This Article Order Full text via Infotrieve Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Virtanen, I. Articles by Kivilaakso, E. Search for Related Content PubMed PubMed Citation Articles by Virtanen, I. Articles by Kivilaakso, E.

American Journal of Pathology, Vol 147, 1123-1132, Copyright © 1995 by American Society for Investigative Pathology

REGULAR ARTICLES

Differential expression of laminin chains and their integrin receptors in human gastric mucosa

I Virtanen, T Tani, N Back, O Happola, L Laitinen, T Kiviluoto, J Salo, RE Burgeson, VP Lehto and E Kivilaakso
Department of Anatomy, University of Helsinki, Finland.

The proliferating cells of the gastric mucosa are found among the pit and mucous neck cells. These cells migrate upward to renew the surface epithelium and downward to restitute the glandular cells. As the epithelial basement membranes (BMs) function as substrate for cell adhesion and migration as well as signals for their differentiation, we studied, by indirect immunofluorescence microscopy, the distribution of different laminin chains and their integrin receptors in adult human stomach. The immunoreactivity for laminin alpha 2 chain localized to the BMs of glands and the lower parts of the gastric pits whereas the laminin alpha 3 chain (laminin-5/kalinin) immunoreactivity was strictly confined to BMs underneath the surface epithelium and the upper parts of the pits. Proliferating mucosal epithelial cells, identified by Ki- 67 antibodies, were confined to the areas containing both alpha 2 and alpha 3 laminin chains. The alpha 1, beta 1, and gamma 1 laminin chains were found in all BMs of the mucosa whereas the beta 2 chain was prominent in mucosal blood vessels and also detectable in some glands. Among the laminin integrin receptors, the alpha 3 and beta 4 subunits were seen to be expressed in cells along the BMs with the alpha 3 laminin chain. The alpha 6 integrin, on the other hand, was seen in all gastric epithelia. The present results demonstrate that in the adult human stomach laminin alpha 2 and alpha 3 chains show zonal distribution in BM underlying gastric mucosal epithelium whereas other laminin chains show a more general distribution.

This article has been cited by other articles:

				R. F. Klees, R. M. Salasznyk, K. Kingsley, W. A. Williams, A. Boskey, and G. E. Plopper Laminin-5 Induces Osteogenic Gene Expression in Human Mesenchymal Stem Cells through an ERK-dependent Pathway Mol. Biol. Cell, February 1, 2005; 16(2): 881 - 890. [Abstract] [Full Text] [PDF]

				I. Virtanen, M. Korhonen, N. Petajaniemi, T. Karhunen, L.-E. Thornell, L. M. Sorokin, and Y. T. Konttinen Laminin Isoforms in Fetal and Adult Human Adrenal Cortex J. Clin. Endocrinol. Metab., October 1, 2003; 88(10): 4960 - 4966. [Abstract] [Full Text] [PDF]

				H. Yamamoto, F. Itoh, S. Iku, M. Hosokawa, and K. Imai Expression of the {{gamma}}2 Chain of Laminin-5 at the Invasive Front Is Associated with Recurrence and Poor Prognosis in Human Esophageal Squamous Cell Carcinoma Clin. Cancer Res., April 1, 2001; 7(4): 896 - 900. [Abstract] [Full Text]

				N. Koshikawa, K. Moriyama, H. Takamura, H. Mizushima, Y. Nagashima, S. Yanoma, and K. Miyazaki Overexpression of Laminin {{gamma}}2 Chain Monomer in Invading Gastric Carcinoma Cells Cancer Res., November 1, 1999; 59(21): 5596 - 5601. [Abstract] [Full Text] [PDF]