Detection of the GLUT3 facilitative glucose transporter in rat L6 muscle cells: Regulation by cellular differentiation, insulin and insulin-like growth factor-I

Philip J. Bilan, Yasuhide Mitsumoto, Frances Maher, Ian A. Simpson, Amira Klip

Research output: Contribution to journalArticle

63 Citations (Scopus)

Abstract

The GLUT3 facilitative glucose transporter protein was found to be expressed in rat L6 muscle cells. It was detected at both the myoblast and myotube stage. GLUT3 protein content per mg of total membrane protein increased significantly during L6 cell differentiation. Subcellular fractionation demonstrated that the GLUT3 protein was predominantly localized in plasma membrane-enriched fractions of either myoblasts or myotubes. Short-term exposure of L6 myotubes to IGF-I or insulin caused a redistribution of GLUT3 protein from an intracellular membrane fraction to the plasma membrane, without affecting total membrane GLUT3 protein content. Long-term exposure of L6 myotubes to IGF-I produced an increase of GLUT3 protein in total membranes and all subcellular membrane fractions, especially the plasma membrane. We propose that the GLUT3 glucose transporter may play an important role in glucose metabolism in developing muscle.

Original languageEnglish (US)
Pages (from-to)1129-1137
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume186
Issue number2
DOIs
StatePublished - Jul 31 1992

Fingerprint

Glucose Transporter Type 3
Facilitative Glucose Transport Proteins
Insulin-Like Growth Factor I
Muscle Cells
Skeletal Muscle Fibers
Muscle
Rats
Cells
Insulin
Cell membranes
Membranes
Myoblasts
Cell Membrane
Membrane Proteins
Intracellular Membranes
Subcellular Fractions
Fractionation
Metabolism
Cell Differentiation
Glucose

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "The GLUT3 facilitative glucose transporter protein was found to be expressed in rat L6 muscle cells. It was detected at both the myoblast and myotube stage. GLUT3 protein content per mg of total membrane protein increased significantly during L6 cell differentiation. Subcellular fractionation demonstrated that the GLUT3 protein was predominantly localized in plasma membrane-enriched fractions of either myoblasts or myotubes. Short-term exposure of L6 myotubes to IGF-I or insulin caused a redistribution of GLUT3 protein from an intracellular membrane fraction to the plasma membrane, without affecting total membrane GLUT3 protein content. Long-term exposure of L6 myotubes to IGF-I produced an increase of GLUT3 protein in total membranes and all subcellular membrane fractions, especially the plasma membrane. We propose that the GLUT3 glucose transporter may play an important role in glucose metabolism in developing muscle.",
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Detection of the GLUT3 facilitative glucose transporter in rat L6 muscle cells : Regulation by cellular differentiation, insulin and insulin-like growth factor-I. / Bilan, Philip J.; Mitsumoto, Yasuhide; Maher, Frances; Simpson, Ian A.; Klip, Amira.

In: Biochemical and Biophysical Research Communications, Vol. 186, No. 2, 31.07.1992, p. 1129-1137.

Research output: Contribution to journalArticle

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