Inhibitory roles for SHP-1 and SOCS-3 following pituitary proopiomelanocortin induction by leukemia inhibitory factor

• Published in: The Journal of clinical investigation Vol. 104; no. 9; pp. 1277 - 1285
• Main Authors: Bousquet, Corinne, Susini, Christiane, Melmed, Shlomo
• Format: Journal Article
• Language: English
• Published: United States American Society for Clinical Investigation 01.11.1999
• Subjects: Animals; Catalysis; Cell Line; DNA-Binding Proteins - metabolism; Down-Regulation; Growth Inhibitors - pharmacology; Interleukin-6; Intracellular Signaling Peptides and Proteins; Janus Kinase 2; Leukemia Inhibitory Factor; Lymphokines - pharmacology; Mice; Models, Biological; Phosphorylation; Pituitary Gland - metabolism; Pro-Opiomelanocortin - metabolism; Protein Tyrosine Phosphatase, Non-Receptor Type 11; Protein Tyrosine Phosphatase, Non-Receptor Type 6; Protein Tyrosine Phosphatases - metabolism; Protein Tyrosine Phosphatases - physiology; Protein-Tyrosine Kinases - metabolism; Proteins - physiology; Proto-Oncogene Proteins; Repressor Proteins; SH2 Domain-Containing Protein Tyrosine Phosphatases; Signal Transduction; STAT3 Transcription Factor; Suppressor of Cytokine Signaling 3 Protein; Suppressor of Cytokine Signaling Proteins; Time Factors; Trans-Activators - metabolism; Transcription Factors; Transfection

Leukemia inhibitory factor (LIF) is a pleiotropic cytokine that stimulates the hypothalamo-pituitary-adrenal (HPA) axis through JAK-STAT activation. We show here that LIF-induced JAK2 and STAT3 tyrosine phosphorylation is transient, disappearing within 20 and 40 minutes, respectively. LIF activates...