FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2017328052> ?p ?o ?g. }

• W2017328052 endingPage "65" @default.
• W2017328052 startingPage "57" @default.
• W2017328052 abstract "In human PMN (polymorphonuclear cells), challenged by P-selectin, the β2-integrin Mac-1 (macrophage antigen-1) promoted the activation of the SRC (cellular homologue of Rous sarcoma virus oncogenic protein) family members HCK (haematopoietic cell kinase) and LYN (an SRC family protein tyrosine kinase) and phosphorylation of a P-110 (110 kDa protein). SRC kinase activity in turn was necessary for macrophage antigen-1-mediated adhesion [Piccardoni, Sideri, Manarini, Piccoli, Martelli, de Gaetano, Cerletti and Evangelista (2001) Blood 98, 108–116]. This suggested that an SRC-dependent outside-in signalling strengthens the β2-integrin interaction with the ligand. To support this hypothesis further, in the present study, we used the monoclonal antibody KIM127 or manganese to lock β2 integrins in a high-affinity state, and homotypic PMN adhesion was analysed to monitor β2-integrin adhesive function. KIM127 or manganese induced PMN homotypic adhesion and P-110 phosphorylation. Both these processes were abolished by blocking antibodies against the common β2 chain, by a combination of antibodies against αL and αM or by inhibitors of SRC activity. Confocal microscopy showed that activation epitopes were expressed by β2 integrins co-localized with patches of F-actin at the adhesion sites. Blockade of SRC kinases or of actin polymerization prevented clustering of activated integrins as well as F-actin accumulation. FACS analysis showed that SRC inhibitors modified neither basal nor manganese-induced KIM127 binding. An SRC-dependent outside-in signalling initiated by β2 integrins was also required for adhesion triggered by interleukin-8. These results confirm the hypothesis that an SRC-dependent outside-in signalling triggered by high affinity and ligand binding is necessary to stabilize β2-integrin-mediated adhesion. Allowing clustering of activated integrins, SRC might link the high-affinity with the high-avidity state. Proline-rich tyrosine kinase-2 appears to be involved in this process." @default.
• W2017328052 created "2016-06-24" @default.
• W2017328052 creator A5003668565 @default.
• W2017328052 creator A5018086938 @default.
• W2017328052 creator A5028922467 @default.
• W2017328052 creator A5032438574 @default.
• W2017328052 creator A5032733277 @default.
• W2017328052 creator A5033092400 @default.
• W2017328052 creator A5056729409 @default.
• W2017328052 creator A5056779726 @default.
• W2017328052 creator A5063700425 @default.
• W2017328052 creator A5064218020 @default.
• W2017328052 date "2004-05-15" @default.
• W2017328052 modified "2023-10-12" @default.
• W2017328052 title "SRC-dependent outside-in signalling is a key step in the process of autoregulation of beta2 integrins in polymorphonuclear cells" @default.
• W2017328052 cites W113835883 @default.
• W2017328052 cites W133332340 @default.
• W2017328052 cites W141774154 @default.
• W2017328052 cites W1484320290 @default.
• W2017328052 cites W1489319787 @default.
• W2017328052 cites W1510401881 @default.
• W2017328052 cites W1521881285 @default.
• W2017328052 cites W1532497207 @default.
• W2017328052 cites W1534090153 @default.
• W2017328052 cites W1572786395 @default.
• W2017328052 cites W1613698407 @default.
• W2017328052 cites W1646222158 @default.
• W2017328052 cites W1865638244 @default.
• W2017328052 cites W1867680312 @default.
• W2017328052 cites W1895802579 @default.
• W2017328052 cites W1970923523 @default.
• W2017328052 cites W1982536372 @default.
• W2017328052 cites W1983447167 @default.
• W2017328052 cites W2002475242 @default.
• W2017328052 cites W2006018450 @default.
• W2017328052 cites W2013867315 @default.
• W2017328052 cites W2015831421 @default.
• W2017328052 cites W2027266132 @default.
• W2017328052 cites W2030192350 @default.
• W2017328052 cites W2039308855 @default.
• W2017328052 cites W2041827175 @default.
• W2017328052 cites W2045619217 @default.
• W2017328052 cites W2062823148 @default.
• W2017328052 cites W2077634410 @default.
• W2017328052 cites W2078970200 @default.
• W2017328052 cites W2090895449 @default.
• W2017328052 cites W2097877636 @default.
• W2017328052 cites W2120581641 @default.
• W2017328052 cites W2122028809 @default.
• W2017328052 cites W2125435732 @default.
• W2017328052 cites W2126618915 @default.
• W2017328052 cites W2135987235 @default.
• W2017328052 cites W2140799426 @default.
• W2017328052 cites W2153844283 @default.
• W2017328052 cites W2160953520 @default.
• W2017328052 cites W2161878252 @default.
• W2017328052 cites W2162498814 @default.
• W2017328052 cites W2163240674 @default.
• W2017328052 doi "https://doi.org/10.1042/bj20040151" @default.
• W2017328052 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1224154" @default.
• W2017328052 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14969582" @default.
• W2017328052 hasPublicationYear "2004" @default.
• W2017328052 type Work @default.
• W2017328052 sameAs 2017328052 @default.
• W2017328052 citedByCount "39" @default.
• W2017328052 countsByYear W20173280522012 @default.
• W2017328052 countsByYear W20173280522013 @default.
• W2017328052 countsByYear W20173280522014 @default.
• W2017328052 countsByYear W20173280522015 @default.
• W2017328052 countsByYear W20173280522016 @default.
• W2017328052 countsByYear W20173280522017 @default.
• W2017328052 countsByYear W20173280522018 @default.
• W2017328052 countsByYear W20173280522019 @default.
• W2017328052 countsByYear W20173280522023 @default.
• W2017328052 crossrefType "journal-article" @default.
• W2017328052 hasAuthorship W2017328052A5003668565 @default.
• W2017328052 hasAuthorship W2017328052A5018086938 @default.
• W2017328052 hasAuthorship W2017328052A5028922467 @default.
• W2017328052 hasAuthorship W2017328052A5032438574 @default.
• W2017328052 hasAuthorship W2017328052A5032733277 @default.
• W2017328052 hasAuthorship W2017328052A5033092400 @default.
• W2017328052 hasAuthorship W2017328052A5056729409 @default.
• W2017328052 hasAuthorship W2017328052A5056779726 @default.
• W2017328052 hasAuthorship W2017328052A5063700425 @default.
• W2017328052 hasAuthorship W2017328052A5064218020 @default.
• W2017328052 hasBestOaLocation W20173280522 @default.
• W2017328052 hasConcept C108636557 @default.
• W2017328052 hasConcept C1491633281 @default.
• W2017328052 hasConcept C153911025 @default.
• W2017328052 hasConcept C170493617 @default.
• W2017328052 hasConcept C171779818 @default.
• W2017328052 hasConcept C183141693 @default.
• W2017328052 hasConcept C184235292 @default.
• W2017328052 hasConcept C185592680 @default.
• W2017328052 hasConcept C195687474 @default.
• W2017328052 hasConcept C196347352 @default.
• W2017328052 hasConcept C2779976819 @default.
• W2017328052 hasConcept C553184892 @default.

• next