Journal article
Integrin alpha 6 beta 4 mediates dynamic interactions with laminin
Journal of cell science, v 107 ( Pt 11)(11), pp 3153-3163
Nov 1994
PMID: 7699012
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
We present here a novel form of dynamic adhesion in which both the integrin receptor and the ligand supporting dynamic adhesion have been identified. Laminar flow assays showed that laminin supported attachment of alpha 6 beta 4-positive cells in the presence of fluid shear stress (tau < or = 2 dyn/cm2), indicating that these cells adhered to laminin within a fraction of a second. Further increases in flow rate (3.5 dyn/cm2 < or = tau < or = 100 dyn/cm2) initiated rolling of attached cells in the direction of flow, suggesting that rapidly formed adhesion is reversible and repeatable. Laminin fragment E8, which interacts with alpha 6 integrins, supported dynamic attachment and rolling but extracellular matrix glycoprotein fibronectin did not. In cell lines that express alpha 6 beta 4 but not alpha 6 beta 1 an anti-alpha 6 monoclonal antibody inhibited attachment to laminin in the presence of flow and following 5 minutes of static incubation. Infusion of this antibody onto cells adherent to laminin-coated slides led to rapid detachment of cells from the substratum. An anti-beta 1 monoclonal antibody diminished adhesion strength following static incubation but did not inhibit rapid attachment and flow-initiated rolling. These results indicate that in some alpha 6 beta 4-expressing epithelial and carcinoma cell lines, integrin alpha 6 beta 4 mediates rapidly formed dynamic interactions with laminin.
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Details
- Title
- Integrin alpha 6 beta 4 mediates dynamic interactions with laminin
- Creators
- A Tözeren - Department of Mechanical Engineering, Catholic University of America, Washington, DC 20064H K KleinmanS WuA M MercurioS W Byers
- Publication Details
- Journal of cell science, v 107 ( Pt 11)(11), pp 3153-3163
- Publisher
- Company of Biologists; England
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:A1994PV95900019
- Scopus ID
- 2-s2.0-0028171789
- Other Identifier
- 991014878445004721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Cell Biology