Isolation and Characterization of Laminin-10/11 Secreted by Human Lung Carcinoma Cells : LAMININ-10/11 MEDIATES CELL ADHESION THROUGH INTEGRIN α3β1

Kikkawa, Yamato; Sanzen, Noriko; Sekiguchi, Kiyotoshi

Journal of Biological Chemistry, 1998, 273(25), 15854-15859

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Identifier to cite or link to this item: https://hdl.handle.net/11094/71439

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Title
Isolation and Characterization of Laminin-10/11 Secreted by Human Lung Carcinoma Cells : LAMININ-10/11 MEDIATES CELL ADHESION THROUGH INTEGRIN α3β1
Creator
NRID
1000020274227 1000020274227
CreatorName
Kikkawa, Yamato
CreatorName
Sanzen, Noriko
NRID
1000050187845 1000050187845
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Scopus Author ID
7201662709 7201662709
ORCID
0000-0002-6433-1410 0000-0002-6433-1410
CreatorName
Sekiguchi, Kiyotoshi
Description
This research was originally published in the Journal of Biological Chemistry. Yamato Kikkawa, Noriko Sanzen and Kiyotoshi Sekiguchi. Isolation and Characterization of Laminin-10/11 Secreted by Human Lung Carcinoma Cells : LAMININ-10/11 MEDIATES CELL ADHESION THROUGH INTEGRIN α3β1. J. Biol. Chem. 1998; 273: 15854-15859 © the American Society for Biochemistry and Molecular Biology
Abstract
A panel of human tumor cell lines was screened for selective expression of laminin α5 chain, a newly identified laminin subunit comprising laminin-10 (α5β1γ1) and -11 (α5β2γ1). The lung adenocarcinoma cell line A549 was found to express the α5 chain at relatively high levels but no detectable amounts of other α chains. The laminin variants containing α5 chain were purified from the conditioned medium of A549 cells by immunoaffinity chromatography using the anti-laminin monoclonal antibody 4C7 which was shown recently to recognize the laminin α5 chain (Tiger, C.-F., Champliaud, M.-F., Pedrosa-Domellof, F., Thornell, L.-E., Ekblom, P., and Gullberg, D. (1997) J. Biol. Chem. 272, 28590–28595). The purified laminin variants consisted of three chains with molecular masses of 350, 220, and 210 kDa. The 350-kDa chain was specifically recognized by another anti-α5 chain monoclonal antibody capable of recognizing denatured α5 chain on immunoblots, whereas the 210-kDa chain was recognized by an anti-γ1 chain antibody. The purified α5 chain-containing laminin variants (hereafter referred to as laminin-10/11) were highly active in mediating adhesion of A549 cells to the substratum with potency as high as that of laminin-5 and significantly higher than those of laminin-1, laminin-2/4, or fibronectin. Adhesion to substrata coated with laminin-10/11 was specifically inhibited by anti-integrin antibodies directed against the integrin α3 or β1 subunit but not by those against α2 or α6 subunit, indicating that laminin-10/11 is specifically recognized by integrin α3β1. Given the wide distribution of laminin-10/11 in the basement membrane of various tissue types and dominant expression of integrin α3β1 in most epithelial cells, specific interaction of laminin-10/11 with integrin α3β1 may play an important role in in vivo regulation of proliferation and differentiation of epithelial cells through the basement membrane.
Publisher
American Society for Biochemistry and Molecular Biology
Source Title
Journal of Biological Chemistry
Volume (Issue)
273(25)
Page
15854-15859
Date of Issued
1998-06
Language
English
Handle URL
https://hdl.handle.net/11094/71439
eISSN
1083351X
NCID
AA1202441X
Relation.isIdenticalTo
DOI (Publisher Version)
https://doi.org/10.1074/jbc.273.25.15854
Access Rights
open access
oaire:version
Version of Record
Category
学術雑誌論文 Journal Article