Interaction of insulin with muscle receptors: Specific binding of [125I]insulin by the plasma membrane of the rat skeletal muscle

1980 ◽  
Vol 10 (6) ◽  
pp. 496-499 ◽  
Author(s):  
B. N. Leibush ◽  
V. M. Bondareva
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Specific Binding ◽  
Rat Skeletal Muscle ◽  
Muscle Receptors

Insulin increases the Na(+)-K(+)-ATPase alpha 2-subunit in the surface of rat skeletal muscle: morphological evidence

1993 ◽  
Vol 265 (6) ◽  
pp. C1716-C1722 ◽  
Author(s):  
A. Marette ◽  
J. Krischer ◽  
L. Lavoie ◽  
C. Ackerley ◽  
J. L. Carpentier ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Cellular Localization ◽  
Protein A ◽  
Morphological Evidence ◽  
Mammalian Skeletal Muscle ◽  
Tissue Fixation ◽  
Insulin Stimulation ◽  
Rat Skeletal Muscle ◽  
Quantitative Evidence

The cellular localization of the alpha 2-subunit of the Na(+)-K(+)-ATPase was defined by immunoelectron microscopy, and the effect of insulin on the amount of alpha 2-immunoreactive subunits on the cell surface was quantitated. Two protocols were used for tissue fixation and immunolocalization. Protocol 1 was characterized by fixation with 2% paraformaldehyde, use of a monoclonal antibody, and detection with 3-nm-diameter gold-labeled Fab fragments or 10-nm gold-labeled immunoglobulin G. Protocol 2 was characterized by fixation with 4% paraformaldehyde plus 0.1% glutaraldehyde, use of a polyclonal antibody, and detection with 10-nm gold-labeled protein A. In control muscle, the alpha 2-subunit of the Na(+)-K(+)-ATPase was present at the plasma membrane and in intracellular tubular and vesicular structures located in subsarcolemmal and triadic regions. Acute insulin stimulation increased the number of immunolabeled alpha 2-subunits in the plasma membrane after both fixation protocols. The gain in the plasma membrane ranged from 1.5- to 3.7-fold and was significant at the level of P < 0.005. These results provide morphological quantitative evidence that the alpha 2-subunit of the Na(+)-K(+)-ATPase is present both at the plasma membrane and intracellularly in mammalian skeletal muscle and that insulin acutely increases its abundance in the muscle surface.

scholarly journals Acute exercise increases the number of plasma membrane glucose transporters in rat skeletal muscle

FEBS Letters ◽  
1988 ◽  
Vol 238 (2) ◽  
pp. 235-239 ◽  
Author(s):  
Michael F. Hirshman ◽  
Harriet Wallberg-Henriksson ◽  
Lawrence J. Wardzala ◽  
Elizabeth D. Horton ◽  
Edward S. Horton
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Acute Exercise ◽  
Glucose Transporters ◽  
Rat Skeletal Muscle

Effect of nerve stimulation on rat skeletal muscle. A study of plasma membrane

1985 ◽  
Vol 41 (11) ◽  
pp. 1396-1398 ◽  
Author(s):  
A. Shah ◽  
F. Nagao ◽  
V. Sahgal ◽  
H. Singh
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Nerve Stimulation ◽  
Rat Skeletal Muscle

Acute endurance exercise increases plasma membrane fatty acid transport proteins in rat and human skeletal muscle

2012 ◽  
Vol 302 (2) ◽  
pp. E183-E189 ◽  
Author(s):  
Nicolette S. Bradley ◽  
Laelie A. Snook ◽  
Swati S. Jain ◽  
George J. F. Heigenhauser ◽  
Arend Bonen ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Fatty Acid ◽  
Human Skeletal Muscle ◽  
Transport Proteins ◽  
Fatty Acid Transport ◽  
Acid Transport ◽  
Rat Skeletal Muscle ◽  
Muscle Plasma Membrane ◽  
Fatty Acid Transport Proteins

Fatty acid transport proteins are present on the plasma membrane and are involved in the uptake of long-chain fatty acids into skeletal muscle. The present study determined whether acute endurance exercise increased the plasma membrane content of fatty acid transport proteins in rat and human skeletal muscle and whether the increase was accompanied by an increase in long-chain fatty acid transport in rat skeletal muscle. Sixteen subjects cycled for 120 min at ∼60 ± 2% V̇o2 peak. Two skeletal muscle biopsies were taken at rest and again following cycling. In a parallel study, eight Sprague-Dawley rats ran for 120 min at 20 m/min, whereas eight rats acted as nonrunning controls. Giant sarcolemmal vesicles were prepared, and protein content of FAT/CD36 and FABPpm was measured in human and rat vesicles and whole muscle homogenate. Palmitate uptake was measured in the rat vesicles. In human muscle, plasma membrane FAT/CD36 and FABPpm protein contents increased 75 and 20%, respectively, following 120 min of exercise. In rat muscle, plasma membrane FAT/CD36 and FABPpm increased 20 and 30%, respectively, and correlated with a 30% increase in palmitate transport following 120 min of running. These data suggest that the translocation of FAT/CD36 and FABPpm to the plasma membrane in rat skeletal muscle is related to the increase in fatty acid transport and oxidation that occurs with endurance running. This study is also the first to demonstrate that endurance cycling induces an increase in plasma membrane FAT/CD36 and FABPpm content in human skeletal muscle, which is predicted to increase fatty acid transport.

scholarly journals Characterization of L-carnitine transport into rat skeletal muscle plasma membrane vesicles

2000 ◽  
Vol 267 (7) ◽  
pp. 1985-1994 ◽  
Author(s):  
Simona Berardi ◽  
Bruno Stieger ◽  
Bruno Hagenbuch ◽  
Ernesto Carafoli ◽  
Stephan Krähenbühl
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Membrane Vesicles ◽  
Rat Skeletal Muscle ◽  
Plasma Membrane Vesicles ◽  
Muscle Plasma Membrane ◽  
Carnitine Transport

Glucose transport into rat skeletal muscle: interaction between exercise and insulin

1988 ◽  
Vol 65 (2) ◽  
pp. 909-913 ◽  
Author(s):  
H. Wallberg-Henriksson ◽  
S. H. Constable ◽  
D. A. Young ◽  
J. O. Holloszy
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Glucose Transport ◽  
Transport Process ◽  
Sugar Transport ◽  
Glucose Transporters ◽  
Mammalian Skeletal Muscle ◽  
Rat Skeletal Muscle ◽  
Wide Range ◽  
Exercise Induced

This study was done to evaluate the effect of insulin on sugar transport into skeletal muscle after exercise. The permeability of rat epitrochlearis muscle to 3-O-methylglucose (3-MG) was measured after exposure to a range of insulin concentrations 30, 60, and 180 min after a bout of exercise. Thirty and 60 min after exercise, the effects of exercise and insulin on 3-MG transport were additive over a wide range of insulin concentrations, with no increase in sensitivity or responsiveness to insulin. After 180 min, when approximately 66% of the exercise-induced increase in sugar transport had worn off, both the responsiveness and sensitivity of the glucose transport process to insulin were increased. These findings appear compatible with the hypothesis that the actions of exercise and insulin result in activation and/or translocation into the plasma membrane of two separate pools of glucose transporters in mammalian skeletal muscle.

scholarly journals Sphingomyelin Levels in the Plasma Membrane Correlate with the Activation State of Muscle Satellite Cells

2006 ◽  
Vol 54 (4) ◽  
pp. 375-384 ◽  
Author(s):  
Yosuke Nagata ◽  
Hideshi Kobayashi ◽  
Masato Umeda ◽  
Naoshi Ohta ◽  
Seiichiro Kawashima ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Satellite Cells ◽  
Plasma Membranes ◽  
Specific Binding ◽  
Postnatal Growth ◽  
Bioactive Lipids ◽  
Specific Binding Protein ◽  
C2c12 Muscle Cells

Satellite cells are responsible for postnatal growth, hypertrophy, and regeneration of skeletal muscle. They are normally quiescent, and must be activated to fulfill these functions, yet little is known of how this is regulated. As a first step in determining the role of lipids in this process, we examined the dynamics of sphingomyelin in the plasma membrane. Sphingomyelin contributes to caveolae/lipid rafts, which act to concentrate signaling molecules, and is also a precursor of several bioactive lipids. Proliferating or differentiated C2C12 muscle cells did not bind lysenin, a sphingomyelin-specific binding protein, but noncycling reserve cells did. Quiescent satellite cells also bound lysenin, revealing high levels of sphingomyelin in their plasma membranes. On activation, however, the levels of sphingomyelin drop, so that lysenin did not label proliferating satellite cells. Although most satellite cell progeny differentiate, others stop cycling, maintain Pax7, downregulate MyoD, and escape immediate differentiation. Importantly, many of these Pax7-positive/MyoD-negative cells also regained lysenin binding on their surface, showing that the levels of sphingomyelin had again increased. Our observations show that quiescent satellite cells are characterized by high levels of sphingomyelin in their plasma membranes and that lysenin provides a novel marker of myogenic quiescence.

Catecholamine Binding to Plasma Membrane Enriched Fractions of Heart and Skeletal Muscle

1975 ◽  
Vol 53 (3) ◽  
pp. 458-469 ◽  
Author(s):  
Julien Vallières ◽  
Maureen Drummond ◽  
George I. Drummond
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Specific Binding ◽  
Hydroxyl Groups ◽  
Guinea Pig Heart ◽  
Beta Adrenergic ◽  
Beta Agonists ◽  
Low Concentrations ◽  
Adrenergic Antagonists ◽  
Filtration Technique

Binding of [3H]epinephrine to plasma membrane enriched fractions from guinea pig heart and rabbit skeletal muscle was investigated using the micropore filtration technique. [3H]Epinephrine and [3H]norepinephrine were found to be degraded rapidly in aqueous buffer at pH 7.6 and 37 °C. Deterioration of the compounds could be prevented by low concentrations of dithiothreitol. Binding of [3H]epinephrine to both membrane preparations was a slow process requiring 60 min to approach equilibrium in the case of cardiac membranes at 37 °C, and 20 min for skeletal muscle membranes at 0 °C. Binding was antagonized by the unlabeled beta-agonists, isopropyl-norepinephrine, epinephrine, and norepinephrine but all were equipotent. A variety of catechol compounds were as effective antagonists of binding as the catecholamines. The beta-adrenergic antagonists propranolol, pronethalol, and dichloroisoproterenol were not effective in inhibiting binding to either membrane preparation. D-Norepinephrine and L-norepinephrine were equieffective in antagonizing binding of [3H]norepinephrine to skeletal muscle membranes. It was concluded that binding of labeled catecholamine to isolated tissue membranes using the micropore filtration technique does not represent interaction with the specific beta-adrenergic receptor, but more likely reflects a less specific binding of compounds having one or more hydroxyl groups on a ring.

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