Open AccessModulation of Protein Tyrosine Phosphatase 1B by Erythropoietin in UT-7 Cell Line
Author(s) -
Mariana Alejandra Callero,
Gladys Pérez,
Daniela Vittori,
Nicolás Pregi,
Alcira Nesse
Publication year - 2007
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000107518
Subject(s) - protein tyrosine phosphatase , phosphorylation , tyrosine phosphorylation , erythropoietin receptor , signal transduction , microbiology and biotechnology , phosphatase , receptor tyrosine kinase , biology , janus kinase 2 , tyrosine kinase , erythropoietin , biochemistry , chemistry , endocrinology
Since the reversible phosphorylation of tyrosyl residues is a critical event in cellular signaling pathways activated by erythropoietin (Epo), attention has been focused on protein tyrosine phosphatases (PTPs) and their coordinated action with protein tyrosine kinases. The prototypic member of the PTP family is PTP1B, a widely expressed non-receptor PTP located both in cytosol and intracellular membranes via its hydrophobic C-terminal targeting sequence. PTP1B has been implicated in the regulation of signaling pathways involving tyrosine phosphorylation induced by growth factors, cytokines, and hormones, such as the downregulation of erythropoietin and insulin receptors. However, little is known about which factor modulates the activity of this enzyme.