Abstract
A 400-kDa transforming growth factor beta (TGF-beta) receptor was purified from plasma membranes of bovine liver using Triton X-100 extraction, wheat germ lectin-Sepharose 4B affinity chromatography, DEAE-cellulose anion exchange chromatography, and Sepharose CL-4B gel filtration chromatography. This procedure yielded approximately 20 micrograms of the receptor from 1 kg of bovine liver. During purification, the 400-kDa TGF-beta receptor was detected by a cross-linking assay in which the TGF-beta receptor-125I-TGF-beta complex was cross-linked by disuccinimidyl suberate, a bifunctional reagent, and analyzed by 5.5% sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by autoradiography. This novel 400-kDa TGF-beta receptor was also identified on cultured cells including cells reported to lack the type III receptor. The 400-kDa TGF-beta receptor, a nonproteoglycan glycoprotein, appears to be distinct from TGF-beta receptors (types I, II, III, and IV) previously identified on cultured cells and is designated as the type V receptor. The 400-kDa TGF-beta receptor as well as type I, II, and III receptors underwent internalization upon 125I-TGF-beta binding in mink lung epithelial cells.
Highlights
From the DeDartment of U3iochernistr-yand Molecular Biology and the §Departmentof Medicine, St
A 400-kDa transforming growth factor @ (TGF-8) sion in most cell types, the multiple biological functions of receptor was purified from plasma membranes of bo- TGF-/3 imply a physiological role for Transforminggrowthfactor P (TGF-P) inwound repair vine liver using Triton X - 1 0 0 extraction, wheat germ (4), tissue fibrosis (5), and morphogenesis (1-3)
Sized receptors for TGF-/3 have been identified in many cell types by cross-linking of ’2sI-labeled TGF-P (‘“I-TGF-P) to cells in the presence of bifunctional reagents (7)
Summary
From the DeDartment of U3iochernistr-yand Molecular Biology and the §Departmentof Medicine, St. This cross-linking assay appears to be specific and enabled us to detect the400-kDa receptor for TGF-P. After washing with 0.05 M NaCl inHEPES/Triton X-100 buffer, the columnwas of this purified TGF-P receptor was further verified by its close migration with bovine liver a2M receptor (440 kDa) on 5.5% SDS-polyacrylamide gel (data not shown).
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