| Laminin-211 in skeletal muscle function. | |
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MedLine Citation:
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PMID: 23154401 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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A chain is no stronger than its weakest link is an old idiom that holds true for muscle biology. As the name implies, skeletal muscle's main function is to move the bones. However, for a muscle to transmit force and withstand the stress that contractions give rise to, it relies on a chain of proteins attaching the cytoskeleton of the muscle fiber to the surrounding extracellular matrix. The importance of this attachment is illustrated by a large number of muscular dystrophies caused by interruption of the cytoskeletal-extracellular matrix interaction. One of the major components of the extracellular matrix is laminin, a heterotrimeric glycoprotein and a major constituent of the basement membrane. It has become increasingly apparent that laminins are involved in a multitude of biological functions, including cell adhesion, differentiation, proliferation, migration and survival. This review will focus on the importance of laminin-211 for normal skeletal muscle function. |
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Authors:
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Johan Holmberg; Madeleine Durbeej |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-11-15 |
Journal Detail:
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Title: Cell adhesion & migration Volume: 7 ISSN: 1933-6926 ISO Abbreviation: Cell Adh Migr Publication Date: 2012 Nov |
Date Detail:
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Created Date: 2012-11-16 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101469464 Medline TA: Cell Adh Migr Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Muscle Biology Unit; Department of Experimental Medical Science; Lund University; Lund, Sweden. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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