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Cyclic nucleotide response element binding (CREB) protein activation is involved in K562 erythroleukemia cells differentiation
Author(s) -
Di Pietro Roberta,
di Giacomo Viviana,
Caravatta Luciana,
Sancilio Silvia,
Rana Rosa Alba,
Cataldi Amelia
Publication year - 2006
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.21106
Subject(s) - creb , k562 cells , hemin , microbiology and biotechnology , biology , p38 mitogen activated protein kinases , cellular differentiation , kinase , transcription factor , protein kinase a , chemistry , apoptosis , biochemistry , heme , gene , enzyme
K562 are human erythroleukemia cells inducible to differentiate into megakaryocytic or erythroid lineage by different agents. Cyclic nucleotide Response Element Binding (CREB) protein, a nuclear transcription factor which mediates c‐AMP signaling, is a potential candidate involved in the occurrence of erythroid differentiation and adaptive response. Here we investigated signaling events in K562 cells induced with 30 µM hemin to undergo erythroid differentiation. CREB activation was detected early 1 h after hemin treatment and up to 4 and 6 days of treatment, when K562 terminal differentiation occurs together with caspase‐3 maximal activation and PARP degradation. It was interesting to note that after hemin treatment in the presence of SB203580, p38 MAP kinase specific inhibitor, a reduced rate of CREB phosphorylation as well as a lower percentage of CD71/Gly+ (Glycophorin A) cells were detectable, demonstrating the p38 MAP kinase dependency of these phenomena. All in all these results document a novel relationship between CREB activation and differentiation‐related apoptotic cell death and assign a role to p38 MAP kinase pathway in determining these events in K562 erythroleukemia cells. J. Cell. Biochem. 100: 1070–1079, 2007. © 2006 Wiley‐Liss, Inc.

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