Involvement of integrins and the cytoskeleton in modulation of skeletal muscle glycogen synthesis by changes in cell volume

Muscle glycogen synthesis is modulated by physiologically relevant changes in cell volume. We have investigated the possible involvement of integrin-extracellular matrix interactions in this process using primary cultures of rat skeletal muscle subject to hypo- or hyper-osmotic exposure with integri...

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Bibliographic Details
Published in:FEBS letters 1997-11, Vol.417 (1), p.101-103
Main Authors: Low, Sylvia Y, Rennie, Michael J, Taylor, Peter M
Format: Article
Language:English
Subjects:
Androstadienes - pharmacology
Animals
Cell volume
Cells, Cultured
Colchicine - pharmacology
Culture Media
Cytochalasin D - pharmacology
Cytoskeleton
Cytoskeleton - metabolism
Deoxyglucose - metabolism
FAK
focal adhesion kinase
Glucose - metabolism
Glycogen - biosynthesis
Glycogen synthesis
Integrin
Integrins - metabolism
MAP kinase
mitogen-activated protein kinase
Monosaccharide Transport Proteins - metabolism
Muscle, Skeletal - cytology
Muscle, Skeletal - metabolism
Oligopeptides - metabolism
Oligopeptides - pharmacology
Osmotic Pressure
phosphatidylinositol 3-kinase
PI3-kinase
Rats
Skeletal muscle
Wortmannin
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Summary:Muscle glycogen synthesis is modulated by physiologically relevant changes in cell volume. We have investigated the possible involvement of integrin-extracellular matrix interactions in this process using primary cultures of rat skeletal muscle subject to hypo- or hyper-osmotic exposure with integrin binding peptide GRGDTP to disrupt integrin actions and the inactive analogue GRGESP as control. Osmotically induced increases (77%) and decreases (34%) in glycogen synthesis ( d-[ 14C]-glucose incorporation into glycogen) were prevented by GRGDTP (but not GRGESP) without affecting glucose transport. Cytoskeletal disruption with cytochalasin D or colchicine had similar effects to GRGDTP. Osmotically induced modulation of muscle glycogen synthesis involves integrin-extracellular matrix interactions and cytoskeletal elements, possibly as components of a cell-volume `sensing' mechanism.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)01264-7