Expression of a thioredoxin-related protein-1 is induced by prostaglandin E2

Kye Young Kim, June Woo Lee, Minseon Park, Myeong Ho Jung, Gyoung A. Jeon, Myeong Jin Nam

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Prostaglandin E2 (PGE2) plays an important role in protection of the gastric mucosa against various damaging agents and growth-inhibitory activity on tumor cells. However, the precise regulation mechanism of PGE2 in gastric cancer cells is still unclear. In this study, we isolated a gene, which is regulated by PGE2 in SNU-1, human gastric adenocarcinoma cells, using differential display RT-PCR (DD RT-PCR) and characterized the function of the gene induced by PGE2. The full-length cDNA of the gene was cloned by the rapid amplification of cDNA ends method. The 1659 base pair cDNA consists of a 30-nt 5′-noncoding region, an 891-nt open reading frame and a 738-nt 3′noncoding region that includes a poly (A) signal. As a result of protein motif search, we found that it has a conserved thioredoxin-active site, Cys-Gly-Pro-Cys and a Myb-DNA binding domain repeat signature. Thus, we designated this gene product as thioredoxin-related protein-1, TRP-1. TRP-1 was expressed in a lower extent in renal, gastric and colon cancer tissues and is translated into 33 kDa protein in nuclear and cytoplasmic fractions. TRP-1 has a thioredoxin activity, which was detected using the insulin disulfide reduction assay. Another potential role of TRP-1 is repression of B-Myb activity through direct binding to B-Myb, a transcriptional factor induced at G1-S transition. Finally, TRP-1 overexpression inhibits mammalian cell proliferation and specifically predispose to G0/G1 phase arrest. In conclusion, these results imply that TRP-1 is a mammalian thioredoxin and plays as a transcriptional repressor through direct binding to the transcription factor B-Myb.

Original languageEnglish (US)
Pages (from-to)1670-1679
Number of pages10
JournalInternational Journal of Cancer
Volume118
Issue number7
DOIs
StatePublished - Apr 1 2006
Externally publishedYes

Fingerprint

Thioredoxins
Dinoprostone
Proteins
Complementary DNA
Genes
Stomach Neoplasms
Cell Cycle Resting Phase
Amino Acid Motifs
Poly A
Kidney Neoplasms
G1 Phase
Nuclear Proteins
Gastric Mucosa
Base Pairing
Disulfides
Colonic Neoplasms
Open Reading Frames
trophoblastin
Catalytic Domain
Stomach

Keywords

  • B-Myb
  • Prostaglandin E
  • Thioredoxin-related protein 1

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

Cite this

Expression of a thioredoxin-related protein-1 is induced by prostaglandin E2. / Kim, Kye Young; Lee, June Woo; Park, Minseon; Jung, Myeong Ho; Jeon, Gyoung A.; Nam, Myeong Jin.

In: International Journal of Cancer, Vol. 118, No. 7, 01.04.2006, p. 1670-1679.

Research output: Contribution to journalArticle

Kim, Kye Young ; Lee, June Woo ; Park, Minseon ; Jung, Myeong Ho ; Jeon, Gyoung A. ; Nam, Myeong Jin. / Expression of a thioredoxin-related protein-1 is induced by prostaglandin E2. In: International Journal of Cancer. 2006 ; Vol. 118, No. 7. pp. 1670-1679.
@article{a33cda9c22714e69bd1ee0fe79925656,
title = "Expression of a thioredoxin-related protein-1 is induced by prostaglandin E2",
abstract = "Prostaglandin E2 (PGE2) plays an important role in protection of the gastric mucosa against various damaging agents and growth-inhibitory activity on tumor cells. However, the precise regulation mechanism of PGE2 in gastric cancer cells is still unclear. In this study, we isolated a gene, which is regulated by PGE2 in SNU-1, human gastric adenocarcinoma cells, using differential display RT-PCR (DD RT-PCR) and characterized the function of the gene induced by PGE2. The full-length cDNA of the gene was cloned by the rapid amplification of cDNA ends method. The 1659 base pair cDNA consists of a 30-nt 5′-noncoding region, an 891-nt open reading frame and a 738-nt 3′noncoding region that includes a poly (A) signal. As a result of protein motif search, we found that it has a conserved thioredoxin-active site, Cys-Gly-Pro-Cys and a Myb-DNA binding domain repeat signature. Thus, we designated this gene product as thioredoxin-related protein-1, TRP-1. TRP-1 was expressed in a lower extent in renal, gastric and colon cancer tissues and is translated into 33 kDa protein in nuclear and cytoplasmic fractions. TRP-1 has a thioredoxin activity, which was detected using the insulin disulfide reduction assay. Another potential role of TRP-1 is repression of B-Myb activity through direct binding to B-Myb, a transcriptional factor induced at G1-S transition. Finally, TRP-1 overexpression inhibits mammalian cell proliferation and specifically predispose to G0/G1 phase arrest. In conclusion, these results imply that TRP-1 is a mammalian thioredoxin and plays as a transcriptional repressor through direct binding to the transcription factor B-Myb.",
keywords = "B-Myb, Prostaglandin E, Thioredoxin-related protein 1",
author = "Kim, {Kye Young} and Lee, {June Woo} and Minseon Park and Jung, {Myeong Ho} and Jeon, {Gyoung A.} and Nam, {Myeong Jin}",
year = "2006",
month = "4",
day = "1",
doi = "10.1002/ijc.21572",
language = "English (US)",
volume = "118",
pages = "1670--1679",
journal = "International Journal of Cancer",
issn = "0020-7136",
publisher = "Wiley-Liss Inc.",
number = "7",

}

TY - JOUR

T1 - Expression of a thioredoxin-related protein-1 is induced by prostaglandin E2

AU - Kim, Kye Young

AU - Lee, June Woo

AU - Park, Minseon

AU - Jung, Myeong Ho

AU - Jeon, Gyoung A.

AU - Nam, Myeong Jin

PY - 2006/4/1

Y1 - 2006/4/1

N2 - Prostaglandin E2 (PGE2) plays an important role in protection of the gastric mucosa against various damaging agents and growth-inhibitory activity on tumor cells. However, the precise regulation mechanism of PGE2 in gastric cancer cells is still unclear. In this study, we isolated a gene, which is regulated by PGE2 in SNU-1, human gastric adenocarcinoma cells, using differential display RT-PCR (DD RT-PCR) and characterized the function of the gene induced by PGE2. The full-length cDNA of the gene was cloned by the rapid amplification of cDNA ends method. The 1659 base pair cDNA consists of a 30-nt 5′-noncoding region, an 891-nt open reading frame and a 738-nt 3′noncoding region that includes a poly (A) signal. As a result of protein motif search, we found that it has a conserved thioredoxin-active site, Cys-Gly-Pro-Cys and a Myb-DNA binding domain repeat signature. Thus, we designated this gene product as thioredoxin-related protein-1, TRP-1. TRP-1 was expressed in a lower extent in renal, gastric and colon cancer tissues and is translated into 33 kDa protein in nuclear and cytoplasmic fractions. TRP-1 has a thioredoxin activity, which was detected using the insulin disulfide reduction assay. Another potential role of TRP-1 is repression of B-Myb activity through direct binding to B-Myb, a transcriptional factor induced at G1-S transition. Finally, TRP-1 overexpression inhibits mammalian cell proliferation and specifically predispose to G0/G1 phase arrest. In conclusion, these results imply that TRP-1 is a mammalian thioredoxin and plays as a transcriptional repressor through direct binding to the transcription factor B-Myb.

AB - Prostaglandin E2 (PGE2) plays an important role in protection of the gastric mucosa against various damaging agents and growth-inhibitory activity on tumor cells. However, the precise regulation mechanism of PGE2 in gastric cancer cells is still unclear. In this study, we isolated a gene, which is regulated by PGE2 in SNU-1, human gastric adenocarcinoma cells, using differential display RT-PCR (DD RT-PCR) and characterized the function of the gene induced by PGE2. The full-length cDNA of the gene was cloned by the rapid amplification of cDNA ends method. The 1659 base pair cDNA consists of a 30-nt 5′-noncoding region, an 891-nt open reading frame and a 738-nt 3′noncoding region that includes a poly (A) signal. As a result of protein motif search, we found that it has a conserved thioredoxin-active site, Cys-Gly-Pro-Cys and a Myb-DNA binding domain repeat signature. Thus, we designated this gene product as thioredoxin-related protein-1, TRP-1. TRP-1 was expressed in a lower extent in renal, gastric and colon cancer tissues and is translated into 33 kDa protein in nuclear and cytoplasmic fractions. TRP-1 has a thioredoxin activity, which was detected using the insulin disulfide reduction assay. Another potential role of TRP-1 is repression of B-Myb activity through direct binding to B-Myb, a transcriptional factor induced at G1-S transition. Finally, TRP-1 overexpression inhibits mammalian cell proliferation and specifically predispose to G0/G1 phase arrest. In conclusion, these results imply that TRP-1 is a mammalian thioredoxin and plays as a transcriptional repressor through direct binding to the transcription factor B-Myb.

KW - B-Myb

KW - Prostaglandin E

KW - Thioredoxin-related protein 1

UR - http://www.scopus.com/inward/record.url?scp=33644852674&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33644852674&partnerID=8YFLogxK

U2 - 10.1002/ijc.21572

DO - 10.1002/ijc.21572

M3 - Article

C2 - 16231315

AN - SCOPUS:33644852674

VL - 118

SP - 1670

EP - 1679

JO - International Journal of Cancer

JF - International Journal of Cancer

SN - 0020-7136

IS - 7

ER -