| An increase or a decrease in myosin II phosphorylation inhibits macrophage motility. | |
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MedLine Citation:
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PMID: 2071674 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Myosin II purified from mammalian non-muscle cells is phosphorylated on the 20-kD light chain subunit (MLC20) by the Ca2+/calmodulin-dependent enzyme myosin light chain kinase (MLCK). The importance of MLC20 phosphorylation in regulating cell motility was investigated by introducing either antibodies to MLCK (MK-Ab) or a Ca2+/calmodulin-independent, constitutively active form of MLCK (MK-) into macrophages. The effects of these proteins on cell motility were then determined using a quantitative chemotaxis assay. Chemotaxis is significantly diminished in macrophages containing MK-Ab compared to macrophages containing control antibodies. Moreover, there is an inverse relationship between the number of cells that migrate and the amount of MK-Ab introduced into cells. Interestingly, there is also an inverse relationship between the number of cells that migrate and the amount of MK- introduced into cells. Other experiments demonstrated that MK-Ab decreased intracellular MLC20 phosphorylation while MK- increased MLC20 phosphorylation. MK- also increased the amount of myosin associated with the cytoskeleton. These data demonstrate that the regulation of MLCK is an important aspect of cell motility and suggest that MLC20 phosphorylation must be maintained within narrow limits during translational motility by mammalian cells. |
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Authors:
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A K Wilson; G Gorgas; W D Claypool; P de Lanerolle |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of cell biology Volume: 114 ISSN: 0021-9525 ISO Abbreviation: J. Cell Biol. Publication Date: 1991 Jul |
Date Detail:
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Created Date: 1991-08-19 Completed Date: 1991-08-19 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 0375356 Medline TA: J Cell Biol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 277-83 Citation Subset: IM |
Affiliation:
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Department of Physiology, College of Medicine, University of Illinois, Chicago 60680. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Antibodies / diagnostic use, physiology Cell Movement / drug effects, physiology Chemotaxis / drug effects, physiology Macrophages / drug effects, physiology* Male Myosin-Light-Chain Kinase / immunology, physiology Myosins / metabolism*, physiology Phosphorylation Rats Rats, Inbred Strains |
| Grant Support | |
ID/Acronym/Agency:
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HL02411/HL/NHLBI NIH HHS; HL35808/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Antibodies; EC 2.7.11.18/Myosin-Light-Chain Kinase; EC 3.6.4.1/Myosins |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
| Full Text | |
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Journal Information Journal ID (nlm-ta): J Cell Biol Journal ID (publisher-id): J. Cell Biol. ISSN: 0021-9525 ISSN: 1540-8140 Publisher: The Rockefeller University Press |
Article Information Download PDF  Print publication date: Day: 2 Month: 7 Year: 1991 Volume: 114 Issue: 2 First Page: 277 Last Page: 283 ID: 2289083 Publisher Id: 91302469 PubMed Id: 2071674 |
| An increase or a decrease in myosin II phosphorylation inhibits macrophage motility | |
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