Rapid Preparation of a Plasma Membrane Fraction from Adipocytes and Muscle Cells: Application to Detection of Translocated Glucose Transporter 4 on the Plasma Membrane

2007 ◽  
Vol 71 (9) ◽  
pp. 2343-2346 ◽  
Author(s):  
Shin NISHIUMI ◽  
Hitoshi ASHIDA
Keyword(s):  
Plasma Membrane ◽  
Membrane Fraction ◽  
Glucose Transporter ◽  
Muscle Cells ◽  
Glucose Transporter 4 ◽  
Rapid Preparation ◽  
Plasma Membrane Fraction

scholarly journals Surface-labelling studies on skeletal-muscle cells in vitro. Heterogeneity of iodinated cell-surface proteins

1980 ◽  
Vol 186 (1) ◽  
pp. 211-216 ◽  
Author(s):  
G A Cates ◽  
P C Holland
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Plasma Membrane ◽  
Membrane Fraction ◽  
Muscle Cells ◽  
Surface Proteins ◽  
Skeletal Muscle Cells ◽  
Plasma Membrane Fraction ◽  
Surface Labelling

1. Two distinct classes of protein were detected at the surface of chick-embryo skeletal-muscle cells after iodination of the cells in monolayer culture. 2. The two classes of iodinated proteins differed in their ability to co-purify with a vesicular plasma-membrane fraction prepared from surface-labelled cells. 3. One class consisted of predominantly high-molecular-weight glycoproteins that co-purified with the plasma-membrane fraction, but showed no significant qualitative or quantitative alterations in labelling with 125I and lactoperoxidase during myogenesis. 4. A second class of predominantly lower-molecular-weight proteins showed reproducible quantitative alterations in 125I-labelling during myogenesis but failed to co-purify with the plasma-membrane fraction. 5. This second class of proteins may represent matrix proteins involved in intercellular adhesion or adhesion of cells to the substratum. They are unlikely to be directly required for the process of plasma-membrane fusion during myogenesis, since they do not copurify with a vesicular plasma-membrane fraction known to be capable of Ca2+-dependent fusion in vitro.

scholarly journals Calcium-dependent fusion of the plasma membrane fraction from human neutrophils with liposomes

1990 ◽  
Vol 1025 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Joseph W. Francis ◽  
James E. Smolen ◽  
Kenneth J. Balazovich ◽  
Rebecca R. Sandborg ◽  
Laurence A. Boxer
Keyword(s):  
Plasma Membrane ◽  
Membrane Fraction ◽  
Human Neutrophils ◽  
Plasma Membrane Fraction ◽  
Calcium Dependent

Association of the hepatic IP3 receptor with the plasma membrane: relevance to mode of action

1993 ◽  
Vol 265 (6) ◽  
pp. C1588-C1596 ◽  
Author(s):  
L. Feng ◽  
N. Kraus-Friedmann
Keyword(s):  
Plasma Membrane ◽  
Membrane Fraction ◽  
Ip3 Receptors ◽  
Ip3 Receptor ◽  
Plasma Membrane Fraction ◽  
T Lymphoma Cells ◽  
T Lymphoma ◽  
Triton X ◽  
Brain Receptor ◽  
The Brain

Studies were carried out to characterize the interaction between inositol 1,4,5-trisphosphate (IP3) receptors and the plasma membrane fraction. Extraction of the membranes with the nonionic detergents Nonidet P-40 and Triton X-100, followed by centrifugation at 100,000 g, resulted in the doubling of the IP3 receptor in the pellets, whereas no detectable binding was found in the supernatants. These data indicate that the detergents did not solubilize the receptor, that it remained associated with membrane particles, and that it is likely to be associated with the cytoskeleton. The cytoskeleton proteins actin, ankyrin, and spectrin were identified in the plasma membrane fraction. However, comparison of the amount of these proteins in different fractions of the detergent, or otherwise treated plasma membrane fractions, showed no direct correlation between the presence of any of these proteins in the plasma membrane fraction and their ability to bind [3H]IP3. This is in contrast to the brain and T-lymphoma cells in which the IP3 receptor is attached to ankyrin (L. Y. W. Bourguigon, H. Jin, N. Iida, N. R. Brandt, and S. H. Zhang. J. Biol. Chem. 268: 6477-6486, 1993; and S. K. Joseph and S. Samanta. J. Biol. Chem 268: 6477-6486, 1993). Thus the hepatic IP3 receptor, which is different from the brain receptor, might attach to the cytoskeleton by anchoring to a different protein. Because cytochalasin D treatment of livers diminishes the ability of IP3 to raise cytosolic free Ca2+ levels, the attachment of the IP3 receptor to the cytoskeleton seems to involve an association with microfilaments.

Sign in / Sign up

Export Citation Format

Share Document