University Library
  • Login
A gateway to Melbourne's research publications
Minerva Access is the University's Institutional Repository. It aims to collect, preserve, and showcase the intellectual output of staff and students of the University of Melbourne for a global audience.
View Item 
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Melbourne Medical School
  • Microbiology & Immunology
  • Microbiology & Immunology - Research Publications
  • View Item
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Melbourne Medical School
  • Microbiology & Immunology
  • Microbiology & Immunology - Research Publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

    THE REGULATION AND FUNCTIONS OF ACTIVIN AND FOLLISTATIN IN INFLAMMATION AND IMMUNITY

    Thumbnail
    Citations
    Scopus
    Web of Science
    Altmetric
    111
    102
    Author
    Hedger, MP; Winnall, WR; Phillips, DJ; de Kretser, DM
    Editor
    Litwack, G
    Date
    2011-01-01
    Source Title
    ACTIVINS AND INHIBINS
    Publisher
    ELSEVIER ACADEMIC PRESS INC
    University of Melbourne Author/s
    WINNALL, WENDY
    Affiliation
    Microbiology And Immunology
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Hedger, M. P., Winnall, W. R., Phillips, D. J. & de Kretser, D. M. (2011). THE REGULATION AND FUNCTIONS OF ACTIVIN AND FOLLISTATIN IN INFLAMMATION AND IMMUNITY. ACTIVINS AND INHIBINS, 85, pp.255-297. https://doi.org/10.1016/B978-0-12-385961-7.00013-5.
    Access Status
    This item is currently not available from this repository
    URI
    http://hdl.handle.net/11343/28990
    DOI
    10.1016/B978-0-12-385961-7.00013-5
    Description

    C1 - Journal Articles Refereed

    Abstract
    The activins are members of the transforming growth factor β superfamily with broad and complex effects on cell growth and differentiation. Activin A has long been known to be a critical regulator of inflammation and immunity, and similar roles are now emerging for activin B, with which it shares 65% sequence homology. These molecules and their binding protein, follistatin, are widely expressed, and their production is increased in many acute and chronic inflammatory conditions. Synthesis and release of the activins are stimulated by inflammatory cytokines, Toll-like receptor ligands, and oxidative stress. The activins interact with heterodimeric serine/threonine kinase receptor complexes to activate SMAD transcription factors and the MAP kinase signaling pathways, which mediate inflammation, stress, and immunity. Follistatin binds to the activins with high affinity, thereby obstructing the activin receptor binding site, and targets them to cell surface proteoglycans and lysosomal degradation. Studies on transgenic mice and those with gene knockouts, together with blocking studies using exogenous follistatin, have established that activin A plays critical roles in the onset of cachexia, acute and chronic inflammatory responses such as septicemia, colitis and asthma, and fibrosis. However, activin A also directs the development of monocyte/macrophages, myeloid dendritic cells, and T cell subsets to promote type 2 and regulatory immune responses. The ability of both endogenous and exogenous follistatin to block the proinflammatory and profibrotic actions of activin A has led to interest in this binding protein as a potential therapeutic for limiting the severity of disease and to improve subsequent damage associated with inflammation and fibrosis. However, the ability of activin A to sculpt the subsequent immune response as well means that the full range of effects that might arise from blocking activin bioactivity will need to be considered in any therapeutic applications.
    Keywords
    Endocrinology; Innate Immunity; Reproduction; Endocrine Organs and Diseases (excl. Diabetes); Immune System and Allergy; Reproductive System and Disorders

    Export Reference in RIS Format     

    Endnote

    • Click on "Export Reference in RIS Format" and choose "open with... Endnote".

    Refworks

    • Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References


    Collections
    • Minerva Elements Records [45770]
    • Microbiology & Immunology - Research Publications [1555]
    Minerva AccessDepositing Your Work (for University of Melbourne Staff and Students)NewsFAQs

    BrowseCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects
    My AccountLoginRegister
    StatisticsMost Popular ItemsStatistics by CountryMost Popular Authors