Document Detail


Increased expression of dipeptidyl peptidase IV in human mesothelial cells by malignant ascites from ovarian carcinoma patients.
MedLine Citation:
PMID:  12239451     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cell surface aminopeptidases play an important role in biological processes through degradation of small peptides. There are many bioactive peptides in ascites and these peptides are involved in carcinoma cell dissemination and infiltration. In human mesothelial cells dipeptidyl peptidase IV (DPPIV) shows the highest expression mostly in four cell surface aminopeptidases: aminopeptidase A, neutral endopeptidase 24-11, aminopeptidase N and DPPIV. Since mesothelial cells are always in contact with ascites, we examined the influence of malignant ascites on DPPIV. DPPIV enzyme activity in mesothelial cells was enhanced by the addition of ascites obtained from ovarian carcinoma patients in a time- and concentration-dependent manner, and flow cytometry and immunocytochemistry also revealed an increased expression of DPPIV on the cell surface of mesothelial cells. The <3-kD fraction of malignant ascites increased the DPPIV enzyme activity to the same level as the total ascites. Northern hybridization demonstrated that DPPIV mRNA was increased 3-fold by the addition of the <3-kD malignant ascites. In conclusion, DPPIV is highly expressed in human mesothelial cells and was regulated by ascites.
Authors:
H Kajiyama; F Kikkawa; O Maeda; T Suzuki; K Ino; S Mizutani
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Oncology     Volume:  63     ISSN:  0030-2414     ISO Abbreviation:  Oncology     Publication Date:  2002  
Date Detail:
Created Date:  2002-09-19     Completed Date:  2002-10-30     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0135054     Medline TA:  Oncology     Country:  Switzerland    
Other Details:
Languages:  eng     Pagination:  158-65     Citation Subset:  IM    
Copyright Information:
Copyright 2002 S. Karger AG, Basel
Affiliation:
Department of Obstetrics and Gynecology, Nagoya University School of Medicine, Nagoya, Japan.
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MeSH Terms
Descriptor/Qualifier:
Aminopeptidases / metabolism
Antigens, CD26 / metabolism*
Ascites / enzymology
Cell Adhesion
Female
Humans
Immunohistochemistry
Kinetics
Omentum / enzymology
Ovarian Neoplasms / enzymology*,  surgery
Tumor Cells, Cultured
Chemical
Reg. No./Substance:
EC 3.4.11.-/Aminopeptidases; EC 3.4.14.5/Antigens, CD26

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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