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Article: Determination of interactions between human thrombopoietin and its receptor MPL by yeast two-hybrid system and affinity biosensor

TitleDetermination of interactions between human thrombopoietin and its receptor MPL by yeast two-hybrid system and affinity biosensor
Authors
Hsieh, DPHHuxtable, SNg, KFChen, HMTsang, PWKWang, JXu, P
KeywordsHeterologous expression
IAsys Affinity Biosensor
MPL
Thrombopoietin (TPO)
Yeast two-hybrid
Issue Date2000
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/biocel
Citation
International Journal Of Biochemistry And Cell Biology, 2000, v. 32 n. 5, p. 481-488 How to Cite?
DOI: http://dx.doi.org/10.1016/S1357-2725(99)00132-6
AbstractThe binding of human thrombopoietin to the extracellular domain of its receptor MPL prompts a cascade transduction of intracellular signals, leading to the development of megakaryocyte precursors and the production of circulating platelets. We have used a yeast two-hybrid system to reveal, via in vivo interactions between different deletion constructs of MPL and thrombopoietin, that the extracellular subunit 1 of MPL is the ligand binding site and the N-terminal domain of thrombopoietin alone is sufficient for the binding. The extracellular portion of MPL was heterologously expressed in E. coli and its specific affinity with thrombopoietin was visualized in vitro by resonance mirror biosensor technique. Copyright (C) 2000.
Persistent Identifierhttp://hdl.handle.net/10722/90702
ISSN
1357-2725
2021 Impact Factor: 5.652
2020 SCImago Journal Rankings: 1.241
ISI Accession Number ID
WOS:000086837700002
References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorHsieh, DPHen_HK
dc.contributor.authorHuxtable, Sen_HK
dc.contributor.authorNg, KFen_HK
dc.contributor.authorChen, HMen_HK
dc.contributor.authorTsang, PWKen_HK
dc.contributor.authorWang, Jen_HK
dc.contributor.authorXu, Pen_HK
dc.date.accessioned2010-09-17T10:07:01Z-
dc.date.available2010-09-17T10:07:01Z-
dc.date.issued2000en_HK
dc.identifier.citationInternational Journal Of Biochemistry And Cell Biology, 2000, v. 32 n. 5, p. 481-488en_HK
dc.identifier.issn1357-2725en_HK
dc.identifier.urihttp://hdl.handle.net/10722/90702-
dc.description.abstractThe binding of human thrombopoietin to the extracellular domain of its receptor MPL prompts a cascade transduction of intracellular signals, leading to the development of megakaryocyte precursors and the production of circulating platelets. We have used a yeast two-hybrid system to reveal, via in vivo interactions between different deletion constructs of MPL and thrombopoietin, that the extracellular subunit 1 of MPL is the ligand binding site and the N-terminal domain of thrombopoietin alone is sufficient for the binding. The extracellular portion of MPL was heterologously expressed in E. coli and its specific affinity with thrombopoietin was visualized in vitro by resonance mirror biosensor technique. Copyright (C) 2000.en_HK
dc.languageengen_HK
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/biocelen_HK
dc.relation.ispartofInternational Journal of Biochemistry and Cell Biologyen_HK
dc.subjectHeterologous expression-
dc.subjectIAsys Affinity Biosensor-
dc.subjectMPL-
dc.subjectThrombopoietin (TPO)-
dc.subjectYeast two-hybrid-
dc.subject.meshBinding Sitesen_HK
dc.subject.meshBiosensing Techniquesen_HK
dc.subject.meshHumansen_HK
dc.subject.meshNeoplasm Proteinsen_HK
dc.subject.meshProto-Oncogene Proteins - genetics - isolation & purification - metabolismen_HK
dc.subject.meshReceptors, Cytokineen_HK
dc.subject.meshReceptors, Thrombopoietinen_HK
dc.subject.meshRecombinant Proteins - genetics - isolation & purification - metabolismen_HK
dc.subject.meshThrombopoietin - genetics - metabolismen_HK
dc.subject.meshTime Factorsen_HK
dc.subject.meshTwo-Hybrid System Techniquesen_HK
dc.subject.meshYeasts - geneticsen_HK
dc.titleDetermination of interactions between human thrombopoietin and its receptor MPL by yeast two-hybrid system and affinity biosensoren_HK
dc.typeArticleen_HK
dc.identifier.emailTsang, PWK:pwktsang@hku.hken_HK
dc.identifier.authorityTsang, PWK=rp01388en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S1357-2725(99)00132-6en_HK
dc.identifier.pmid10736563-
dc.identifier.scopuseid_2-s2.0-0034192353en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034192353&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume32en_HK
dc.identifier.issue5en_HK
dc.identifier.spage481en_HK
dc.identifier.epage488en_HK
dc.identifier.isiWOS:000086837700002-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridHsieh, DPH=7103265321en_HK
dc.identifier.scopusauthoridHuxtable, S=6701525229en_HK
dc.identifier.scopusauthoridNg, KF=7403178777en_HK
dc.identifier.scopusauthoridChen, HM=7501623412en_HK
dc.identifier.scopusauthoridTsang, PWK=8334953500en_HK
dc.identifier.scopusauthoridWang, J=7701314238en_HK
dc.identifier.scopusauthoridXu, P=7202215533en_HK
dc.identifier.issnl1357-2725-

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