Osteogenic protein-1 binds to activin type II receptors and induces certain activin-like effects
| Autor: | Hidetoshi Yamashita, Kohei Miyazono, T. K. Sampath, C H Heldin, Danny Huylebroeck, James C. Smith, P. ten Dijke, M Andries |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1995 |
| Předmět: |
medicine.medical_specialty
Follistatin animal structures Activin Receptors Bone Morphogenetic Protein 7 ACVR1 In Vitro Techniques Xenopus Proteins Mesoderm Pituitary Gland Anterior Transforming Growth Factor beta Internal medicine TGF beta signaling pathway Chlorocebus aethiops medicine Animals Erythropoiesis Inhibins Receptors Growth Factor Receptor Activin type 2 receptors Cells Cultured Glycoproteins Embryonic Induction biology Proteins Cell Biology Activin receptor Transforming growth factor beta Articles Growth Inhibitors Recombinant Proteins Cell biology Activins Endocrinology Mink embryonic structures Bone Morphogenetic Proteins biology.protein Follicle Stimulating Hormone ACVR2B hormones hormone substitutes and hormone antagonists Protein Binding Signal Transduction |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | Proteins in the TGF-beta superfamily transduce their effects through binding to type I and type II serine/threonine kinase receptors. Osteogenic protein-1 (OP-1, also known as bone morphogenetic protein-7 or BMP-7), a member of the TGF-beta superfamily which belongs to the BMP subfamily, was found to bind activin receptor type I (ActR-I), and BMP receptors type IA (BMPR-IA) and type IB (BMPR-IB) in the presence of activin receptors type II (ActR-II) and type IIB (ActR-IIB). The binding affinity of OP-1 to ActR-II was two- to threefold lower than that of activin A. A transcriptional activation signal was transduced after binding of OP-1 to the complex of ActR-I and ActR-II, or that of BMPR-IB and ActR-II. These results indicate that ActR-II can act as a functional type II receptor for OP-1, as well as for activins. Some of the known biological effects of activin were observed for OP-1, including growth inhibition and erythroid differentiation induction. Compared to activin, OP-1 was shown to be a poor inducer of mesoderm in Xenopus embryos. Moreover, follistatin, an inhibitor of activins, was found to inhibit the effects of OP-1, if added at a 10-fold excess. However, certain effects of activin, like induction of follicle stimulating hormone secretion in rat pituitary cells were not observed for OP-1. OP-1 has overlapping binding specificities with activins, and shares certain but not all of the functional effects of activins. Thus, OP-1 may have broader effects in vivo than hitherto recognized. |
| Databáze: | OpenAIRE |
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