Interleukin 1 alpha activates two forms of p54 alpha mitogen-activated protein kinase in rabbit liver.
Open Access
- 1 December 1994
- journal article
- Published by Rockefeller University Press in The Journal of Experimental Medicine
- Vol. 180 (6), 2017-2025
- https://doi.org/10.1084/jem.180.6.2017
Abstract
We have identified in rabbits two hepatic forms of T669 peptide kinases that are very strongly activated after systemic injection with the inflammatory cytokine interleukin 1 (IL-1). The T669 peptide contains a major phosphorylation site of the epidermal growth factor receptor, threonine 699 and is a substrate for mitogen-activated protein (MAP) kinases. The kinases were purified to homogeneity and corresponded to 50- and 55-kD proteins on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Amino acid sequencing of 12 tryptic peptides of both kinases identified them as p54 MAP kinase alpha. This kinase belongs to the novel family of stress-activated protein kinases. This is the first evidence of IL-1 activating a specific protein kinase in vivo.Keywords
This publication has 14 references indexed in Scilit:
- Interleukin-1 activates a novel protein kinase that phosphorylates the epidermal-growth-factor receptor peptide T669Biochemical Journal, 1994
- The mitogen-activated protein kinase signal transduction pathwayJournal of Biological Chemistry, 1993
- Interleukin 1 signaling occurs exclusively via the type I receptor.Proceedings of the National Academy of Sciences, 1993
- Accelerated high‐sensitivity microsequencing of proteins and peptides using a miniature reaction cartridgeProtein Science, 1992
- Interleukin-1 represents a new modality for the activation of extracellular signal-regulated kinases/microtubule-associated protein-2 kinases.Journal of Biological Chemistry, 1991
- Phosphorylation of c-jun mediated by MAP kinasesNature, 1991
- pp54 microtubule-associated protein 2 kinase. A novel serine/threonine protein kinase regulated by phosphorylation and stimulated by poly-L-lysine.Journal of Biological Chemistry, 1990
- The periodic association of MAP2 with brain microtubules in vitro.The Journal of cell biology, 1979
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970