Antagonists of activin signaling: mechanisms and potential biological applications
Activins are members of the transforming growth factor-β (TGF-β) superfamily that control many physiological processes such as cell proliferation and differentiation, immune responses, wound repair and various endocrine activities. Activins elicit these diverse biological responses by signaling via...
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| Published in | Trends in endocrinology and metabolism Vol. 16; no. 2; pp. 73 - 78 |
|---|---|
| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Elsevier Ltd
01.03.2005
Elsevier |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1043-2760 1879-3061 |
| DOI | 10.1016/j.tem.2005.01.003 |
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| Abstract | Activins are members of the transforming growth factor-β (TGF-β) superfamily that control many physiological processes such as cell proliferation and differentiation, immune responses, wound repair and various endocrine activities. Activins elicit these diverse biological responses by signaling via type I and type II receptor serine kinases. Recent studies have revealed details of the roles of inhibin, betaglycan, follistatin and its related protein follistatin-related gene (FLRG), Cripto and BAMBI in antagonizing activin action, and exogenous antagonists against the activin type I (SB-431542 and SB-505124) and type II (activin-M108A) receptors have been developed. Understanding how activin signaling is controlled extracellularly is the first step in providing treatment for wound healing and for disorders such as cachexia and cancer, which result from a deregulated activin pathway. |
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| AbstractList | Activins are members of the transforming growth factor-beta (TGF-beta) superfamily that control many physiological processes such as cell proliferation and differentiation, immune responses, wound repair and various endocrine activities. Activins elicit these diverse biological responses by signaling via type I and type II receptor serine kinases. Recent studies have revealed details of the roles of inhibin, betaglycan, follistatin and its related protein follistatin-related gene (FLRG), Cripto and BAMBI in antagonizing activin action, and exogenous antagonists against the activin type I (SB-431542 and SB-505124) and type II (activin-M108A) receptors have been developed. Understanding how activin signaling is controlled extracellularly is the first step in providing treatment for wound healing and for disorders such as cachexia and cancer, which result from a deregulated activin pathway. Activins are members of the transforming growth factor-β (TGF-β) superfamily that control many physiological processes such as cell proliferation and differentiation, immune responses, wound repair and various endocrine activities. Activins elicit these diverse biological responses by signaling via type I and type II receptor serine kinases. Recent studies have revealed details of the roles of inhibin, betaglycan, follistatin and its related protein follistatin-related gene (FLRG), Cripto and BAMBI in antagonizing activin action, and exogenous antagonists against the activin type I (SB-431542 and SB-505124) and type II (activin-M108A) receptors have been developed. Understanding how activin signaling is controlled extracellularly is the first step in providing treatment for wound healing and for disorders such as cachexia and cancer, which result from a deregulated activin pathway. Activins are members of the transforming growth factor-beta (TGF-beta) superfamily that control many physiological processes such as cell proliferation and differentiation, immune responses, wound repair and various endocrine activities. Activins elicit these diverse biological responses by signaling via type I and type II receptor serine kinases. Recent studies have revealed details of the roles of inhibin, betaglycan, follistatin and its related protein follistatin-related gene (FLRG), Cripto and BAMBI in antagonizing activin action, and exogenous antagonists against the activin type I (SB-431542 and SB-505124) and type II (activin-M108A) receptors have been developed. Understanding how activin signaling is controlled extracellularly is the first step in providing treatment for wound healing and for disorders such as cachexia and cancer, which result from a deregulated activin pathway.Activins are members of the transforming growth factor-beta (TGF-beta) superfamily that control many physiological processes such as cell proliferation and differentiation, immune responses, wound repair and various endocrine activities. Activins elicit these diverse biological responses by signaling via type I and type II receptor serine kinases. Recent studies have revealed details of the roles of inhibin, betaglycan, follistatin and its related protein follistatin-related gene (FLRG), Cripto and BAMBI in antagonizing activin action, and exogenous antagonists against the activin type I (SB-431542 and SB-505124) and type II (activin-M108A) receptors have been developed. Understanding how activin signaling is controlled extracellularly is the first step in providing treatment for wound healing and for disorders such as cachexia and cancer, which result from a deregulated activin pathway. |
| Author | Vale, Wylie W. Gray, Peter C. Harrison, Craig A. Robertson, David M. |
| Author_xml | – sequence: 1 givenname: Craig A. surname: Harrison fullname: Harrison, Craig A. email: craig.harrison@phimr.monash.edu.au organization: Prince Henry's Institute of Medical Research, 246 Clayton Road, Clayton, VIC 3168, Australia – sequence: 2 givenname: Peter C. surname: Gray fullname: Gray, Peter C. organization: Clayton Foundation Laboratories for Peptide Biology, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA – sequence: 3 givenname: Wylie W. surname: Vale fullname: Vale, Wylie W. organization: Clayton Foundation Laboratories for Peptide Biology, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA – sequence: 4 givenname: David M. surname: Robertson fullname: Robertson, David M. organization: Prince Henry's Institute of Medical Research, 246 Clayton Road, Clayton, VIC 3168, Australia |
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| Keywords | Signal transduction Endogenous Antagonist Review Activin Mechanism of action Biological receptor |
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| Snippet | Activins are members of the transforming growth factor-β (TGF-β) superfamily that control many physiological processes such as cell proliferation and... Activins are members of the transforming growth factor-beta (TGF-beta) superfamily that control many physiological processes such as cell proliferation and... |
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| SubjectTerms | Activins - antagonists & inhibitors Activins - metabolism Animals Apud cells. Peptide and protein hormones. Growth factors Biological and medical sciences Cachexia - therapy Fundamental and applied biological sciences. Psychology Hormone Antagonists - pharmacology Hormone Antagonists - therapeutic use Humans Neoplasms - therapy Signal Transduction Vertebrates: endocrinology Wound Healing - drug effects |
| Title | Antagonists of activin signaling: mechanisms and potential biological applications |
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