TY - JOUR
T1 - Dipeptidyl peptidase IV expression in endometrial endometrioid adenocarcinoma and its inverse correlation with tumor grade
AU - Khin, Ei Ei
AU - Kikkawa, Fumitaka
AU - Ino, Kazuhiko
AU - Kajiyama, Hiroaki
AU - Suzuki, Takahiro
AU - Shibata, Kiyosumi
AU - Tamakoshi, Koji
AU - Nagasaka, Tetsuro
AU - Mizutani, Shigehiko
N1 - Funding Information:
This work was supported in part by Grants-in-Aid from the Ministry of Posts and Telecommunications for specific medical research (collaboration with Nagoya Teishin Hospital) and Education, and the fund of Showakai and Ogya.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2003/3/1
Y1 - 2003/3/1
N2 - OBJECTIVES: Dipeptidyl peptidase IV (DPPIV)/CD26 is a ceil surface aminopeptidase. This study investigated the expression and localization of DPPIV in endometrial endometrioid adenocarcinomas of different grades. STUDY DESIGN: Immunohistochemical analysis was performed by using DPPIV and regulated on activation, normal T-cell expressed and secreted (RANTES) specific monoclonal antibodies. Cell proliferation was evaluated by bromodeoxyuridine (BrdU) uptake assay. RESULTS: Immunohistochemical analyses showed that DPPIV was strongly or moderately stained in glandular cells of the normal secretory phase. In endometrial adenocarcinoma, the DPPIV expression decreased with advancing grade (P < .01). Furthermore, RANTES, one of the possible DPPIV substrates, was highly expressed in all grades of endometrial adenocarcinoma cells. The addition of RANTES to endometrial adenocarcinoma ceils increased proliferation in a concentration-dependent manner. CONCLUSION: DPPIV is expressed in normal endometrial glandular cells, but its expression in endometrial adenocarcinoma is down-regulated with increasing grade. Our data also suggest a regulatory role of this ectoenzyme in neoplastic transformation and progression of endometrial adenocarcinomas possibly by degrading certain bioactive peptides such as RANTES.
AB - OBJECTIVES: Dipeptidyl peptidase IV (DPPIV)/CD26 is a ceil surface aminopeptidase. This study investigated the expression and localization of DPPIV in endometrial endometrioid adenocarcinomas of different grades. STUDY DESIGN: Immunohistochemical analysis was performed by using DPPIV and regulated on activation, normal T-cell expressed and secreted (RANTES) specific monoclonal antibodies. Cell proliferation was evaluated by bromodeoxyuridine (BrdU) uptake assay. RESULTS: Immunohistochemical analyses showed that DPPIV was strongly or moderately stained in glandular cells of the normal secretory phase. In endometrial adenocarcinoma, the DPPIV expression decreased with advancing grade (P < .01). Furthermore, RANTES, one of the possible DPPIV substrates, was highly expressed in all grades of endometrial adenocarcinoma cells. The addition of RANTES to endometrial adenocarcinoma ceils increased proliferation in a concentration-dependent manner. CONCLUSION: DPPIV is expressed in normal endometrial glandular cells, but its expression in endometrial adenocarcinoma is down-regulated with increasing grade. Our data also suggest a regulatory role of this ectoenzyme in neoplastic transformation and progression of endometrial adenocarcinomas possibly by degrading certain bioactive peptides such as RANTES.
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U2 - 10.1067/mob.2003.169
DO - 10.1067/mob.2003.169
M3 - Article
C2 - 12634639
AN - SCOPUS:0037339805
SN - 0002-9378
VL - 188
SP - 670
EP - 676
JO - American Journal of Obstetrics and Gynecology
JF - American Journal of Obstetrics and Gynecology
IS - 3
ER -