Skeletal muscle glucose transport and metabolism are enhanced in transgenic mice overexpressing the Glut4 glucose transporter

P. A. Hansen, E. A. Gulve, B. A. Marshall, J. Gao, Jeffrey E. Pessin, J. O. Holloszy, M. Mueckler

Research output: Contribution to journalArticle

146 Citations (Scopus)

Abstract

Skeletal muscle glucose transport and metabolism were studied in a line of transgenic mice overexpressing the human Glut4 facilitative glucose transporter. Skeletal muscle Glut4 protein levels were increased 2-4-fold in transgenic animals relative to their nontransgenic litter mates. Glut4 overexpression increased total transport activity (measured with 1 mM 2- deoxy-D-glucose) in the isolated extensor digitorum brevis muscle in the presence of insulin; this increase was due to 1) an increase in basal glucose transport (0.8 ± 0.1 versus 0.5 ± 0.1 μmol · ml-1 · 20 min-1 in transgenic and control mice, respectively) and 2) an increase in insulin- stimulated transport (1.5 ± 0.1 versus 0.8 ± 0.1 μmol · ml-1 · 20 min-1 above basal transport in transgenic and control mice, respectively). Glut4 overexpression also increased glucose transport stimulated by muscle contractions. In addition, glycolysis and glucose incorporation into glycogen were enhanced in muscle isolated from transgenic mice compared to controls. These data demonstrate that Glut4 overexpression in skeletal muscle increases insulin- and contraction-stimulated glucose transport activity and glucose metabolism. These findings are consistent with the role of Glut4 as the primary mediator of transport stimulated by insulin or contractions.

Original languageEnglish (US)
Pages (from-to)1679-1684
Number of pages6
JournalJournal of Biological Chemistry
Volume270
Issue number4
StatePublished - 1995
Externally publishedYes

Fingerprint

Facilitative Glucose Transport Proteins
Metabolism
Transgenic Mice
Muscle
Skeletal Muscle
Glucose
Insulin
Muscles
Genetically Modified Animals
Muscle Proteins
Deoxyglucose
Glycolysis
Muscle Contraction
Glycogen
Animals
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Hansen, P. A., Gulve, E. A., Marshall, B. A., Gao, J., Pessin, J. E., Holloszy, J. O., & Mueckler, M. (1995). Skeletal muscle glucose transport and metabolism are enhanced in transgenic mice overexpressing the Glut4 glucose transporter. Journal of Biological Chemistry, 270(4), 1679-1684.

Skeletal muscle glucose transport and metabolism are enhanced in transgenic mice overexpressing the Glut4 glucose transporter. / Hansen, P. A.; Gulve, E. A.; Marshall, B. A.; Gao, J.; Pessin, Jeffrey E.; Holloszy, J. O.; Mueckler, M.

In: Journal of Biological Chemistry, Vol. 270, No. 4, 1995, p. 1679-1684.

Research output: Contribution to journalArticle

Hansen, PA, Gulve, EA, Marshall, BA, Gao, J, Pessin, JE, Holloszy, JO & Mueckler, M 1995, 'Skeletal muscle glucose transport and metabolism are enhanced in transgenic mice overexpressing the Glut4 glucose transporter', Journal of Biological Chemistry, vol. 270, no. 4, pp. 1679-1684.
Hansen, P. A. ; Gulve, E. A. ; Marshall, B. A. ; Gao, J. ; Pessin, Jeffrey E. ; Holloszy, J. O. ; Mueckler, M. / Skeletal muscle glucose transport and metabolism are enhanced in transgenic mice overexpressing the Glut4 glucose transporter. In: Journal of Biological Chemistry. 1995 ; Vol. 270, No. 4. pp. 1679-1684.
@article{d5048a26635940449d5d58d6e835c3ca,
title = "Skeletal muscle glucose transport and metabolism are enhanced in transgenic mice overexpressing the Glut4 glucose transporter",
abstract = "Skeletal muscle glucose transport and metabolism were studied in a line of transgenic mice overexpressing the human Glut4 facilitative glucose transporter. Skeletal muscle Glut4 protein levels were increased 2-4-fold in transgenic animals relative to their nontransgenic litter mates. Glut4 overexpression increased total transport activity (measured with 1 mM 2- deoxy-D-glucose) in the isolated extensor digitorum brevis muscle in the presence of insulin; this increase was due to 1) an increase in basal glucose transport (0.8 ± 0.1 versus 0.5 ± 0.1 μmol · ml-1 · 20 min-1 in transgenic and control mice, respectively) and 2) an increase in insulin- stimulated transport (1.5 ± 0.1 versus 0.8 ± 0.1 μmol · ml-1 · 20 min-1 above basal transport in transgenic and control mice, respectively). Glut4 overexpression also increased glucose transport stimulated by muscle contractions. In addition, glycolysis and glucose incorporation into glycogen were enhanced in muscle isolated from transgenic mice compared to controls. These data demonstrate that Glut4 overexpression in skeletal muscle increases insulin- and contraction-stimulated glucose transport activity and glucose metabolism. These findings are consistent with the role of Glut4 as the primary mediator of transport stimulated by insulin or contractions.",
author = "Hansen, {P. A.} and Gulve, {E. A.} and Marshall, {B. A.} and J. Gao and Pessin, {Jeffrey E.} and Holloszy, {J. O.} and M. Mueckler",
year = "1995",
language = "English (US)",
volume = "270",
pages = "1679--1684",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "4",

}

TY - JOUR

T1 - Skeletal muscle glucose transport and metabolism are enhanced in transgenic mice overexpressing the Glut4 glucose transporter

AU - Hansen, P. A.

AU - Gulve, E. A.

AU - Marshall, B. A.

AU - Gao, J.

AU - Pessin, Jeffrey E.

AU - Holloszy, J. O.

AU - Mueckler, M.

PY - 1995

Y1 - 1995

N2 - Skeletal muscle glucose transport and metabolism were studied in a line of transgenic mice overexpressing the human Glut4 facilitative glucose transporter. Skeletal muscle Glut4 protein levels were increased 2-4-fold in transgenic animals relative to their nontransgenic litter mates. Glut4 overexpression increased total transport activity (measured with 1 mM 2- deoxy-D-glucose) in the isolated extensor digitorum brevis muscle in the presence of insulin; this increase was due to 1) an increase in basal glucose transport (0.8 ± 0.1 versus 0.5 ± 0.1 μmol · ml-1 · 20 min-1 in transgenic and control mice, respectively) and 2) an increase in insulin- stimulated transport (1.5 ± 0.1 versus 0.8 ± 0.1 μmol · ml-1 · 20 min-1 above basal transport in transgenic and control mice, respectively). Glut4 overexpression also increased glucose transport stimulated by muscle contractions. In addition, glycolysis and glucose incorporation into glycogen were enhanced in muscle isolated from transgenic mice compared to controls. These data demonstrate that Glut4 overexpression in skeletal muscle increases insulin- and contraction-stimulated glucose transport activity and glucose metabolism. These findings are consistent with the role of Glut4 as the primary mediator of transport stimulated by insulin or contractions.

AB - Skeletal muscle glucose transport and metabolism were studied in a line of transgenic mice overexpressing the human Glut4 facilitative glucose transporter. Skeletal muscle Glut4 protein levels were increased 2-4-fold in transgenic animals relative to their nontransgenic litter mates. Glut4 overexpression increased total transport activity (measured with 1 mM 2- deoxy-D-glucose) in the isolated extensor digitorum brevis muscle in the presence of insulin; this increase was due to 1) an increase in basal glucose transport (0.8 ± 0.1 versus 0.5 ± 0.1 μmol · ml-1 · 20 min-1 in transgenic and control mice, respectively) and 2) an increase in insulin- stimulated transport (1.5 ± 0.1 versus 0.8 ± 0.1 μmol · ml-1 · 20 min-1 above basal transport in transgenic and control mice, respectively). Glut4 overexpression also increased glucose transport stimulated by muscle contractions. In addition, glycolysis and glucose incorporation into glycogen were enhanced in muscle isolated from transgenic mice compared to controls. These data demonstrate that Glut4 overexpression in skeletal muscle increases insulin- and contraction-stimulated glucose transport activity and glucose metabolism. These findings are consistent with the role of Glut4 as the primary mediator of transport stimulated by insulin or contractions.

UR - http://www.scopus.com/inward/record.url?scp=0028947967&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028947967&partnerID=8YFLogxK

M3 - Article

C2 - 7829503

AN - SCOPUS:0028947967

VL - 270

SP - 1679

EP - 1684

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 4

ER -