Potential mechanism of insulin action on glucose transport in the isolated rat adipose cell. Apparent translocation of intracellular transport systems to the plasma membrane.

Cushman, Samuel W.; Wardzala, L J

doi:10.1016/s0021-9258(19)85561-8

Cited by 1,059 publications

(72 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The present experiments have shown that almost all of the internal stores ofNa+/K+-ATPase seem to be recovered in fraction II, probably in the form of small and but partly sealed vesicles. It is widely accepted that insulin stimulates the translocation of glucose transporters from internal stores to the plasma membrane in adipocytes and muscles [26][27][28][29][30][31]. Furthermore, the existence of internal stores of Na+-selective channels [32] and H+-ATPase [33] has been shown.…”

Section: Discussionmentioning

confidence: 99%

Insulin stimulates the translocation of Na+/K+-dependent ATPase molecules from intracellular stores to the plasma membrane in frog skeletal muscle

Omatsu‐Kanbe

Kitasato

1990

Biochemical Journal

View full text Add to dashboard Cite

The mechanism of the stimulation of Na+/K+ transport by insulin in frog skeletal muscle was studied. The ouabain-binding capacity in detergent-treated plasma membranes of insulin-exposed muscles was increased 1.9-fold compared with that of controls. Na+/K(+)-ATPase activity was found in an intracellular 'light fraction' (fraction II) prepared by using anion-exchange chromatography. Marker enzyme activities for plasma and Golgi membranes were not detected in this fraction. The specific activity of Na+/K(+)-ATPase in fraction II from insulin-exposed muscles was 58% of that in an identical fraction from control muscles. No significant difference in the protein yield of the plasma membrane preparation was observed between these two groups. In parallel with the decrease in the Na+/K(+)-ATPase activity in fraction II from insulin-exposed muscles, the ouabain-binding capacity in this fraction was also decreased. The addition of saponin to fraction II increased both Na+/K(+)-ATPase activity and ouabain binding, indicating that some of the Na+/K(+)-ATPase is located in sealed vesicles. These findings support the view that insulin stimulates the translocation of Na+/K(+)-ATPase molecules from fraction II to the plasma membrane.

show abstract

Section: Discussionmentioning

confidence: 99%

Insulin stimulates the translocation of Na+/K+-dependent ATPase molecules from intracellular stores to the plasma membrane in frog skeletal muscle

Omatsu‐Kanbe

Kitasato

1990

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…2). Glucose transporters as studied by cytochalasin B binding In the literature, almost all the studies of D-glucoseinhibitable binding of labelled cytochalasin B carried out to evaluate the function of glucose transporters have yielded linear Scatchard plots [8,10,30]. No change in Kd was observed whether insulin was present or not.…”

Section: Discussion 3-o-methylglucose Transportmentioning

confidence: 99%

Effects of insulin on glucose transport and glucose transporters in rat heart

Zaninetti

Greco-Perotto

Assimacopoulos-Jeannet

et al. 1988

Biochemical Journal

View full text Add to dashboard Cite

The effect of insulin on glucose transport and glucose transporters was studied in perfused rat heart. Glucose transport was measured by the efflux of labelled 3-O-methylglucose from hearts preloaded with this hexose. Insulin stimulated 3-O-methylglucose transport by: (a) doubling the maximal velocity (Vmax); (b) decreasing the Kd from 6.9 to 2.7 mM; (c) increasing the Hill coefficient toward 3-O-methylglucose from 1.9 to 3.1; (d) increasing the efficiency of the transport process (k constant). Glucose transporters in enriched plasma and microsomal membranes from heart were quantified by the [3H]cytochalasin-B-binding assay. When added to normal hearts, insulin produced the following changes in the glucose transporters: (a) it increased the translocation of transporters from an intracellular pool to the plasma membranes; (b) it increased (from 1.6 to 2.7) the Hill coefficient of the transporters translocated into the plasma membranes toward cytochalasin B, suggesting the existence of a positive co-operativity among the transporters appearing in these membranes; (c) it increased the affinity of the transporters (and hence, possibly, of glucose) for cytochalasin B. The data provide evidence that the stimulatory effect of insulin on glucose transport may be due not to the sole translocation of intracellular glucose transporters to the plasma membrane, but to changes in the functional properties thereof.

show abstract

“…The glucose transporters GLUT1 and GLUT4 are important for dynamic energy regulation in skeletal muscle cells; this glucose transport system is preferentially based on GLUT1 in myoblasts and GLUT4 in myotubes (Guillet-Deniau et al 1994). GLUT4 translocates between intracellular compartments and the plasma membrane in both muscle and adipocytes (Cushman and Wardzala 1980;Suzuki and Kono 1980). However, compared with adipocytes, less is known about the molecular machinery of the glucose transport in muscle fibers, because progress in this area has been hampered by the lack of muscle cell lines/systems, which closely reflect the anatomy and physiology of muscle fibers.…”

mentioning

confidence: 99%

Myotube Formation on Micro-patterned Glass: Intracellular Organization and Protein Distribution in C2C12 Skeletal Muscle Cells

Yamamoto

Csikasz

Liu

et al. 2008

J Histochem Cytochem.

View full text Add to dashboard Cite

S U M M A R Y Proliferation and fusion of myoblasts are needed for the generation and repair of multinucleated skeletal muscle fibers in vivo. Studies of myocyte differentiation, cell fusion, and muscle repair are limited by an appropriate in vitro muscle cell culture system. We developed a novel cell culture technique [two-dimensional muscle syncytia (2DMS) technique] that results in formation of myotubes, organized in parallel much like the arrangement in muscle tissue. This technique is based on UV lithography-produced micropatterned glass on which conventionally cultured C2C12 myoblasts proliferate, align, and fuse to neatly arranged contractile myotubes in parallel arrays. Combining this technique with fluorescent microscopy, we observed alignment of actin filament bundles and a perinuclear distribution of glucose transporter 4 after myotube formation. Newly formed myotubes contained adjacently located MyoD-positive and MyoD-negative nuclei, suggesting fusion of MyoD-positive and MyoD-negative cells. In comparison, the closely related myogenic factor Myf5 did not exhibit this pattern of distribution. Furthermore, cytoplasmic patches of MyoD colocalized with bundles of filamentous actin near myotube nuclei. At later stages of differentiation, all nuclei in the myotubes were MyoD negative. The 2DMS system is thus a useful tool for studies on muscle alignment, differentiation, fusion, and subcellular protein localization. (J Histochem Cytochem 56:881-892, 2008)

show abstract

Potential mechanism of insulin action on glucose transport in the isolated rat adipose cell. Apparent translocation of intracellular transport systems to the plasma membrane.

Cited by 1,059 publications

References 21 publications

Insulin stimulates the translocation of Na+/K+-dependent ATPase molecules from intracellular stores to the plasma membrane in frog skeletal muscle

Insulin stimulates the translocation of Na+/K+-dependent ATPase molecules from intracellular stores to the plasma membrane in frog skeletal muscle

Effects of insulin on glucose transport and glucose transporters in rat heart

Myotube Formation on Micro-patterned Glass: Intracellular Organization and Protein Distribution in C2C12 Skeletal Muscle Cells

Contact Info

Product

Resources

About