Protein tyrosine phosphatase 1b (PTP1B) is involved in the defective erythropoietic function of carbamylated erythropoietin

CHAMORRO MARÍA EUGENIA; MALTANERI ROMINA EUGENIA; VITTORI DANIELA; NESSE, ALCIRA

INTERNATIONAL JOURNAL OF BIOCHEMISTRY AND CELLULAR BIOLOGY

PERGAMON-ELSEVIER SCIENCE LTD

Lugar: Amsterdam; Año: 2015 vol. 61 p. 63 - 71

1357-2725

IntroductionIt is now recognized that the carbamylation of erythropoietin(Epo) in lysine residues makes this protein unable to act as a growthfactor for erythropoiesis, while it retains its ability to protect neu-ronal cells from damage. In accordance with other authors (Brineset al., 2004; Leist et al., 2004; Coleman et al., 2006; Fantacci et al.,2006), we demonstrated that Epo and cEpo exerted similar pro-tective effects on neuroblastoma-derived SH-SY5Y cells induced toapoptosis by staurosporine or TNF-, while cEpo was unable to sup-port proliferation of the UT-7 and TF-1 cell lines, both capable oferythroid differentiation (Chamorro et al., 2013). Furthermore, inthis previous paper we presented an advance on the study of thedifferential effects between Epo and cEpo on hematopoietic andnon-hematopoietic cells, since we reported the inability of cEpo tocompletely activate cell proliferation signaling pathways