Localization of transforming growth factor beta binding site in betaglycan. Comparison with small extracellular matrix proteoglycans.
作者： D Fukushima , R Bützow , A Hildebrand , E Ruoslahti
DOI: 10.1016/S0021-9258(18)41585-2
关键词:
摘要: The most abundant binding molecule for transforming growth factor beta (TGF-beta) on many cell types is betaglycan, a transmembrane proteoglycan. To localize the site TGF-beta in parts of betaglycan extracellular portion were expressed as recombinant fusion proteins bacteria and tested their ability to compete 1 Hep G2 cells. One fragment encompassing 226 residues near domain (amino acids 543-769) (Lopez-Casillas, F., Cheifetz, S., Doody, J., Andres, J. L., Lane, W. Massague, (1991) Cell 67, 785-795) was active, whereas representing other ectodomain inactive. Affinity measurements revealed two classes sites (Kd = 3.9 nM Kd 145 nM) active protein. protein immobilized inhibited by core small interstitial proteoglycans decorin, biglycan fibromodulin, each also known bind TGF-beta. effective concentrations these similar those required indicating affinities betaglycan. cross-linking showed that, at low concentrations, enhanced type II receptor endogenous but had no effect I receptor. At high all receptors. activity mink lung bioassay concentrations. results indicate that decorin same or closely spaced with one another binding. In addition, may cooperate
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