Purification of the colony-stimulating factor 1 receptor and demonstration of its tyrosine kinase activity.
Colony-stimulating factor 1 (CSF-1) regulates the survival, proliferation, and differentiation of mononuclear phagocytes. The CSF-1 receptor was purified from cell membranes of the J774.2 mouse macrophage cell line by solubilization with Triton X-100, CSF-1 affinity chromatography, and gel filtration. The purified receptor is a protein or glycoprotein of 165 kDa comprising a single polypeptide chain that is not covalently associated, either as a homopolymer, or with any other protein. CSF-1 stimulated autophosphorylation of the purified receptor in tyrosine residues. Casein but not histone was shown to act as a substrate for the tyrosine protein kinase activity of purified receptor.
D000818:Animals; D002460:Cell Line; D003115:Colony-Stimulating Factors / Q000378:metabolism; D007700:Kinetics; D008264:Macrophages; D051379:Mice; D008970:Molecular Weight; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000302:isolation & purification / Q000378:metabolism*; D016184:Receptors, Colony-Stimulating Factor
D003115:Colony-Stimulating Factors; D011956:Receptors, Cell Surface; D016184:Receptors, Colony-Stimulating Factor; D011505:Protein-Tyrosine Kinases