Purification of insulin-dependent exocytic vesicles containing the glucose transporter.

James, David E.; Lederman, Lynne; Pilch, Paul F.

doi:10.1016/s0021-9258(18)60887-7

Cited by 59 publications

(9 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A similar mechanism of insulin action has been described in mouse 3T3-L1 adipocytes (Biber and Lienhard, 1986;Blok et al, 1988). Vesicles containing the insulin-responsive intracellular GT have recently been isolated from 3T3-L1 adipocytes (Biber and Lienhard, 1986) and from rat adipocytes (James et al, 1987).…”

mentioning

confidence: 54%

See 1 more Smart Citation

Localization of transferrin receptors and insulin-like growth factor II receptors in vesicles from 3T3-L1 adipocytes that contain intracellular glucose transporters.

Tanner

Lienhard

1989

The Journal of Cell Biology

View full text Add to dashboard Cite

Abstract. Transferrin receptors in detergent extracts of subcellular membrane fractions prepared from 3T3-L1 adipocytes were measured by a binding assay. There was a small but significant increase (1.2-fold) in the amount of receptor in a crude plasma membrane fraction and a 40% decrease in the number of transferrin receptors in microsomal membranes prepared from insulin-treated cells, when compared with corresponding fractions from control cells. Intracellular vesicles containing insulin-responsive glucose transporters (GT) have been isolated by immunoadsorption from the microsomal fraction (Biber, J. W., and G. E. Lienhard. 1986. J. Biol. Chem. 261:16180-16184). All of the transferrin receptors in this fraction were localized in these vesicles; however, because the GT vesicles contain '~30-fold fewer transferrin receptors than GT, on the average only one vesicle in three contains a transferrin receptor.The binding of ~25I-pentamannose 6-phosphate BSA to 3T3-L1 adipocytes at 4°C was used to monitor surface insulin-like growth factor II (IGF-II)/mannose 6-phosphate receptors. Exposure of cells to insulin at 37°C for 5 min resulted in a 2.5-4.5-fold increase in surface receptors. There was a corresponding 20% decrease in the amount of IGF-II receptors in the microsomal membranes prepared from insulin-treated cells, as assayed by immunoblotting. Moreover, the IGF-II receptors and GT were located in the same intracellular vesicles, since antibodies to the carboxyterminal peptide of either protein immunoadsorbed vesicles containing 70-95 % of both proteins initially present in the microsomal fraction. In conjunction with other studies, these results indicate that in 3T3-L1 adipocytes, three membrane proteins (the GT, the transferrin receptor, and the IGF-II receptor) respond similarly to insulin, by redistributing to the surface from intracellular compartment(s) in which they are colocalized.

show abstract

mentioning

confidence: 54%

“…A vesicle population enriched in GT has also been prepared from rat adipocytes (James et al, 1987). The procedure involved isolation of a low-density microsomal fraction, followed by sucrose gradient centrifugation, and agarose gel electrophoresis.…”

Section: Discussionmentioning

confidence: 99%

Localization of transferrin receptors and insulin-like growth factor II receptors in vesicles from 3T3-L1 adipocytes that contain intracellular glucose transporters.

Tanner

Lienhard

1989

The Journal of Cell Biology

View full text Add to dashboard Cite

show abstract

“…Thus, the insulin stimulated translocation of GLUT4 storage vesicles (GSV) from the intracellular storage pools to the plasma membrane (PM). Upon deposition of the GLUT4 protein on the PM, glucose uptake was increased by 10-to 20-fold [30][31][32]. Thus, enhancing translocation and expression of GLUT4 might be a promising anti-obesity strategy.…”

Section: Increased Ampk-dependent Gene Expressionmentioning

confidence: 99%

The Efficacy of Gynostemma pentaphyllum Extract in Anti-obesity Therapy

Kim¹,

Kim²,

Lee³

et al. 2019

Rec.Nat.Prod.

View full text Add to dashboard Cite

In the present study, we investigated a saponin-enriched fraction from Gynostemma pentaphyllum extract (GPE) and isolated gypenoside L (GL), gypenoside LI (GLI), and ginsenoside Rg3 (Rg3). To explore the anti-obesity activities of these compounds, we investigated the effects of GL, GLI, and Rg3 on glucose uptake and activation of AMPK in L6 skeletal muscle cells. GPE, GL, GLI, and Rg3 markedly increased glucose uptake activity and GLUT4 gene expression in L6 myotubes. The enhanced glucose uptake was mediated by the activation of the AMPK-ACC signaling pathway. In addition, we observed that GPE, GL, GLI, and Rg3 increased the expression of SIRT1 and PPARγ coacvtivator-1α (PGC-1α). Our results suggest the potential use of Gynostemma pentaphyllum in developing a therapeutic agent to reduce body weight and prevent diet-related diseases via glucose uptake and AMPK activation.

show abstract

“…Much is known about the mechanisms by which insulin activates glucose transport in adipocytes or in muscle; a major mechanism by which insulin mediates this effect is to increase the number of glucose transporters residing in the plasma membrane of the cell (Cushman & Wardzala, 1980;Suzuki & Kono, 1980;Kono et al, 1981;Karnieli et al, 1981;James et al, 1987), as a consequence of a translocation of glucose transporters from an intracellular location to the plasma membrane. However, our knowledge of the mechanism involved in insulin action to activate amino acid transport through system A is scarce, as is structural information on the system A transporter.…”

Section: Introductionmentioning

confidence: 99%

Insulin-stimulated α-(methyl)aminoisobutyric acid uptake in skeletal muscle. Evidence for a short-term activation of uptake independent of Na+ electrochemical gradient and protein synthesis

Gumà

Testar

Palacı́n

et al. 1988

Biochemical Journal

View full text Add to dashboard Cite

1. The present study was designed to explore the mechanisms by which insulin stimulates system A of amino acid transport in extensor digitorum longus (EDL) muscles, by using a system A analogue, alpha-(methyl)aminoisobutyric acid (MeAIB). 2. Insulin stimulation of MeAIB uptake was noted after only 30 min of incubation and was maximal at 60 min. Kinetics of the insulin effect on MeAIB uptake were characterized by an increased Vmax. without modification of Km for MeAIB. 3. Incubation of EDL muscles with cycloheximide for 90 min did not modify MeAIB uptake in either the presence or the absence of insulin, indicating the independence of insulin action from protein synthesis de novo. Incubations for 180 min with cycloheximide caused a decrease in basal MeAIB uptake; however, the percentage stimulation of amino acid transport by insulin was unaltered. Basal MeAIB uptake was increased by incubation for 180 min, but under these conditions no change in the percentage effect of insulin was found. 4. Ouabain, gramicidin D, or both, markedly decreased basal MeAIB uptake by EDL muscle, but the percentage effect of insulin was unaltered. 5. We conclude that insulin action on amino acid transport through system A in muscle is rapid, is characterized by an increased Vmax., and is independent of protein synthesis de novo and the Na+ electrochemical gradient. Our data are compatible with insulin acting directly on the system A transporter.

show abstract

Purification of insulin-dependent exocytic vesicles containing the glucose transporter.

Cited by 59 publications

References 39 publications

Localization of transferrin receptors and insulin-like growth factor II receptors in vesicles from 3T3-L1 adipocytes that contain intracellular glucose transporters.

Localization of transferrin receptors and insulin-like growth factor II receptors in vesicles from 3T3-L1 adipocytes that contain intracellular glucose transporters.

The Efficacy of Gynostemma pentaphyllum Extract in Anti-obesity Therapy

Insulin-stimulated α-(methyl)aminoisobutyric acid uptake in skeletal muscle. Evidence for a short-term activation of uptake independent of Na+ electrochemical gradient and protein synthesis

Contact Info

Product

Resources

About