Cleavage of membrane-anchored growth factors involves distinct protease activities regulated through common mechanisms.
The membrane-anchored forms of transforming growth factor-alpha (TGF-alpha) and stem cell growth factors ( Kit ligands) KL-1 and KL-2 are converted to soluble growth factor forms by a regulated proteolytic cleavage process. Each of these proteins is cleaved at a distinct site, however their cleavage is activated via a common set of intracellular signaling mechanisms. By using a panel of protease inhibitors, we show here that at least two cell-associated serine protease activities with distinct specificities participate in membrane growth factor cleavage. Two serine protease inhibitors of broad specificity, diisopropylfluorophosphate and 3,4-dichloroisocoumarin, prevent the cleavage of proTGF-alpha and KL-1 but not that of KL-2. Of the agents tested, N-tosyl-L-phenylalanine chloromethyl ketone and various haloenol lactone derivatives are the most potent inhibitors of cleavage of all three membrane growth factors. It is concluded that cleavage of membrane-anchored growth factors involves a proteolytic system with multiple serine protease activities regulated through common mechanisms.[1]References
- Cleavage of membrane-anchored growth factors involves distinct protease activities regulated through common mechanisms. Pandiella, A., Bosenberg, M.W., Huang, E.J., Besmer, P., Massagué, J. J. Biol. Chem. (1992) [Pubmed]
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