| pubmed-article:7790373 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7790373 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:7790373 | lifeskim:mentions | umls-concept:C0083867 | lld:lifeskim |
| pubmed-article:7790373 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:7790373 | lifeskim:mentions | umls-concept:C0050668 | lld:lifeskim |
| pubmed-article:7790373 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:7790373 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:7790373 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:7790373 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7790373 | pubmed:dateCreated | 1995-7-27 | lld:pubmed |
| pubmed-article:7790373 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:7790373 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7790373 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7790373 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7790373 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7790373 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7790373 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:7790373 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:7790373 | pubmed:author | pubmed-author:YamashitaHH | lld:pubmed |
| pubmed-article:7790373 | pubmed:author | pubmed-author:SmithJ CJC | lld:pubmed |
| pubmed-article:7790373 | pubmed:author | pubmed-author:HuylebroeckDD | lld:pubmed |
