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J. Biol. Chem., Vol. 260, Issue 5, 2636-2645, 03, 1985
J Massague and B Like
Type beta transforming growth factor (beta TGF) purified from human
platelets to homogeneity as judged by NH2-terminal amino acid sequence
analysis has been labeled with 125I to characterize its interaction with
cellular receptors. Binding of 125I-beta TGF to target cells is
temperature- and time-dependent, specific, saturable, and reversible. About
1.6-1.9 X 10(4) binding sites/cell with high affinity for beta TGF (Kd =
5.6-7.8 X 10(-11) M and 9.1-14 X 10(-11) M, respectively) are found in
NRK-49F and BALB/c 3T3 cells. beta TGF receptors do not appear to undergo
acute down-regulation by the ligand. Specific binding of 125I-beta TGF has
been observed in several human, rat, and mouse fibroblast lines and in
some, but not all, tumor-derived cell lines examined. 125I-beta TGF has
been cross-linked to intact cells and isolated membrane preparations using
disuccinimidyl suberate. Cells and isolated membranes from human, rat, and
mouse origin affinity labeled with 125I-beta TGF exhibit a major labeled
species of approximately 280 kilodaltons that has the properties of high
affinity and specificity expected from a physiologically relevant beta TGF
receptor. Minor labeled species of 70-90 kilodaltons are also labeled by
125I-beta TGF, but they correspond to molecular species with low apparent
affinity (Kd approximately 10(-8) M) for 125I-beta TGF.
Cellular receptors for type beta transforming growth factor. Ligand binding and affinity labeling in human and rodent cell lines
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