Shedding of epithin/PRSS14 is induced by TGF-β and mediated by tumor necrosis factor-α converting enzyme

Hyo Seon Lee, Bo Mi Park, Youngkyung Cho, Sauryang Kim, Chungho Kim, Moon Gyo Kim, Dongeun Park

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


Epithin/PRSS14, a type II transmembrane serine protease, plays critical roles in cancer metastasis. Previously, we have reported that epithin/PRSS14 undergoes ectodomain shedding in response to phorbol myristate acetate (PMA) stimulation. In this study, we show that transforming growth factor-β (TGF-β) induces rapid epithin/PRSS14 shedding through receptor mediated pathway in 427.1.86 thymoma cells. Tumor necrosis factor-α converting enzyme (TACE) is responsible for this shedding. Amino acid sequence encompassing the putative shedding cleavage site of epithin/PRSS14 exhibit strong homology to the cleavage site of l-selectin, a known TACE substrate. TACE inhibitor, TAPI-0 and TACE siRNA greatly reduced TGF-β-induced epithin/PRSS14 shedding. TGF-β treatment induces translocation of intracellular pool of TACE to the membrane where epithin/PRSS14 resides. These findings suggest that TGF-β induces epithin/PRSS14 shedding by mediating translocation of epithin/PRSS14 sheddase, TACE, to the membrane.

Original languageEnglish
Pages (from-to)1084-1090
Number of pages7
JournalBiochemical and biophysical research communications
Issue number4
Publication statusPublished - 2014 Oct 3


  • Ectodomain shedding
  • Epithin
  • TGF-β
  • Tumor necrosis factor-α converting enzyme (TACE)

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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