Advertisement
Journal of Biological Chemistry
Open access logo
Advanced searchSave search
Journal Article| Volume 266, ISSUE 16, P10122-10130, June 05, 1991

Protein synthesis inhibitors activate glucose transport without increasing plasma membrane glucose transporters in 3T3-L1 adipocytes

Open AccessPublished:June 05, 1991DOI:https://doi.org/10.1016/S0021-9258(18)99198-2
Protein synthesis inhibitors activate glucose transport without increasing plasma membrane glucose transporters in 3T3-L1 adipocytes
Previous ArticleDNA substrate requirements for stable joint molecule formation by the RecA and single-stranded DNA-binding proteins of Escherichia coli
Next ArticleActivation of mitogen-activated protein kinase in BC3H1 myocytes by fluoroaluminate
      This paper is only available as a PDF. To read, Please Download here.
      In this study, we tested the hypothesis that hexose transport regulation may involve proteins with relatively rapid turnover rates. 3T3-L1 adipocytes, which exhibit 10-fold increases in hexose transport rates within 30 min of the addition of 100 nM insulin, were utilized. Exposure of these cells to 300 microM anisomycin or 500 microM cycloheximide caused a maximal, 7-fold increase in 2-deoxyglucose transport rate after 4-8 h. The effects due to either insulin (0.5 h) or anisomycin (5 h) on the kinetics of zero-trans 3-O-methyl[14C]glucose transport were similar, resulting in 2.5-3-fold increases in apparent Vmax values (control Vmax = 1.6 +/- 0.3 x 10(-7) mmol/s/10(6) cells) coupled with approximately 2-fold decreases in apparent Km values (control Km = 23 +/- 3.3 mM). Insulin elicited the expected increases in plasma membrane levels of HepG2/erythrocyte (GLUT1) and muscle/adipocyte (GLUT4) transporters (1.6- and 2.8-fold, respectively) as determined by protein immunoblotting. In contrast, neither total cellular contents nor plasma membrane levels of these two transporter isoforms were increased when 3T3-L1 adipocytes were treated with either anisomycin or cycloheximide. 3-[125I]Iodo-4-azidophenethylamido-7-O-succinyldeacetylforskoli n labeling of glucose transporters in plasma membrane fractions of similarly treated cells was also unaffected by these agents. Thus, a striking discrepancy was observed between the marked increase in cellular hexose transport rates due to these protein synthesis inhibitors and the unaltered amounts of glucose transporter proteins in the plasma membrane fraction. These data indicate that short-term protein synthesis inhibition in 3T3-L1 adipocytes leads to large increases in the intrinsic catalytic activity of one or both of the GLUT1 and GLUT4 transporter isoforms.

      REFERENCES

        • Levine R.
        • Goldstein M.S.
        Recent Prog. Horm. Res. 1955; 11: 343-380
        • Suzuki K.
        • Ko no T.
        Proc. Natl. Acad. Sci. U. S. A. 1980; 77: 2542-2545
        • Cushman S.W.
        • Wardzala L.J.
        J. Biol. Chem. 1980; 255: 4758-4762
        • Wardzala L.J.
        • Jeanrenaud B.
        J. Biol. Chem. 1981; 256: 7090-7093
        • Wardzala L.J.
        • Jeanrenaud B.
        Biochim. Biophys. Acta. 1983; 730: 49-56
        • Watanabe T.
        • Smith M.M.
        • Robinson F.W.
        • Kono T.
        J. Biol. Chem. 1984; 259: 13117-13122
        • Oka Y.
        • Czech M.P.
        J. Biol. Chem. 1984; 259: 8125-8133
        • Kono T.
        • Suzuki K.
        • Dansey L.E.
        • Robinson F.W.
        • Blevins T.L.
        J. Biol. Chem. 1981; 256: 6400-6407
        • Baly D.L.
        • Horuk R.
        J. Biol. Chem. 1987; 262: 21-24
        • Matthaei S.
        • Olefsky J.
        • Karnieli E.
        Biochem. J. 1988; 251: 491-497
        • Jones T.L.Z.
        • Cushman S.W.
        J. Biol. Chem. 1989; 264: 7874-7877
        • Gould G.W.
        • Derechin V.
        • James D.E.
        • Tordjman K.
        • Ahern S.
        • Gibbs E.M.
        • Lienhard G.E.
        • Mueckler M.
        J. Biol. Chem. 1989; 264: 2180-2184
        • James D.E.
        • Strube M.
        • Mueckler M.
        Nature. 1989; 338: 83-87
        • Oka Y.
        • Asano T.
        • Shibasaki Y.
        • Kasuga M.
        • Kanazawa Y.
        • Takaku F.
        J. Biol. Chem. 1988; 263: 13432-13439
        • Zorzano A.
        • Wilkinson W.
        • Kotliar N.
        • Thoidis G.
        • Wadzinkski B.E.
        • Ruoho A.E.
        • Pilch P.F.
        J. Biol. Chem. 1989; 264: 12358-12363
        • Calderhead D.M.
        • Kitagawa K.
        • Tanner L.I.
        • Holman G.D.
        • Leinhard G.E.
        J. Biol. Chem. 1990; 265: 13800-13808
        • Clancy B.M.
        • Czech M.P.
        J. Biol. Chem. 1990; 265: 12434-12443
        • Frost S.C.
        • Lane M.D.
        J. Biol. Chem. 1985; 260: 2646-2652
        • Simpson I.A.
        • Yver D.R.
        • Hissin P.J.
        • Wardzala L.J.
        • Karnieli E.
        • Salans L.B.
        • Cushman S.W.
        Biochim. Biophys. Acta. 1983; 763: 393-407
        • Avruch J.
        • Wallach D.F.H.
        Biochim. Biophys. Acta. 1971; 233: 334-347
        • Doolittle R.F.
        Of Urfs and Orfs, pp.85. University Science Books, Mill Valley, CA1983
        • Laemmli U.K.
        Nature. 1970; 227: 680-685
        • Wadzinski B.E.
        • Shanahan M.F.
        • Ruoho A.E.
        J. Biol. Chem. 1987; 262: 17683-17689
        • Wadzinski B.E.
        • Shanahan M.F.
        • Clark R.B.
        • Ruoho A.E.
        Biochem. J. 1988; 255: 983-990
        • Lewis J.B.
        • Mathews M.B.
        Cell. 1980; 21: 303-313
        • Greenberg M.E.
        • Hermanowski A.L.
        • Ziff E.B.
        Mol. Cell. Biol. 1986; 6: 1050-1057
        • Toyoda N.
        • Flanagan J.E.
        • Kono T.
        J. Biol. Chem. 1987; 262: 2737-2745
        • Suzuki K.
        J. Biol. Chem. 1988; 263: 12247-12252
        • Martz A.
        • Mookerjee B.K.
        • Jung C.Y.
        J. Biol. Chem. 1986; 261: 13606-13609
        • Joost H.G.
        • Weber T.M.
        • Cushman S.W.
        Biochem. J. 1988; 249: 155-161
        • Christopher C.W.
        • Ullrey D.
        • Colby W.
        • Kalckar H.M.
        Proc. Natl. Acad. Sci. U. S. A. 1976; 73: 2429-2433
        • Tordjman K.M.
        • Leingang K.A.
        • James D.E.
        • Mueckler M.M.
        Proc. Natl. Acad. Sci. U. S. A. 1989; 86: 7761-7765
        • Berger J.
        • Bisivas C.
        • Vicario P.P.
        • Strout H.V.
        • Saperstein R.
        • Pilch P.F.
        Nature. 1989; 340: 70-72
        • Karnieli E.
        • Hissin P.J.
        • Simpson I.A.
        • Salans L.B.
        • Cushman S.W.
        J. Clin. Invest. 1981; 68: 811-814
        • Haspel H.C.
        • Wilk E.W.
        • Birnbaum M.J.
        • Cushman S.W.
        • Rosen O.M.
        J. Biol. Chem. 1986; 261: 6778-6789
        • Yamada K.
        • Tillotson L.G.
        • Isselbacher K.J.
        J. Biol. Chem. 1983; 258: 9786-9792
        • Simpson I.A.
        • Cushman S.W.
        Annu. Rev. Biochem. 1986; 55: 1059-1089
        • Kuroda M.
        • Honner R.C.
        • Cushman S.W.
        • Londos C.
        • Simpson I.A.
        J. Biol. Chem. 1987; 262: 245-253
        • Smith U.
        • Kuroda M.
        • Simpson I.A.
        J. Biol. Chem. 1984; 259: 8758-8763
        • Green A.
        Biochem. J. 1983; 212: 189-195
        • Joost H.G.
        • Weber T.M.
        • Cushman S.W.
        • Simpson I.A.
        J. Biol. Chem. 1986; 261: 10033-10036
        • Harrison S.A.
        • Buxton J.M.
        • Clancy B.M.
        • Czech M.P.
        J. Biol. Chem. 1990; 265: 20106-20116
        • Gale E.F.
        • Cundliffe E.
        • Reynolds P.E.
        • Richmond M.H.
        • Waring M.J.
        The Molecular Basis of Antibiotic Action. 2nd ed. John Wiley & Sons, New York1972: 502-507
        • Messina J.L.
        J. Biol. Chem. 1990; 265: 11700-11705
        • Kozma S.C.
        • Lane H.A.
        • Ferrari S.
        • Luther H.
        • Siegmann M.
        • Thomas G.
        EMBOJ. 1989; 8: 4125-4132
        • Burger M.
        • Lawen A.
        • Martini O.H.W.
        Eur. J. Biochem. 1988; 183: 255-262
        • Price D.J.
        • Nemenoff R.A.
        • Avruch J.
        J. Biol. Chem. 1989; 264: 13825-13833
        • Fukumoto H.
        • Kayano T.
        • Buse J.B.
        • Edwards Y.
        • Pilch P.F.
        • Bell G.I.
        • Seino S.
        J. Biol. Chem. 1989; 264: 7776-7779

      Article info

      Publication history

      Published online: June 05, 1991

      Identification

      DOI: https://doi.org/10.1016/S0021-9258(18)99198-2

      Copyright

      © 1991 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.

      User license

      Creative Commons Attribution (CC BY 4.0) |
      How you can reuse Information Icon
      Creative Commons Attribution (CC BY 4.0)

      Permitted

      • Read, print & download
      • Redistribute or republish the final article
      • Text & data mine
      • Translate the article
      • Reuse portions or extracts from the article in other works
      • Sell or re-use for commercial purposes

      Elsevier's open access license policy

      ScienceDirect

      Access this article on ScienceDirect

      ASBMB  ASBMB  ASBMB  ASBMB

      ISSN 0021-9258
      We use cookies to help provide and enhance our service and tailor content. To update your cookie settings, please visit the for this site.
      Copyright © 2022 Elsevier Inc. except certain content provided by third parties. The content on this site is intended for healthcare professionals.


      RELX