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

doi:10.1016/j.bbrc.2014.09.055

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

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

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-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 language	English
Pages (from-to)	1084-1090
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	452
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2014.09.055
Publication status	Published - 2014 Oct 3

Bibliographical note

Funding Information:
This work was supported by the Grant from the National Research Foundation of Korea ( NRF-2011-0009555 ) to D.P. and by Inha University Research Grant and the Korea Healthcare Technology R&D Project ( A111927 ), Ministry of Health & Welfare to M.G.K. H.S.L., B.M.P., and Y.C. were the recipients of the BK21 fellowship. None of the authors of this work has financial interest related to this work.

Keywords

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

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/j.bbrc.2014.09.055

Cite this

@article{9da7510dcd244736a3c2063a951b0612,

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

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-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.",

keywords = "Ectodomain shedding, Epithin, TGF-β, Tumor necrosis factor-α converting enzyme (TACE)",

author = "Lee, {Hyo Seon} and Park, {Bo Mi} and Youngkyung Cho and Sauryang Kim and Chungho Kim and Kim, {Moon Gyo} and Dongeun Park",

note = "Funding Information: This work was supported by the Grant from the National Research Foundation of Korea ( NRF-2011-0009555 ) to D.P. and by Inha University Research Grant and the Korea Healthcare Technology R&D Project ( A111927 ), Ministry of Health & Welfare to M.G.K. H.S.L., B.M.P., and Y.C. were the recipients of the BK21 fellowship. None of the authors of this work has financial interest related to this work.",

year = "2014",

month = oct,

day = "3",

doi = "10.1016/j.bbrc.2014.09.055",

language = "English",

volume = "452",

pages = "1084--1090",

journal = "Biochemical and biophysical research communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "4",

}

TY - JOUR

T1 - Shedding of epithin/PRSS14 is induced by TGF-β and mediated by tumor necrosis factor-α converting enzyme

AU - Lee, Hyo Seon

AU - Park, Bo Mi

AU - Cho, Youngkyung

AU - Kim, Sauryang

AU - Kim, Chungho

AU - Kim, Moon Gyo

AU - Park, Dongeun

N1 - Funding Information: This work was supported by the Grant from the National Research Foundation of Korea ( NRF-2011-0009555 ) to D.P. and by Inha University Research Grant and the Korea Healthcare Technology R&D Project ( A111927 ), Ministry of Health & Welfare to M.G.K. H.S.L., B.M.P., and Y.C. were the recipients of the BK21 fellowship. None of the authors of this work has financial interest related to this work.

PY - 2014/10/3

Y1 - 2014/10/3

N2 - 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.

AB - 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.

KW - Ectodomain shedding

KW - Epithin

KW - TGF-β

KW - Tumor necrosis factor-α converting enzyme (TACE)

UR - http://www.scopus.com/inward/record.url?scp=84907898299&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2014.09.055

DO - 10.1016/j.bbrc.2014.09.055

M3 - Article

C2 - 25245289

AN - SCOPUS:84907898299

SN - 0006-291X

VL - 452

SP - 1084

EP - 1090

JO - Biochemical and biophysical research communications

JF - Biochemical and biophysical research communications

IS - 4

ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this