MSAP enhances migration of C6 glioma cells through phosphorylation of the myosin regulatory light chain

A key regulatory mechanism in cell motility is the control of myosin activity, which in non-muscle cells is determined by phosphorylation of the myosin regulatory light chain (MRLC). Here we show that MRLC-interacting protein (MIR)-interacting saposin-like protein (MSAP) enhances cell spreading in f...

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Bibliographic Details
Published in:Cellular and molecular life sciences : CMLS 2005-06, Vol.62 (11), p.1260-1266
Main Authors: Bornhauser, B C, Lindholm, D
Format: Article
Language:English
Subjects:
3T3 Cells
Animals
Carrier Proteins - genetics
Carrier Proteins - metabolism
Carrier Proteins - physiology
Cell adhesion & migration
Cell Line, Tumor
Cell Movement - drug effects
Cell Movement - physiology
Cellular biology
Fibroblasts - cytology
Fibroblasts - drug effects
Glioma - drug therapy
Glioma - pathology
Glioma - physiopathology
Kinases
Mice
Myosin Light Chains - drug effects
Myosin Light Chains - metabolism
Phosphorylation
Proteins
Rats
RNA Interference - physiology
RNA, Small Interfering - pharmacology
Saposins - antagonists & inhibitors
Saposins - metabolism
Saposins - pharmacology
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Summary:A key regulatory mechanism in cell motility is the control of myosin activity, which in non-muscle cells is determined by phosphorylation of the myosin regulatory light chain (MRLC). Here we show that MRLC-interacting protein (MIR)-interacting saposin-like protein (MSAP) enhances cell spreading in fibroblasts and migration of rat C6 glioma cells through increases in MRLC phosphorylation. Overexpression of MSAP enhanced the motility of glioma cells measured in matrigel invasion chambers and using a scratch assay. Downregulation of MSAP by RNA interference significantly decreased glioma cell migration and phosphorylation of MRLC. Inhibition of the corresponding MRLC kinase by ML-7 did not affect migration of MSAP-overexpressing cells. The present results show that MSAP controls glioma cell migration via enhancement of MRLC phosphorylation. This effect is independent of the activity of MRLC kinase. Thus, MSAP is a novel modulator of cell motility that influences migration of glioma cells and possibly other tumors.
ISSN:1420-682X
1420-9071
DOI:10.1007/s00018-005-5055-x