Differential tyrosyl-phosphorylation of multiple mitogen-activated protein kinase isoforms in response to prolactin in Nb2 lymphoma cells

Proceedings of the Society for Experimental Biology and Medicine
I G CamarilloJ A Rillema

Abstract

Prolactin (PRL) stimulates mitogenesis and differentiative processes in a variety of cell types. Not all of the molecules involved in PRL signaling, which follows an initial PRL-receptor interaction, have been identified. In the present studies, PRL is shown to stimulate the differential tyrosyl phosphorylation of three isoforms (ERK-1, 2, and 4) of mitogen-activated protein kinases (MAP kinase) in a rat pre-T lymphoma cell line (Nb2). Evidence also suggests that PRL stimulates the tyrosyl phosphorylation of ERK-3, a MAP kinase isoform recently identified. When G1-arrested Nb2 cells are treated with 50 ng/ml oPRL, ERK-1 through 3 become tyrosyl phosphorylated within minutes (an indication of enzyme activation) and then become dephosphorylated within 30 min. Conversely, ERK-4 is rapidly tyrosyl phosphorylated by 5 min, and remains in this state for at least 1 hr.

Citations

Feb 25, 2000·Molecular and Cellular Endocrinology·O GoupilleJ Djiane
Dec 7, 2007·Endocrine Reviews·Nira Ben-JonathanElizabeth W LaPensee
Nov 30, 2000·Biochemical and Biophysical Research Communications·S J KimM S Kim
Oct 24, 2001·Biology of Reproduction·C A GrayT E Spencer
Jan 20, 2001·The Journal of Biological Chemistry·J ZimmermannP Furst

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