Abstract
The interference of low-molecular-weight phosphotyrosine protein phosphatase with the macrophage response to macrophage colony-stimulating factor was investigated. This paper shows that this phosphatase, already known to be involved in platelet-derived growth factor receptor signaling, is physiologically expressed in murine macrophages and dephosphorylates in vitro macrophage colony-stimulating factor receptor molecules immunoprecipitated from macrophage colony-stimulating factor-stimulated macrophages. We obtained the first demonstration that a phosphotyrosine-specific protein phosphatase dephosphorylates the macrophage colony-stimulating factor receptor in vivo and reduces the mitogenic response to macrophage colony-stimulating factor. The data indicate that low-molecular-weight phosphotyrosine protein phosphatase is a negative regulator of macrophage colony-stimulating factor receptor signaling.
Copyright 1998 Academic Press.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
3T3 Cells
-
Animals
-
Cell Count
-
Cell Line
-
DNA / metabolism
-
Humans
-
Macrophage Colony-Stimulating Factor / physiology*
-
Macrophages / cytology
-
Macrophages / enzymology
-
Macrophages / metabolism
-
Mice
-
Mitogens / antagonists & inhibitors
-
Mitogens / physiology*
-
Molecular Weight
-
Phosphorylation / drug effects
-
Protein Tyrosine Phosphatases / biosynthesis*
-
Protein Tyrosine Phosphatases / physiology
-
Receptor, Macrophage Colony-Stimulating Factor / antagonists & inhibitors
-
Receptor, Macrophage Colony-Stimulating Factor / metabolism*
-
Receptor, Macrophage Colony-Stimulating Factor / physiology*
-
Signal Transduction / drug effects
-
Thymidine / metabolism
-
Transfection
-
Tritium / metabolism
-
Tyrosine / antagonists & inhibitors
-
Tyrosine / metabolism*
Substances
-
Mitogens
-
Tritium
-
Tyrosine
-
Macrophage Colony-Stimulating Factor
-
DNA
-
Receptor, Macrophage Colony-Stimulating Factor
-
Protein Tyrosine Phosphatases
-
Thymidine