Role of G proteins and ERK activation in hemin-induced erythroid differentiation of K562 cells

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dc.contributor.authorKucukkaya B.
dc.contributor.authorArslan D.O.
dc.contributor.authorKan B.
dc.date.accessioned2024-07-12T21:51:44Z
dc.date.available2024-07-12T21:51:44Z
dc.date.issued2006en_US
dc.departmentMaltepe Üniversitesien_US
dc.description.abstractHeterotrimeric G proteins which couple extracellular signals to intracellular effectors play a central role in cell growth and differentiation. The pluripotent erythroleukemic cell line K562 that acquires the capability to synthesize hemoglobin in response to a variety of agents can be used as a model system for erythroid differentiation. Using Western blot analysis and RT-PCR, we studied alterations in G protein expression accompanying hemin-induced differentiation of K562 cells. We demonstrated the presence of G ?s, G?i2 and G?q and the absence of G?i1, G?o and G?16 in K562 cells. We observed the short form of G?s to be expressed predominantly in these cells. Treatment of K562 cells with hemin resulted in an increase in the levels of G?s and G ?q. On the other hand, the level of G?i2 was found to increase on the third day after induction with hemin, followed by a decrease to levels lower of those of uninduced cells. The mitogen-activated protein kinase ERK1/2 pathway is crucial in the control of cell proliferation and differentiation. Both Gi- and Gq-coupled receptors stimulate MAPK activation. We therefore examined the phosphorylation of ERK1/2 during hemin-induced differentiation of K562 cells. Using anti-ERK1/2 antibodies, we observed that ERK2 was primarily phosphorylated in K562 cells. ERK2 phosphorylation increased gradually until 48 h and returned to basal values by 96 h following hemin treatment. Our results suggest that changes in G protein expression and ERK2 activity are involved in hemin-induced differentiation of K562 cells. © 2005 Elsevier Inc. All rights reserved.en_US
dc.description.sponsorshipWe are grateful to Dr. Alfred Gilman for the anti-G ?common and G ß? antibodies, Dr. Bernd Nürnberg for the anti-G ?16 antibody and Dr. Azzam A. Maghazachi for the ERK antibodies. This study was supported by the Eczacibasi Scientific Research and Prize Fund, The Scientific and Technical Research Council of Turkey, SBAG-1710 and Marmara University Research Fund.en_US
dc.identifier.doi10.1016/j.lfs.2005.06.041
dc.identifier.endpage1224en_US
dc.identifier.issn0024-3205
dc.identifier.issue11en_US
dc.identifier.pmid16216279en_US
dc.identifier.scopus2-s2.0-31844457300en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage1217en_US
dc.identifier.urihttps://dx.doi.org/10.1016/j.lfs.2005.06.041
dc.identifier.urihttps://hdl.handle.net/20.500.12415/8311
dc.identifier.volume78en_US
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoenen_US
dc.relation.ispartofLife Sciencesen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.snmzKY02196
dc.subjectERK1/2 phosphorylationen_US
dc.subjectErythroid differentiationen_US
dc.subjectG proteinsen_US
dc.subjectHeminen_US
dc.subjectK562en_US
dc.titleRole of G proteins and ERK activation in hemin-induced erythroid differentiation of K562 cellsen_US
dc.typeArticle
dspace.entity.typePublication

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