (online)	1569-1802
ISSN	0945-053X
DOI	10.1016/j.matbio.2018.08.010
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Zs.A 1694: Show issues

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Article ; Online: α6 integrin subunit regulates cerebellar development.

Marchetti, Giovanni / De Arcangelis, Adèle / Pfister, Véronique / Georges-Labouesse, Elisabeth

Cell adhesion & migration

2013 Volume 7, Issue 3, Page(s) 325–332

Abstract: Mutations in genes encoding several basal lamina components as well as their cellular receptors disrupt normal deposition and remodeling of the cortical basement membrane resulting in a disorganized cerebral and cerebellar cortex. The α6 integrin was the ...

Abstract	Mutations in genes encoding several basal lamina components as well as their cellular receptors disrupt normal deposition and remodeling of the cortical basement membrane resulting in a disorganized cerebral and cerebellar cortex. The α6 integrin was the first α subunit associated with cortical lamination defects and formation of neural ectopias. In order to understand the precise role of α6 integrin in the central nervous system (CNS), we have generated mutant mice carrying specific deletion of α6 integrin in neuronal and glia precursors by crossing α6 conditional knockout mice with Nestin-Cre line. Cerebral cortex development occurred properly in the resulting α6 (fl/fl;nestin-Cre) mutant animals. Interestingly, however, cerebellum displayed foliation pattern defects although granule cell (GC) proliferation and migration were not affected. Intriguingly, analysis of Bergmann glial (BG) scaffold revealed abnormalities in fibers morphology associated with reduced processes outgrowth and altered actin cytoskeleton. Overall, these data show that α6 integrin receptors are required in BG cells to provide a proper fissure formation during cerebellum morphogenesis.
MeSH term(s)	Actin Cytoskeleton ; Animals ; Cell Line ; Cell Movement ; Cell Proliferation ; Cerebellum/cytology ; Cerebellum/embryology ; Cerebellum/growth & development ; Gene Expression Regulation, Developmental ; Integrin alpha6/genetics ; Integrin alpha6/metabolism ; Mice ; Mice, Knockout ; Morphogenesis ; Neuroglia/metabolism ; RNA, Messenger/analysis
Chemical Substances	Integrin alpha6 ; RNA, Messenger
Language	English
Publishing date	2013-05-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2268518-2
ISSN	1933-6926 ; 1933-6918
ISSN (online)	1933-6926
ISSN	1933-6918
DOI	10.4161/cam.25140
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Article ; Online: An Arf6- and caveolae-dependent pathway links hemidesmosome remodeling and mechanoresponse.

Osmani, Naël / Pontabry, Julien / Comelles, Jordi / Fekonja, Nina / Goetz, Jacky G / Riveline, Daniel / Georges-Labouesse, Elisabeth / Labouesse, Michel

Molecular biology of the cell

2017 Volume 29, Issue 4, Page(s) 435–451

Abstract: Hemidesmosomes (HDs) are epithelial-specific cell-matrix adhesions that stably anchor the intracellular keratin network to the extracellular matrix. Although their main role is to protect the epithelial sheet from external mechanical strain, how HDs ... ...

Abstract	Hemidesmosomes (HDs) are epithelial-specific cell-matrix adhesions that stably anchor the intracellular keratin network to the extracellular matrix. Although their main role is to protect the epithelial sheet from external mechanical strain, how HDs respond to mechanical stress remains poorly understood. Here we identify a pathway essential for HD remodeling and outline its role with respect to α6β4 integrin recycling. We find that α6β4 integrin chains localize to the plasma membrane, caveolae, and ADP-ribosylation factor-6+ (Arf6+) endocytic compartments. Based on fluorescence recovery after photobleaching and endocytosis assays, integrin recycling between both sites requires the small GTPase Arf6 but neither caveolin1 (Cav1) nor Cavin1. Strikingly, when keratinocytes are stretched or hypo-osmotically shocked, α6β4 integrin accumulates at cell edges, whereas Cav1 disappears from it. This process, which is isotropic relative to the orientation of stretch, depends on Arf6, Cav1, and Cavin1. We propose that mechanically induced HD growth involves the isotropic flattening of caveolae (known for their mechanical buffering role) associated with integrin diffusion and turnover.
MeSH term(s)	ADP-Ribosylation Factors/metabolism ; Caveolin 1/metabolism ; Cell Line ; Cell Membrane/metabolism ; Hemidesmosomes/metabolism ; Hemidesmosomes/ultrastructure ; Humans ; Integrin beta4/metabolism ; Keratinocytes/metabolism ; Microscopy, Electron, Transmission ; Microscopy, Immunoelectron
Chemical Substances	Caveolin 1 ; Integrin beta4 ; ADP-Ribosylation Factors (EC 3.6.5.2) ; ADP-ribosylation factor 6 (EC 3.6.5.2)
Language	English
Publishing date	2017-12-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E17-06-0356
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Zs.A 2853: 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)
Zs.MO 410: Show issues

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Article ; Online: Laminin-binding integrins are essential for the maintenance of functional mammary secretory epithelium in lactation.

Romagnoli, Mathilde / Bresson, Laura / Di-Cicco, Amandine / Pérez-Lanzón, María / Legoix, Patricia / Baulande, Sylvain / de la Grange, Pierre / De Arcangelis, Adèle / Georges-Labouesse, Elisabeth / Sonnenberg, Arnoud / Deugnier, Marie-Ange / Glukhova, Marina A / Faraldo, Marisa M

Development (Cambridge, England)

2020 Volume 147, Issue 4

Abstract: Integrin dimers α3/β1, α6/β1 and α6/β4 are the mammary epithelial cell receptors for laminins, which are major components of the mammary basement membrane. The roles of specific basement membrane components and their integrin receptors in the regulation ... ...

Abstract	Integrin dimers α3/β1, α6/β1 and α6/β4 are the mammary epithelial cell receptors for laminins, which are major components of the mammary basement membrane. The roles of specific basement membrane components and their integrin receptors in the regulation of functional gland development have not been analyzed in detail. To investigate the functions of laminin-binding integrins, we obtained mutant mice with mammary luminal cell-specific deficiencies of the α3 and α6 integrin chains generated using the Cre-Lox approach. During pregnancy, mutant mice displayed decreased luminal progenitor activity and retarded lobulo-alveolar development. Mammary glands appeared functional at the onset of lactation in mutant mice; however, myoepithelial cell morphology was markedly altered, suggesting cellular compensation mechanisms involving cytoskeleton reorganization. Notably, lactation was not sustained in mutant females, and the glands underwent precocious involution. Inactivation of the p53 gene rescued the growth defects but did not restore lactogenesis in mutant mice. These results suggest that the p53 pathway is involved in the control of mammary cell proliferation and survival downstream of laminin-binding integrins, and underline an essential role of cell interactions with laminin for lactogenic differentiation.
MeSH term(s)	Animals ; Cell Differentiation ; Cell Lineage ; Cell Proliferation ; Cell Survival ; Cytoskeleton/physiology ; Disease Progression ; Female ; Gene Deletion ; Hormones/physiology ; Integrin alpha3/physiology ; Integrin alpha6/physiology ; Integrin beta1/physiology ; Integrin beta4/physiology ; Integrins/physiology ; Lactation ; Mammary Glands, Animal/physiology ; Mice ; Mice, Inbred C57BL ; Mice, Inbred CBA ; Mice, Knockout ; Mice, Mutant Strains ; Mutation ; Neoplastic Stem Cells/cytology ; Oligonucleotide Array Sequence Analysis ; Ovary/physiology ; Phenotype ; Pregnancy ; Pregnancy, Animal ; Prognosis ; Protein Binding ; Protein Multimerization
Chemical Substances	Hormones ; Integrin alpha3 ; Integrin alpha6 ; Integrin beta1 ; Integrin beta4 ; Integrins ; Itga3 protein, mouse ; Itgb1 protein, mouse ; Itgb4 protein, mouse
Language	English
Publishing date	2020-02-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.181552
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Ub I Zs.183: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MG 91: Show issues

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Article: Cell adhesion: parallels between vertebrate and invertebrate focal adhesions.

Labouesse, Michel / Georges-Labouesse, Elisabeth

Current biology : CB

2003 Volume 13, Issue 13, Page(s) R528–30

Abstract: Recent studies highlight the striking similarity between vertebrate focal adhesion plaques and Caenorhabditis elegans muscle adhesion structures and position LIM domain proteins as central players at focal adhesions. ...

Abstract	Recent studies highlight the striking similarity between vertebrate focal adhesion plaques and Caenorhabditis elegans muscle adhesion structures and position LIM domain proteins as central players at focal adhesions.
MeSH term(s)	Animals ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins/metabolism ; Cell Adhesion Molecules/physiology ; Focal Adhesions/physiology ; Phylogeny ; Vertebrates ; Zinc Fingers/physiology ; rac GTP-Binding Proteins/metabolism
Chemical Substances	Caenorhabditis elegans Proteins ; Cell Adhesion Molecules ; Mig-2 protein, C elegans (EC 3.6.1.-) ; rac GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2003-07-01
Publishing country	England
Document type	Comparative Study ; Journal Article ; Review
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/s0960-9822(03)00448-2
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Zs.A 3208: Show issues

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Article ; Online: Separation of distinct adhesion complexes and associated cytoskeleton by a micro-stencil-printing method.

Caballero, David / Osmani, Naël / Georges-Labouesse, Elisabeth / Labouesse, Michel / Riveline, Daniel

Cell adhesion & migration

2012 Volume 6, Issue 6, Page(s) 471–475

Abstract: Adhesion between cells and the extracellular matrix is mediated by different types of transmembraneous proteins. Their associations to specific partners lead to the assembly of contacts such as focal adhesions and hemidesmosomes. The spatial overlap ... ...

Abstract	Adhesion between cells and the extracellular matrix is mediated by different types of transmembraneous proteins. Their associations to specific partners lead to the assembly of contacts such as focal adhesions and hemidesmosomes. The spatial overlap between both contacts within cells has however limited the study of each type of contact. Here we show that with "stampcils" focal contacts and hemidesmosomes can be spatially separated: cells are plated within the cavities of a stencil and the grids of the stencil serve as stamps for grafting an extracellular matrix protein-fibronectin. Cells engage new contacts on stamped zones leading to the segregation of adhesions and their associated cytoskeletons, i.e., actin and intermediate filaments of keratins. This new method should provide new insights into cell contacts compositions and dynamics.
MeSH term(s)	Actins/metabolism ; Cell Adhesion ; Cell Adhesion Molecules/metabolism ; Cell Culture Techniques ; Cell Line, Tumor ; Cell Movement ; Cytoskeleton/metabolism ; Fibronectins/metabolism ; Fluorescent Antibody Technique/methods ; Focal Adhesions/metabolism ; Hemidesmosomes/metabolism ; Humans ; Keratinocytes/metabolism ; Multiprotein Complexes/metabolism ; Staining and Labeling/methods ; Time Factors
Chemical Substances	Actins ; Cell Adhesion Molecules ; Fibronectins ; Multiprotein Complexes
Language	English
Publishing date	2012-10-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2268518-2
ISSN	1933-6926 ; 1933-6918
ISSN (online)	1933-6926
ISSN	1933-6918
DOI	10.4161/cam.22198
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Article ; Online: Deciphering the Mammary Stem Cell Niche: A Role for Laminin-Binding Integrins.

Romagnoli, Mathilde / Cagnet, Stéphanie / Chiche, Aurélie / Bresson, Laura / Baulande, Sylvain / de la Grange, Pierre / De Arcangelis, Adèle / Kreft, Maaike / Georges-Labouesse, Elisabeth / Sonnenberg, Arnoud / Deugnier, Marie-Ange / Raymond, Karine / Glukhova, Marina A / Faraldo, Marisa M

Stem cell reports

2019 Volume 12, Issue 4, Page(s) 831–844

Abstract: Integrins, which bind laminin, a major component of the mammary basement membrane, are strongly expressed in basal stem cell-enriched populations, but their role in controlling mammary stem cell function remains unclear. We found that stem cell activity, ...

Abstract	Integrins, which bind laminin, a major component of the mammary basement membrane, are strongly expressed in basal stem cell-enriched populations, but their role in controlling mammary stem cell function remains unclear. We found that stem cell activity, as evaluated in transplantation and mammosphere assays, was reduced in mammary basal cells depleted of laminin receptors containing α3- and α6-integrin subunits. This was accompanied by low MDM2 levels, p53 stabilization, and diminished proliferative capacity. Importantly, disruption of p53 function restored the clonogenicity of α3/α6-integrin-depleted mammary basal stem cells, while inhibition of RHO or myosin II, leading to decreased p53 activity, rescued the mammosphere formation. These data suggest that α3/α6-integrin-mediated adhesion plays an essential role in controlling the proliferative potential of mammary basal stem/progenitor cells through myosin II-mediated regulation of p53 and indicate that laminins might be important components of the mammary stem cell niche.
Language	English
Publishing date	2019-03-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2720528-9
ISSN	2213-6711 ; 2213-6711
ISSN (online)	2213-6711
ISSN	2213-6711
DOI	10.1016/j.stemcr.2019.02.008
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Article ; Online: Deciphering the Mammary Stem Cell Niche: A Role for Laminin-Binding Integrins.

Stem cell reports

2019 Volume 12, Issue 5, Page(s) 1178

Language	English
Publishing date	2019-05-15
Publishing country	United States
Document type	Published Erratum
ZDB-ID	2720528-9
ISSN	2213-6711 ; 2213-6711
ISSN (online)	2213-6711
ISSN	2213-6711
DOI	10.1016/j.stemcr.2019.04.018
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Article ; Online: Tie2-dependent deletion of α6 integrin subunit in mice reduces tumor growth and angiogenesis.

Bouvard, Claire / Segaoula, Zacharie / De Arcangelis, Adèle / Galy-Fauroux, Isabelle / Mauge, Laetitia / Fischer, Anne-Marie / Georges-Labouesse, Elisabeth / Helley, Dominique

International journal of oncology

2014 Volume 45, Issue 5, Page(s) 2058–2064

Abstract: The α6 integrin subunit (α6) has been implicated in cancer cell migration and in the progression of several malignancies, but its role in tumor angiogenesis is unclear. In mice, anti-α6 blocking antibodies reduce tumor angiogenesis, whereas Tie1- ... ...

Abstract	The α6 integrin subunit (α6) has been implicated in cancer cell migration and in the progression of several malignancies, but its role in tumor angiogenesis is unclear. In mice, anti-α6 blocking antibodies reduce tumor angiogenesis, whereas Tie1-dependent α6 gene deletion enhances neovessel formation in melanoma and lung carcinoma. To clarify the discrepancy in these results we used the cre-lox system to generate a mouse line, α6fl/fl‑Tie2Cre(+), with α6 gene deletion specifically in Tie2-lineage cells: endothelial cells, pericytes, subsets of hematopoietic stem cells, and Tie2-expressing monocytes/macrophages (TEMs), known for their proangiogenic properties. Loss of α6 expression in α6fl/fl‑Tie2Cre(+) mice reduced tumor growth in a murine B16F10 melanoma model. Immunohistological analysis of the tumors showed that Tie2-dependent α6 gene deletion was associated with reduced tumor vascularization and with reduced infiltration of proangiogenic Tie2-expressing macrophages. These findings demonstrate that α6 integrin subunit plays a major role in tumor angiogenesis and TEM infiltration. Targeting α6 could be used as a strategy to reduce tumor growth.
MeSH term(s)	Animals ; Cell Lineage ; Cell Movement/genetics ; Cell Proliferation/genetics ; Gene Expression Regulation, Neoplastic ; Humans ; Integrin alpha6/biosynthesis ; Integrin alpha6/genetics ; Macrophages/metabolism ; Macrophages/pathology ; Melanoma, Experimental/genetics ; Melanoma, Experimental/pathology ; Mice ; Mice, Transgenic ; Neovascularization, Pathologic/genetics ; Neovascularization, Pathologic/pathology ; Receptor, TIE-2/biosynthesis ; Receptor, TIE-2/genetics
Chemical Substances	Integrin alpha6 ; Receptor, TIE-2 (EC 2.7.10.1) ; Tek protein, mouse (EC 2.7.10.1)
Language	English
Publishing date	2014-11
Publishing country	Greece
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1154403-x
ISSN	1791-2423 ; 1019-6439
ISSN (online)	1791-2423
ISSN	1019-6439
DOI	10.3892/ijo.2014.2631
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