A surface component on GH3 pituitary cells that recognizes transforming growth factor-beta, activin, and inhibin.
作者： S Cheifetz , N Ling , R Guillemin , J Massagué
DOI: 10.1016/S0021-9258(19)77820-X
关键词:
摘要: Abstract We have examined the ability of various forms activin and inhibin, which are structurally related to transforming growth factor-beta (TGF-beta), interact with types cell surface TGF-beta binding sites. Activin AB, inhibin A, B were unable compete 125I-TGF-beta 1 for receptor I, II, or III that coexist in human skin fibroblasts, rat liver epithelial cells, mink lung cells. In contrast, activins inhibins effectively competed GH3 pituitary tumor Binding cells was mediated by about 2700 sites/cell a Kd = 90 pM. Affinity labeling these sites cross-linking yielded 70-74-kDa labeled complexes distinct from previously identified components. Labeling components inhibited 1, 2, at concentrations high picomolar low nanomolar range, but it not significantly affected other polypeptide hormones factors tested. The represent novel type protein is unique its recognize members family bioactive polypeptides.
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