| Increased expression of dipeptidyl peptidase IV in human mesothelial cells by malignant ascites from ovarian carcinoma patients. | |
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MedLine Citation:
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PMID: 12239451 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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H Kajiyama; F Kikkawa; O Maeda; T Suzuki; K Ino; S Mizutani |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Oncology Volume: 63 ISSN: 0030-2414 ISO Abbreviation: Oncology Publication Date: 2002 |
Date Detail:
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Created Date: 2002-09-19 Completed Date: 2002-10-30 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0135054 Medline TA: Oncology Country: Switzerland |
Other Details:
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Languages: eng Pagination: 158-65 Citation Subset: IM |
Copyright Information:
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Copyright 2002 S. Karger AG, Basel |
Affiliation:
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Department of Obstetrics and Gynecology, Nagoya University School of Medicine, Nagoya, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Aminopeptidases
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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:
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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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