Abstract
Rat adipose cells treated with Staphylococcus aureus alpha-toxin are permeable and retain their ability to respond to insulin after hormone treatment. The GLUT 4 glucose transporter isoform, specific to fat and muscle cells, is translocated normally from low density microsomes to the plasma membrane in permeabilized cells. Addition of guanosine 5'-O-(3-thiotriphosphate), guanylyl imidodiphosphate, or guanylyl beta, gamma-methylenediphosphate to permeabilized adipocytes induces an insulin-like translocation of GLUT 4 to the plasma membrane; GTP or adenosine 5'-(beta, gamma-imino)triphosphate has no effect. No translocation of GLUT 4 is observed when GTP analogs are added to intact adipocytes. These results suggest the involvement of a GTP-binding protein in insulin-triggered recruitment of GLUT 4 to the cell surface.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Adipose Tissue / metabolism*
-
Amino Acid Sequence
-
Animals
-
Bacterial Toxins / pharmacology
-
Cell Compartmentation / drug effects
-
Cell Membrane / metabolism*
-
Cell Membrane Permeability / drug effects
-
Cells, Cultured
-
Guanosine 5'-O-(3-Thiotriphosphate) / pharmacology
-
Guanosine Triphosphate / pharmacology*
-
Guanylyl Imidodiphosphate / pharmacology
-
Hemolysin Proteins / pharmacology
-
Immunologic Techniques
-
In Vitro Techniques
-
Insulin / pharmacology*
-
Molecular Sequence Data
-
Monosaccharide Transport Proteins / metabolism*
-
Rats
-
Saponins / pharmacology
Substances
-
Bacterial Toxins
-
Hemolysin Proteins
-
Insulin
-
Monosaccharide Transport Proteins
-
Saponins
-
staphylococcal alpha-toxin
-
Guanylyl Imidodiphosphate
-
Guanosine 5'-O-(3-Thiotriphosphate)
-
Guanosine Triphosphate