The activin binding proteins follistatin and follistatin-related protein are differentially regulated in vitro and during cutaneous wound repair

in Journal of Endocrinology
Authors:
M Wankell
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S Kaesler
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YQ Zhang
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C Florence
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S Werner
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R Duan
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DOI:
https://doi.org/10.1677/joe.0.1710385
Volume/Issue:
Volume 171: Issue 3
Article Type:
Other
Page Range:
385–395
Online Publication Date:
01 Dec 2001
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Follistatin is a secreted protein that binds activin in vitro and in vivo and thereby inhibits its biological functions. Recently, related human and murine genes, designated follistatin-related gene (FLRG), were identified, and their products were shown to bind activin with high affinity. In this study we further characterized the murine FLRG protein, and we analyzed its tissue-specific expression and regulation in comparison with those of follistatin. Transient expression of the mouse FLRG protein in COS-1 cells revealed that the FLRG cDNA encodes a secreted glycoprotein. FLRG mRNA was expressed at high levels in the lung, the testis, the uterus and, particularly, the skin. Immunohistochemistry revealed the presence of FLRG in the basement membrane between the dermis and the epidermis and around blood vessels. FLRG mRNA expression was induced in keratinocytes by keratinocyte growth factor, epidermal growth factor and transforming growth factor-beta 1, and in fibroblasts by platelet-derived growth factor and epidermal growth factor. The induction was more rapid, but weaker, than that of follistatin. Most interestingly, both follistatin and FLRG were expressed during the wound healing process, but their distribution within the wound was different. The different expression pattern of FLRG and follistatin and their differential regulation suggest different functions of these activin-binding proteins in vivo.

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Print ISSN:
0022-0795
Online ISSN:
1479-6805
Page(s):
11
Article Type:
Other
Print Publication Date:
01 Dec 2001
Online Publication Date:
01 Dec 2001