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Article: Signaling mechanisms of pertussis toxin-induced myelomonocytic cell adhesion: Role of tyrosine phosphorylation

TitleSignaling mechanisms of pertussis toxin-induced myelomonocytic cell adhesion: Role of tyrosine phosphorylation
Authors
Issue Date1997
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
Citation
Biochemical And Biophysical Research Communications, 1997, v. 236 n. 2, p. 479-482 How to Cite?
AbstractPertussis toxin (PTX) was thought to bind Mac-1 integrin receptor (CD11b/CD18) on TGF-β1/D 3-primed U937 cells and induced cellular adhesion to serum-coated plate. The present study was to investigate the signal transduction pathway utilized by PTX to initiate myeloid cell adhesion in serum. Immunoblotting study showed that PTX induced tyrosine phosphorylation of two cytoplasmic proteins of 150 kDa and 90 kDa in TGF-β1/D 3-primed U937 cells in a time-dependent manner. In addition, PTX-induced myelomonocytic cell adhesion was abolished in the presence of genistein (100 μM), a specific tyrosine kinase inhibitor. 2LPM19c (2 μg/ml), a mouse monoclonal antibody against the CD11b subunit of Mac-1 integrin, or ethylenediamine tetraacetic acid (EDTA, 5 mM) prevented PTX-mediated U937 cell adhesion. On the other hand, nifedipine (1 μM), a calcium channel blocker, significantly reduced PTX-induced U937 cell adhesion. Taken together, it is suggested that binding of PTX to Mac-1 integrin receptor on primed U937 cells triggers protein tyrosine phosphorylation and, to a lesser extent, Ca +2 influx, which eventually lead to monocytic cell adhesion in serum.
Persistent Identifierhttp://hdl.handle.net/10722/83289
ISSN
2015 Impact Factor: 2.371
2015 SCImago Journal Rankings: 1.152
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWong, WSFen_HK
dc.contributor.authorLuk, JMen_HK
dc.date.accessioned2010-09-06T08:39:15Z-
dc.date.available2010-09-06T08:39:15Z-
dc.date.issued1997en_HK
dc.identifier.citationBiochemical And Biophysical Research Communications, 1997, v. 236 n. 2, p. 479-482en_HK
dc.identifier.issn0006-291Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/83289-
dc.description.abstractPertussis toxin (PTX) was thought to bind Mac-1 integrin receptor (CD11b/CD18) on TGF-β1/D 3-primed U937 cells and induced cellular adhesion to serum-coated plate. The present study was to investigate the signal transduction pathway utilized by PTX to initiate myeloid cell adhesion in serum. Immunoblotting study showed that PTX induced tyrosine phosphorylation of two cytoplasmic proteins of 150 kDa and 90 kDa in TGF-β1/D 3-primed U937 cells in a time-dependent manner. In addition, PTX-induced myelomonocytic cell adhesion was abolished in the presence of genistein (100 μM), a specific tyrosine kinase inhibitor. 2LPM19c (2 μg/ml), a mouse monoclonal antibody against the CD11b subunit of Mac-1 integrin, or ethylenediamine tetraacetic acid (EDTA, 5 mM) prevented PTX-mediated U937 cell adhesion. On the other hand, nifedipine (1 μM), a calcium channel blocker, significantly reduced PTX-induced U937 cell adhesion. Taken together, it is suggested that binding of PTX to Mac-1 integrin receptor on primed U937 cells triggers protein tyrosine phosphorylation and, to a lesser extent, Ca +2 influx, which eventually lead to monocytic cell adhesion in serum.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/descriptionen_HK
dc.relation.ispartofBiochemical and Biophysical Research Communicationsen_HK
dc.titleSignaling mechanisms of pertussis toxin-induced myelomonocytic cell adhesion: Role of tyrosine phosphorylationen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0006-291X&volume=236&spage=479&epage=482&date=1997&atitle=Signaling+mechanisms+of+pertussis+toxin-induced+myelomonocytic+cell+adhesion:+role+of+tyrosine+phosphorylationen_HK
dc.identifier.emailLuk, JM: jmluk@hkucc.hku.hken_HK
dc.identifier.authorityLuk, JM=rp00349en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1006/bbrc.1997.6986en_HK
dc.identifier.pmid9240464-
dc.identifier.scopuseid_2-s2.0-0031577278en_HK
dc.identifier.hkuros24778en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031577278&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume236en_HK
dc.identifier.issue2en_HK
dc.identifier.spage479en_HK
dc.identifier.epage482en_HK
dc.identifier.isiWOS:A1997XM95500050-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWong, WSF=16225877200en_HK
dc.identifier.scopusauthoridLuk, JM=7006777791en_HK

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