Document Detail


Aminopeptidase A expression in cervical neoplasia and its relationship to neoplastic transformation and progression.
MedLine Citation:
PMID:  10838501     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Aminopeptidase A (AP-A) is a cell surface metallopeptidase which specifically cleaves the amino-terminal acidic residue from peptide substrates such as angiotensin II. AP-A is identical to the differentiation-related antigen, murine BP-1 or human kidney gp160, and is involved in regulating cell differentiation and/or neoplastic transformation of certain normal and transformed cells. We examined expression of AP-A in premalignant and malignant lesions of the uterine cervix, and investigated whether its expression was related to disease progression and neoplastic transformation. Formalin-fixed, paraffin-embedded tissue sections including 14 cervical intraepithelial neoplasms (CIN) and 23 invasive squamous cell carcinomas (SCC) were immunohistochemically evaluated. AP-A was localized in the basal cell layer in normal squamous epithelium. In CIN, AP-A expression was found on dysplastic cells, and increased with the severity of the precancerous lesions. In invasive cancer, 18 of 19 non-keratinizing-type SCCs and none of 4 keratinizing-type SCCs expressed AP-A. In addition, AP-A immunoreactivity was significantly correlated with proliferating cell nuclear antigen expression in both CIN and SCC cases. Furthermore, angiotensin II type 1 receptor was present in all AP-A-positive SCCs. These results indicate that AP-A is upregulated as the lesion progresses toward carcinoma in the cervical epithelium, and suggest that AP-A may play a regulatory role in neoplastic transformation and disease progression in cervical neoplasms and may serve as a potential tumor marker during cervical neoplasia development.
Authors:
H Fujimura; K Ino; T Nagasaka; N Nakashima; H Nakazato; F Kikkawa; S Mizutani
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Oncology     Volume:  58     ISSN:  0030-2414     ISO Abbreviation:  Oncology     Publication Date:  2000 May 
Date Detail:
Created Date:  2000-07-18     Completed Date:  2000-07-18     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0135054     Medline TA:  Oncology     Country:  SWITZERLAND    
Other Details:
Languages:  eng     Pagination:  342-52     Citation Subset:  IM    
Copyright Information:
Copyright 2000 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:
Adult
Aged
Aminopeptidases / analysis*
Blotting, Western
Cell Transformation, Neoplastic / metabolism*
Cervical Intraepithelial Neoplasia / enzymology*,  pathology
Cervix Uteri / enzymology
Disease Progression
Epithelium / enzymology
Female
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Neoplastic
Glutamyl Aminopeptidase
Humans
Immunohistochemistry
Middle Aged
Uterine Cervical Neoplasms / enzymology*,  pathology
Chemical
Reg. No./Substance:
EC 3.4.11.-/Aminopeptidases; EC 3.4.11.7/Glutamyl Aminopeptidase

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


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