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• W1561987129 abstract "Previous studies from our laboratory[Philip, A. & O’Connor-McCourt, M. D. (1991) J. Biol. Chem.266, 22290--22296] have shown that the lung exhibited the highest uptake of circulating [125I]-transforming growth factor-β1 (TGF-β1) on a per gram basis. This observation, together with the lack of information on TGF-β receptor expression in the lung, prompted us to attempt to characterize TGF-β receptors in this tissue. In the present report we show that the type III TGF-β receptor is the most abundant TGF-β binding protein in rat lung membranes and that it exhibits a 10-fold higher affinity for TGF-β2 than for TGF-β1. We observed that the majority of the type III receptor population in lung membranes is cleaved at a site in the central portion of the ectodomain, the resulting two fragments (95 kDa and 58 kDa) being held together by disulfide bonds. Furthermore, we demonstrate that a soluble form of the ectodomain of the type III receptor is shed from rat lung membranes in an efficient manner, with protease cleavage occurring at a site close to the transmembrane domain. This shedding is controllable by temperature, thus providing a system to study the mechanism of ectodomain release. Using this system, we show that the shedding is inhibited by prior ligand binding and by membrane solubilization. The identification of a membrane preparation which exhibits controllable and quantitative release of the type III receptor ectodomain provides a unique cell-free system for further studies of the mechanism of shedding of the type III TGF-β receptor ectodomain." @default.
• W1561987129 created "2016-06-24" @default.
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• W1561987129 date "1999-05-01" @default.
• W1561987129 modified "2023-10-18" @default.
• W1561987129 title "Ectodomain cleavage and shedding of the type III transforming growth factor-β receptor in lung membranes" @default.
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• W1561987129 doi "https://doi.org/10.1046/j.1432-1327.1999.00298.x" @default.
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