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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003984naa a2200361 4500
001oai:DiVA.org:uu-193349
003SwePub
008130131s2013 | |||||||||||000 ||eng|
024a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1933492 URI
024a https://doi.org/10.1074/jbc.M112.3870762 DOI
040 a (SwePub)uu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Koutsioumpa, Marinau Department of Pharmacy, Laboratory of Molecular Pharmacology, University of Patras, Greece4 aut
2451 0a Interplay between αvβ3 Integrin and Nucleolin Regulates Human Endothelial and Glioma Cell Migration
264 1c 2013
338 a print2 rdacarrier
520 a The multifunctional protein nucleolin (NCL) is overexpressed on the surface of activated endothelial and tumor cells and mediates the stimulatory actions of several angiogenic growth factors, such as pleiotrophin (PTN). Because α(v)β(3) integrin is also required for PTN-induced cell migration, the aim of the present work was to study the interplay between NCL and α(v)β(3) by using biochemical, immunofluorescence, and proximity ligation assays in cells with genetically altered expression of the studied molecules. Interestingly, cell surface NCL localization was detected only in cells expressing α(v)β(3) and depended on the phosphorylation of β(3) at Tyr(773) through receptor protein-tyrosine phosphatase β/ζ (RPTPβ/ζ) and c-Src activation. Downstream of α(v)β(3,) PI3K activity mediated this phenomenon and cell surface NCL was found to interact with both α(v)β(3) and RPTPβ/ζ. Positive correlation of cell surface NCL and α(v)β(3) expression was also observed in human glioblastoma tissue arrays, and inhibition of cell migration by cell surface NCL antagonists was observed only in cells expressing α(v)β(3). Collectively, these data suggest that both expression and β(3) integrin phosphorylation at Tyr(773) determine the cell surface localization of NCL downstream of the RPTPβ/ζ/c-Src signaling cascade and can be used as a biomarker for the use of cell surface NCL antagonists as anticancer agents.
700a Polytarchou, Christosu Department of Cancer Immunology & AIDS, Dana Farber Cancer Institute, Boston, Massachusetts 02215, USA4 aut
700a Courty, Joséu Laboratoire CRRET, Universite Paris Est Creteil Val de Marne, avenue du General de Gaulle, 94010 Creteil Cedex, France4 aut
700a Zhang, Yueu Sino-French Research Centre for Life Sciences and Genomics, CNRS/LIA124, Rui Jin Hospital, Jiao Tong University Medical School, 197 Rui Jin Er Road, Shanghai 200025, China4 aut
700a Kieffer, Nellyu Sino-French Research Centre for Life Sciences and Genomics, CNRS/LIA124, Rui Jin Hospital, Jiao Tong University Medical School, 197 Rui Jin Er Road, Shanghai 200025, China4 aut
700a Mikelis, Constantinosu Department of Pharmacy, Laboratory of Molecular Pharmacology, University of Patras, Greece4 aut
700a Skandalis, Spyros Su Uppsala universitet,Ludwiginstitutet för cancerforskning4 aut
700a Hellman, Ulfu Uppsala universitet,Ludwiginstitutet för cancerforskning4 aut0 (Swepub:uu)ulfhm
700a Iliopoulos, Dimitriosu Department of Cancer Immunology & AIDS, Dana Farber Cancer Institute, Boston, Massachusetts 02215, USA4 aut
700a Papadimitriou, Evangeliau Department of Pharmacy, Laboratory of Molecular Pharmacology, University of Patras, Greece4 aut
710a Department of Pharmacy, Laboratory of Molecular Pharmacology, University of Patras, Greeceb Department of Cancer Immunology & AIDS, Dana Farber Cancer Institute, Boston, Massachusetts 02215, USA4 org
773t Journal of Biological Chemistryg 288:1, s. 343-354q 288:1<343-354x 0021-9258x 1083-351X
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-193349
8564 8u https://doi.org/10.1074/jbc.M112.387076

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