Dermatopontin interacts with transforming growth factor β and enhances its biological activity

Osamu Okamoto, Sakuhei Fujiwara, Mayumi Abe, Yasufumi Sato

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109 Citations (Scopus)


Dermatopontin, a recently found low-molecular-mass component of the extracellular matrix, was studied for its interaction with decorin and transforming growth factor β (TGF-β) and its influence on TGF-β bioactivity. Dermatopontin reacted with decorin with an apparent K(d) of 100 nM in a solid-phase assay. Dermatopontin inhibited the formation of the decorin-TGF-β1 complex. Decorin also competed with dermatopontin for the binding of this cytokine. The dermatopontin-decorin complex bound 3-fold more TGF-β1 than did each component individually, and binding was inhibited more strongly by decorin preincubated with dermatopontin than by dermatopontin or decorin alone. Dermatopontin augmented the biological activity of TGF-β1, as analysed by the expression of luciferase in mink lung epithelial cells transfected with a plasminogen activator inhibitor-promoter-luciferase construct, although dermatopontin itself did not show apparent induction of luciferase. Dermatopontin showed weak inhibitory activity on the proliferation of mink lung epithelial cells, and it enhanced the growth-inhibitory activity of TGF-β on these cells. Thus dermatopontin increases the cellular response to TGF-β. These findings strongly suggest that dermatopontin modifies the behaviour of TGF-β through interaction with decorin in the microenvironment of the extracellular matrix in vivo.

Original languageEnglish
Pages (from-to)537-541
Number of pages5
JournalBiochemical Journal
Issue number3
Publication statusPublished - 1999 Feb 1


  • Cytokines
  • Decorin
  • Dermatopontin


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