Shedding of epithin/PRSS14 is induced by TGF-beta and mediated by tumor necrosis factor-alpha converting enzyme
- Authors
- Lee, Hyo Seon; Park, Bo Mi; Cho, Youngkyung; Kim, Sauryang; Kim, Chungho; Kim, Moon Gyo; Park, Dongeun
- Issue Date
- 3-10월-2014
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Epithin; Ectodomain shedding; TGF-beta; Tumor necrosis factor-alpha converting enzyme (TACE)
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.452, no.4, pp.1084 - 1090
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 452
- Number
- 4
- Start Page
- 1084
- End Page
- 1090
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/97117
- DOI
- 10.1016/j.bbrc.2014.09.055
- ISSN
- 0006-291X
- Abstract
- 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-beta (TGF-beta) induces rapid epithin/PRSS14 shedding through receptor mediated pathway in 427.1.86 thymoma cells. Tumor necrosis factor-a 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-beta-induced epithin/PRSS14 shedding. TGF-beta treatment induces translocation of intracellular pool of TACE to the membrane where epithin/PRSS14 resides. These findings suggest that TGF-beta induces epithin/PRSS14 shedding by mediating translocation of epithin/PRSS14 sheddase, TACE, to the membrane. (C) 2014 Elsevier Inc. All rights reserved.
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