Insulin regulation of the two glucose transporters in 3T3-L1 adipocytes.

Calderhead, David M.; Kitagawa, Kouichiro; Tanner, L I; Holman, Geoffrey D.; Lienhard, Gustav E.

doi:10.1016/s0021-9258(18)77419-x

Cited by 220 publications

(29 citation statements)

References 23 publications

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“…The levels of GLUT1 in the intracellular compartment of rat adipose cells are less than 10% of the levels of GLUT4 (Holman et al, 1990). This contrasts with 3T3-L1 cells in which the ratio of GLUT1: GLUT4 is 1:1 or greater (Calderhead et al, 1990;Palfreyman et al, 1992). Even if a very small amount of GLUT1 were in GLUT4 vesicles, we do not think this detracts from the use of the method as any heterogeneity in the vesicle population reflects the heterogeneity of the intact cell.…”

Section: Reconstitution Of Glut4 Vesicle Fusion With Plasma Membranementioning

confidence: 84%

Insulin signaling meets vesicle traffic of GLUT4 at a plasma-membrane-activated fusion step

et al. 2005

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A hypothesis that accounts for most of the available literature on insulin-stimulated GLUT4 translocation is that insulin action controls the access of GLUT4 vesicles to a constitutively active plasma-membrane fusion process. However, using an in vitro fusion assay, we show here that fusion is not constitutively active. Instead, the rate of fusion activity is stimulated 8-fold by insulin. Both the magnitude and time course of stimulated in vitro fusion recapitulate the cellular insulin response. Fusion is cell cytoplasm and SNARE dependent but does not require cell cytoskeleton. Furthermore, insulin activation of the plasma-membrane fraction of the fusion reaction is the essential step in regulation. Akt from the cytoplasm fraction is required for fusion. However, the participation of Akt in the stimulation of in vitro fusion is dependent on its in vitro recruitment onto the insulin-activated plasma membrane.

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Section: Reconstitution Of Glut4 Vesicle Fusion With Plasma Membranementioning

confidence: 84%

Insulin signaling meets vesicle traffic of GLUT4 at a plasma-membrane-activated fusion step

et al. 2005

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“…Furthermore, in several cell models including cardiac myocytes and adipocytes, insulininduced glucose uptake was found to be also mediated by the GLUT 1 transporter in addition to GLUT 4. Thus, the actual decrease in expression levels of the various GLUTs during keratinocyte differentiation could explain the lack of responsiveness to insulin stimulation (Calderhead et al, 1990;Robinson and James, 1992;Fischer et al, 1997;Egert et al, 1999). Altogether, these results might explain the lack of response of the glucose transport system Keratinocytes were stimulated with 10 ±7 M insulin or 10 ±8 M IGF-1 for 24 h. (A) Cytoplasmic (cyto) and plasma membrane (mem) extracts were prepared according to Materials and Methods.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Glucose Transport System in Keratinocytes: Insulin and IGF-1 Differentially Affect Specific Transporters

Shen

Sampson

Tennenbaum

et al. 2000

Journal of Investigative Dermatology

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Skin is one of the major tissues displaying chronic diabetic complications. We have studied glucose transport following stimulation with insulin and IGF-1 in cultured mouse keratinocytes. In proliferating cells, acute stimulation with insulin and IGF-1 increased glucose uptake. Insulin translocated glucose transporters 1 and 5, whereas IGF-1 translocated glucose transporters 2 and 3. With differentiation, glucose transporter 3 expression increased and the expression of glucose transporters 1, 2, and 5 decreased. No increase in glucose uptake was observed, however, following stimulation with either hormone. These results indicate that insulin and IGF-1 differentially regulate glucose uptake as well as expression and translocation of specific transporters in skin keratinocytes.

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“…The former argument is less compelling, since it assumes that the activity catalyzed by plasma membrane GLUT4 is at least comparable to that of GLUTI . While there are no direct measurements of the turnover number of GLUT4, a number of investigators have argued for greater activity of this isoform at the concentrations of substrate used in these experiments (9,23,27,33) . If correct, this would have the effect of making the deoxyglucose uptake assay more sensitive to increased levels of cell surface GLUT4 than GLUTI.…”

Section: Discussionmentioning

confidence: 99%

Isoform-specific subcellular targeting of glucose transporters in mouse fibroblasts.

Hudson

Ruiz

Birnbaum

1992

The Journal of Cell Biology

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Abstract. GLUTI, the erythrocyte glucose transporter, and GLUT4, the adipose/muscle transporter, were each expressed in NIH-3T3 cells by retrovirus-mediated gene transfer. In fibroblasts overexpressing GLUT1, basal as well as insulin-stimulated deoxyglucose uptake was increased. Expression of GLUT4 was without affect on either basal or hormone stimulated hexose uptake. Localization of each of the transporters by indirect immunofluorescence revealed that, whereas GLUTI was found primarily on the cell surface, GLUT4 was directed to vesicles in a perinuclear distribution and throughout the cytoplasm. The GLUT4-containing compartment represented neither Golgi complex nor lysosomes, as evidenced by the failure of 1gp110 or Golgi mannosidase to co-localize. However, ONE of the best-characterized actions of the anabolic hormone insulin is its ability to rapidly and reversibly increase the rate of glucose metabolism in pe ripheral target tissues (8). The flux of sugars across the plasma membrane ofmammaliancells is catalyzed by a class of integral membrane glycoproteins, the facilitated hexose transporters . It is this process which is the primary site of action by which insulin modulates glucose uptake . A number of years ago, it became clear that in the basal state a substantial number of glucose transporters in adipose tissue and probably muscle reside within the cell, where they are inactive presumably solely because of their inaccessibility to extracellular sugars (36) . Shortly after exposure to insulin, the adipose cell redistributes its glucose transporters such that a greater number are located on the cell surface and contribute to the influx of hexoses. Whereas it remains unclear as to whether the "translocation" model explains all of the increase in hexose uptake in response to hormone, redistribution certainly occurs and is important to the overall augmented glucose flux. Therefore, a major part of understanding the mechanism by which insulin regulates hexose metabolism involves characterizing the pathways of subcellular trafficking of glucose transport proteins .Recently, the existence of a gene family encoding related glucose transport proteins has been firmly established (4) . The two isoforms relevant to the experiments discussed be- there was substantial overlap between the distribution of GLUT4 and the transferrin receptor, and some colocalization of the transporter isoform with the mannose-6-phosphate receptor. In addition, when FITCwheat germ agglutinin bound to the cell surface was allowed to internalize at 37°C, it concentrated in vesicular structures coincident with GLUT4 immunoreactivity.These data establish that GLUTI and GLUT4 contain within their amino acid sequences information which dictates targeting to distinct cellular compartments. Moreover, GLUT4 can be recognized by those cellular factors which direct membrane proteins to the endosomal pathway. low are GLUTI and GLUT4. cDNAs encoding the former were originally cloned from human hepatoma and rat brain, and probably also code for the wel...

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Insulin regulation of the two glucose transporters in 3T3-L1 adipocytes.

Cited by 220 publications

References 23 publications

Insulin signaling meets vesicle traffic of GLUT4 at a plasma-membrane-activated fusion step

Insulin signaling meets vesicle traffic of GLUT4 at a plasma-membrane-activated fusion step

Characterization of Glucose Transport System in Keratinocytes: Insulin and IGF-1 Differentially Affect Specific Transporters

Isoform-specific subcellular targeting of glucose transporters in mouse fibroblasts.

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