Literature DB >> 10924130

Modulation of GLUT4 and GLUT1 recycling by insulin in rat adipocytes: kinetic analysis based on the involvement of multiple intracellular compartments.

W Lee1, J Ryu, R A Spangler, C Y Jung.   

Abstract

The trafficking kinetics of GLUT4 and GLUT1 in rat epididymal adipocytes were analyzed by a four-compartment model based upon steady-state pool sizes of three intracellular fractions and one plasma membrane fraction separated and assessed under both basal and insulin-stimulated states. The steady-state compartment sizes provided relative values of the kinetic coefficients characterizing the rate of each process in the loop. Absolute values of these coefficients were obtained by matching the simulated half-times to those observed experimentally and reported in the literature for both basal and insulin-stimulated states. Our analysis revealed that insulin modulates the GLUT4 trafficking at multiple steps in the rat adipocyte, not only reducing the endocytotic rate constant 3-4-fold and increasing the exocytotic rate 8-24-fold but also increasing the two rate coefficients coupling the three intracellular compartments 2-6-fold each. Furthermore, GLUT1 was completely segregated from GLUT4 in two of the three intracellular compartments, and its steady-state distribution is consistent with a four-compartment model of GLUT1 recycling involving an insulin sensitive endocytosis step in common with the GLUT4 system, but with all other processes being insensitive to insulin.

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Year:  2000        PMID: 10924130     DOI: 10.1021/bi0007021

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  7 in total

1.  Insulin-responsive compartments containing GLUT4 in 3T3-L1 and CHO cells: regulation by amino acid concentrations.

Authors:  J S Bogan; A E McKee; H F Lodish
Journal:  Mol Cell Biol       Date:  2001-07       Impact factor: 4.272

2.  OGA inhibition by GlcNAc-selenazoline.

Authors:  Eun Ju Kim; Dona C Love; Etzer Darout; Mohannad Abdo; Brian Rempel; Stephen G Withers; Paul R Rablen; John A Hanover; Spencer Knapp
Journal:  Bioorg Med Chem       Date:  2010-08-11       Impact factor: 3.641

3.  Activation of protein kinase C zeta induces serine phosphorylation of VAMP2 in the GLUT4 compartment and increases glucose transport in skeletal muscle.

Authors:  L Braiman; A Alt; T Kuroki; M Ohba; A Bak; T Tennenbaum; S R Sampson
Journal:  Mol Cell Biol       Date:  2001-11       Impact factor: 4.272

4.  Separation of insulin signaling into distinct GLUT4 translocation and activation steps.

Authors:  Makoto Funaki; Paramjeet Randhawa; Paul A Janmey
Journal:  Mol Cell Biol       Date:  2004-09       Impact factor: 4.272

5.  Proteomic analysis of GLUT4 storage vesicles reveals LRP1 to be an important vesicle component and target of insulin signaling.

Authors:  Mark P Jedrychowski; Carlos A Gartner; Steven P Gygi; Li Zhou; Joachim Herz; Konstantin V Kandror; Paul F Pilch
Journal:  J Biol Chem       Date:  2009-10-28       Impact factor: 5.157

Review 6.  Subcellular trafficking of the substrate transporters GLUT4 and CD36 in cardiomyocytes.

Authors:  Laura K M Steinbusch; Robert W Schwenk; D Margriet Ouwens; Michaela Diamant; Jan F C Glatz; Joost J F P Luiken
Journal:  Cell Mol Life Sci       Date:  2011-05-06       Impact factor: 9.261

7.  Proteomics in the characterization of adipose dysfunction in obesity.

Authors:  David Brockman; Xiaoli Chen
Journal:  Adipocyte       Date:  2012-01-01       Impact factor: 4.534

  7 in total

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