Abstract：
:Follistatin (FS) is well characterized as an activin-binding protein. Recently, a novel follistatin-like protein called follistatin-related gene (FLRG) that has a similar domain organization to that of follistatin has been identified. Like follistatins, FLRG binds activins and bone morphogenetic proteins (BMPs). To study the regulation of FLRG expression, we have analyzed the genomic organization and promoter of the mouse FLRG gene. The mouse FLRG gene consists of five exons, and each encodes discrete functional regions. The overall genomic structure of FLRG is similar to that of FS except that the FLRG gene is missing one exon that codes a third FS domain found in FS. The promoter that covers 2.5 kbp and is linked to a luciferase reporter construct is active in human cervical carcinoma HeLa cells as well as in human embryonic kidney (HEK293) cells. Deletion analysis of the promoter regions indicates that a proximal 550 base pairs are enough for basal FLRG promoter activity in the cell lines. FLRG promoter activity is significantly augmented by phorbol 12-myristate 13-acetate (PMA) treatment, but not by cAMP stimulation. By contrast, FS promoter is activatable either by cAMP or PMA. Thus, although FS and FLRG are structurally and functionally related, their modes of regulation by external stimuli are different.
journal_name
Mol Cell Endocrinoljournal_title
Molecular and cellular endocrinologyauthors
Nakatani M,Yamakawa N,Matsuzaki T,Shimasaki S,Sugino H,Tsuchida Kdoi
10.1016/s0303-7207(01)00734-1keywords:
subject
Has Abstractpub_date
2002-03-28 00:00:00pages
117-23issue
1-2eissn
0303-7207issn
1872-8057pii
S0303720701007341journal_volume
189pub_type
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pub_type： 杂志文章,评审
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journal_title：Molecular and cellular endocrinology
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pub_type： 杂志文章,评审
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pub_type： 杂志文章
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