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11β1 integrin is important for mesenchymal cell function: elimination of
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology.
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Manuscript (Other academic)
Identifiers
URN: urn:nbn:se:uu:diva-89827OAI: oai:DiVA.org:uu-89827DiVA: diva2:161623
Available from: 2002-04-25 Created: 2002-04-25 Last updated: 2010-01-13Bibliographically approved
In thesis
1. Cellular Interactions with Extracellular Matrix During Development and in Muscle Disease
Open this publication in new window or tab >>Cellular Interactions with Extracellular Matrix During Development and in Muscle Disease
2002 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The formation and maintenance of tissues in multicellular animals are crucially dependent on cellular interactions with the extracellular matrix (ECM). Two different studies on such interactions are presented herein.

Studies on expression of laminins in normal and dystrophic skeletal muscle, clarified a much debated issue regarding discrepancies seen for laminin α1-chain expression between human and mouse tissues. Lack of laminin α1-chain expression was verified in both mouse and human skeletal muscle. Furthermore, the earlier discrepancies seen for laminin α1-chain expression was explained by showing that an antibody-reagent, commonly used in human studies, recognised the laminin α5-chain rather than the laminin α1-chain

The integrin α11-chain (forming α11β1 integrin) is the latest addition to the integrin receptor family, and belongs to the I domain-containing group of integrin α-chains. Previous studies had shown that α11β1 is a collagen receptor. In the present study, the in vitro and in vivo functions of the α11-chain were further characterised. Distribution studies on embryonic human and mouse tissues showed that the α11-chain was expressed on mesenchymal cells in the developing tendon, perichondrium, intervertebral disc, and cornea. The interactions of α11β1 integrin with collagen type I and IV were studied in vitro. The α11β1 bound to these collagens in a manner similar to integrin α2β1 (with collagen type I being the preferred ligand for α11β1). Furthermore, α11β1 was shown to mediate migration on collagen type I coated surfaces, and to mediate contraction of collagen type I gels. The in vivo functions of the α11-chain were investigated by the generation of integrin α11-chain null-mice, using gene targeted disruption of the itga11 in embryonic stem cells. Two independent lines of mice lacking α11 protein were generated. Phenotypic analysis of these mice indicated a role for α11β1 in the formation of the musculoskeletal system.

Place, publisher, year, edition, pages
Uppsala: Acta Universitatis Upsaliensis, 2002. 39 p.
Series
Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1104-232X ; 720
Keyword
Cell and molecular biology, integrin, laminin, collagen, muscle, tendon, skeleton, mouse, human, development, Cell- och molekylärbiologi
National Category
Biochemistry and Molecular Biology
Research subject
Molecular Cellbiology
Identifiers
urn:nbn:se:uu:diva-2007 (URN)91-554-5328-7 (ISBN)
Public defence
2002-05-16, Lecture hall B:21 Biomedical Center (BMC), Uppsala, 10:15
Opponent
Available from: 2002-04-25 Created: 2002-04-25Bibliographically approved

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