spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Stamatoglou, S. C.
Right arrow Articles by Hughes, R. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stamatoglou, S. C.
Right arrow Articles by Hughes, R. C.

Journal of Cell Science, Vol 100, Issue 3 599-604, Copyright © 1991 by Company of Biologists

JOURNAL ARTICLES

Distribution of fibronectin and fibronectin-binding proteins, AGp110 and integrin alpha 5 beta 1, during chemically induced hepatocarcinogenesis in adult rats

SC Stamatoglou, MM Manson, JA Green, X Mayol and RC Hughes
National Institute for Medical Research, Mill Hill, London, UK.

We have used single- and double-label immunocytochemistry to examine the distribution of AGp110, integrin alpha 5 beta 1 and fibronectin in adult rat liver during carcinogenesis induced by aflatoxin B1 or diethylnitrosamine. In normal liver fibronectin and the fibronectin integrin receptor alpha 5 beta 1 are localized on all three domains of the parenchymal cell surface: sinusoidal, lateral and canalicular. In contrast, AGp110, a non-integrin monomeric glycoprotein with fibronectin receptor properties, is confined to the bile canalicular (apical) plasma membrane of hepatocytes. Hepatocarcinogenesis induced by aflatoxin B1 causes altered cell foci to form in the parenchyma, followed by enlargement of these foci to form pre-neoplastic nodules and finally hepatocellular carcinomas of either poorly differentiated, trabecular or adenocarcinoma morphology. Expression of AGp110 decreased to a minimal level, at first selectively in altered cell foci, from the 9th week of treatment, and then indiscriminately in poorly differentiated carcinomas. The same lesions that were deficient in AGp110 also displayed a reduced level of fibronectin and alpha 5 beta 1, although the observed change in AGp110 demarcated altered foci and poorly differentiated tumour lesions more sharply, since expression of alpha 5 beta 1 and fibronectin, though substantially reduced, was still faintly apparent on the cell surface. Small acinar structures, observed in late hyperplastic nodules and in trabecular carcinomas, exhibited even, pericellular staining of fibronectin and alpha 5 beta 1, including prominent staining of the lumen area, whereas staining of AGp110 appeared to be confined to the lumen. In larger ducts of overt adenocarcinomas, fibronectin and alpha 5 beta 1 were distributed along the basal surface of the epithelium and AGp110 on the apical domain.(ABSTRACT TRUNCATED AT 250 WORDS)


This article has been cited by other articles:


Home page
 Am. J. Pathol.Home page
F. Marongiu, S. Doratiotto, S. Montisci, P. Pani, and E. Laconi
Liver Repopulation and Carcinogenesis: Two Sides of the Same Coin?
Am. J. Pathol., April 1, 2008; 172(4): 857 - 864.
[Abstract] [Full Text] [PDF]

Home page
 Int ImmunolHome page
M. D. Gallego, M. A. de la Fuente, I. M. Anton, S. Snapper, R. Fuhlbrigge, and R. S. Geha
WIP and WASP play complementary roles in T cell homing and chemotaxis to SDF-1{alpha}
Int. Immunol., February 1, 2006; 18(2): 221 - 232.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 1991