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• W2028573778 endingPage "311" @default.
• W2028573778 startingPage "304" @default.
• W2028573778 abstract "The cell-surface form of human macrophage colony-stimulating factor (CSF-1(256), M-CSFalpha) is a plasma membrane-anchored transmembrane protein from which the soluble CSF-1 is released by ectodomain proteolytic cleavage. We have previously generated two forms of cell surface CSF-1 which failed to undergo the cleavage by deleting residues 161-165 or residues 159-165 in the extracellular juxtamembrane region (1). To determine the biologic significance of the ectodomain cleavage, we compared the biosynthesis and biologic activities of uncleavable mutant CSF-1 forms with those of the cleavable wild-type (WT) CSF-1. We found that the uncleavable CSF-1 forms were able to accumulate on cell surface at about threefold higher level than the cleavable WT CSF-1 did. We further demonstrated that the uncleavable plasma membrane-anchored forms of CSF-1 were biologically active in mediating the proliferation of CSF-1-dependent cells as well as the intercellular adhesion between CSF-1 receptor-bearing cells and CSF-1 expressing cells. Furthermore, the adhesive activity of uncleavable CSF-1 forms was about twofold stronger than that of WT CSF-1, which indicated that the ectodomain cleavage system plays an important role in regulating the biologic activities of membrane-anchored CSF-1." @default.
• W2028573778 created "2016-06-24" @default.
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• W2028573778 date "2000-09-01" @default.
• W2028573778 modified "2023-10-15" @default.
• W2028573778 title "Biological Characterization of Uncleavable Plasma Membrane-Anchored Human Macrophage Colony-Stimulating Factor" @default.
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• W2028573778 doi "https://doi.org/10.1006/bbrc.2000.3423" @default.
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