Involvement of the p38 mitogen-activated protein kinase pathway in tissue inhibitor of metalloproteinases-1-induced erythroid differentiation |
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Authors: | Petitfrère E Kadri Z Boudot C Sowa M L Mayeux P Haye B Billat C |
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Affiliation: | Laboratoire de Biochimie, CNRS FRE-2260, IFR53 Biomolécules, UFR Sciences Exactes et Naturelles, Université de Reims Champagne-Ardenne, Reims, France. emmanuelle.petitfrere@univ-reims.fr |
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Abstract: | We examined the role of the mitogen-activated protein (MAP) kinase pathway in tissue inhibitor of metalloproteinases-1 (TIMP-1)-mediated cellular effects in a human erythroleukemic cell line UT-7. We show that TIMP-1 induced both UT-7 cell erythroid differentiation and proliferation and tyrosine phosphorylation of many intracellular proteins. Using a panel of phosphospecific antibodies, we also demonstrate that phosphorylation of the p38 and c-Jun N-terminal kinases is increased by TIMP-1 whereas phosphorylation of extracellular signal-regulated kinase 1/2 is not induced. Moreover, inhibition of the p38 activity by SB203580 significantly reduces erythroid differentiation induced by TIMP-1, suggesting that the p38 MAP kinase pathway is involved in TIMP-1-induced erythroid differentiation. |
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