| Literature DB >> 8242743 |
P Franzén1, P ten Dijke, H Ichijo, H Yamashita, P Schulz, C H Heldin, K Miyazono.
Abstract
A cDNA clone encoding a 53 kd serine/threonine kinase receptor with an overall structure similar to that of the type II receptor for transforming growth factor beta (TGF beta) was obtained. 125I-TGF beta 1 bound to porcine endothelial cells transfected with the cDNA and formed a cross-linked complex of 70 kd, characteristic of a TGF beta type I receptor. Immunoprecipitation of the cross-linked complexes by antibodies against the cloned receptor revealed the 70 kd complex as well as a 94 kd TGF beta type II receptor complex. The immunoprecipitated novel serine/threonine kinase receptor had biochemical properties of the TGF beta type I receptor and was observed in different cell types. Transfection of the cloned cDNA into TGF beta type I receptor-deficient cells restored TGF beta-induced plasminogen activator inhibitor 1 production. These results suggest that signal transduction by TGF beta involves the formation of a heteromeric complex of two different serine/threonine kinase receptors.Entities:
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Year: 1993 PMID： 8242743 DOI： 10.1016/0092-8674(93)90489-d
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582