scholarly journals Immunocytochemical localization of fat/muscle-type glucose transporter (GLUT4) in the rat skeletal muscle: Effect of insulin treatment.

1992 ◽  
Vol 25 (6) ◽  
pp. 689-696 ◽  
Author(s):  
KUNIAKI TAKATA ◽  
OSAMU EZAKI ◽  
HIROSHI HIRANO
Keyword(s):  
Skeletal Muscle ◽  
Glucose Transporter ◽  
Insulin Treatment ◽  
Immunocytochemical Localization ◽  
Muscle Type ◽  
Rat Skeletal Muscle ◽  
Glucose Transporter Glut4

scholarly journals Phosphatidylinositol 4-kinase, but not phosphatidylinositol 3-kinase, is present in GLUT4-containing vesicles isolated from rat skeletal muscle

1998 ◽  
Vol 335 (2) ◽  
pp. 351-356 ◽  
Author(s):  
S⊘ren KRISTIANSEN ◽  
Toolsie RAMLAL ◽  
Amira KLIP
Keyword(s):  
Skeletal Muscle ◽  
Glucose Transporter ◽  
Kinase Activity ◽  
Surface Membrane ◽  
Fold Increase ◽  
Rat Skeletal Muscle ◽  
Membrane Compartment ◽  
Intracellular Storage ◽  
Glucose Transporter Glut4 ◽  
Adipose Cells

Insulin stimulates the rate of glucose transport into muscle and adipose cells by translocation of glucose transporter (GLUT4)-containing vesicles from an intracellular storage pool to the surface membrane. This event is mediated through the insulin receptor substrates (IRSs), which in turn activate phosphatidylinositol (PI) 3-kinase isoforms. It has been suggested that insulin causes attachment of PI 3-kinases to the intracellular GLUT4-containing vesicles in rat adipose cells. Furthermore, it has also been shown that GLUT4-containing vesicles in adipose cells contain a PI 4-kinase. In the present study we investigate whether GLUT4-containing vesicles isolated from rat skeletal muscle display PI 3-kinase and/or PI 4-kinase activities. Insulin stimulation caused a rapid increase (5–15-fold increase compared with control) in the intracellular cytosolic IRS-1-associated PI-3 kinase activity. This PI 3-kinase activity was also present in a membrane preparation containing the insulin-regulatable pool of GLUT4 transporters. However, when GLUT4-containing vesicles were isolated by immunoprecipitation from basal and insulin-stimulated (3 min) skeletal muscle, the vesicles displayed PI 4-kinase, but not PI 3-kinase, activity. Insulin did not regulate the PI 4-kinase activity in the GLUT4-containing vesicles. In conclusion, GLUT4-containing vesicles from rat skeletal muscle contain a PI 4-kinase, but not a PI 3-kinase. It is suggested that, in skeletal muscle, insulin causes activation of the IRS/PI 3-kinase complex in an intracellular membrane compartment associated closely with the GLUT4-containing vesicles, but not in the GLUT4-containing vesicles themselves.

Regulation of glucose transporter GLUT-4 and hexokinase II gene transcription by insulin and epinephrine

1997 ◽  
Vol 273 (4) ◽  
pp. E682-E687 ◽  
Author(s):  
Jared P. Jones ◽  
G. Lynis Dohm
Keyword(s):  
Skeletal Muscle ◽  
Gene Transcription ◽  
Glucose Transporter ◽  
Male Rats ◽  
Rat Skeletal Muscle ◽  
Hexokinase Ii ◽  
Epinephrine Infusion ◽  
Glut 4 ◽  
Gastrocnemius Muscles

Transport of glucose across the plasma membrane by GLUT-4 and subsequent phosphorylation of glucose by hexokinase II (HKII) constitute the first two steps of glucose utilization in skeletal muscle. This study was undertaken to determine whether epinephrine and/or insulin regulates in vivo GLUT-4 and HKII gene transcription in rat skeletal muscle. In the first experiment, adrenodemedullated male rats were fasted 24 h and killed in the control condition or after being infused for 1.5 h with epinephrine (30 μg/ml at 1.68 ml/h). In the second experiment, male rats were fasted 24 h and killed after being infused for 2.5 h at 1.68 ml/h with saline or glucose (625 mg/ml) or insulin (39.9 μg/ml) plus glucose (625 mg/ml). Nuclei were isolated from pooled quadriceps, tibialis anterior, and gastrocnemius muscles. Transcriptional run-on analysis indicated that epinephrine infusion decreased GLUT-4 and increased HKII transcription compared with fasted controls. Both glucose and insulin plus glucose infusion induced increases in GLUT-4 and HKII transcription of twofold and three- to fourfold, respectively, compared with saline-infused rats. In conclusion, epinephrine and insulin may regulate GLUT-4 and HKII genes at the level of transcription in rat skeletal muscle.

scholarly journals The GLUT4 glucose transporter and the α 2 subunit of the Na+ ,K+ -ATPase do not localize to the same intracellular vesicles in rat skeletal muscle

FEBS Letters ◽  
1995 ◽  
Vol 366 (2-3) ◽  
pp. 109-114 ◽  
Author(s):  
Louis Lavoie ◽  
Lijing He ◽  
Toolsie Ramlal ◽  
Cameron Ackerley ◽  
André Marette ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glucose Transporter ◽  
Rat Skeletal Muscle ◽  
Intracellular Vesicles

Long‐term insulin treatment leads to a change in myosin heavy chain fiber distribution in OLETF rat skeletal muscle

2018 ◽  
Vol 120 (2) ◽  
pp. 2404-2412 ◽  
Author(s):  
Oak‐Kee Hong ◽  
Yoon‐Hee Choi ◽  
Hyuk‐Sang Kwon ◽  
Hee‐Kyoung Jeong ◽  
Jang‐Won Son ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Insulin Treatment ◽  
Fiber Distribution ◽  
Rat Skeletal Muscle ◽  
Oletf Rat

In vivo effect of Trigonella foenum graecum on the expression of pyruvate kinase, phosphoenolpyruvate carboxykinase, and distribution of glucose transporter (GLUT4) in alloxan-diabetic rats

2006 ◽  
Vol 84 (6) ◽  
pp. 647-654 ◽  
Author(s):  
Sameer Mohammad ◽  
Asia Taha ◽  
Kamal Akhtar ◽  
R.N.K. Bamezai ◽  
Najma Zaheer Baquer
Keyword(s):  
Skeletal Muscle ◽  
Pyruvate Kinase ◽  
Plasma Glucose ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Glucose Transporter ◽  
Diabetic Rats ◽  
Altered Expression ◽  
Glucose Levels ◽  
Glucose Transporter Glut4

Plasma glucose levels are maintained by a precise balance between glucose production and its use. Liver pyruvate kinase (PK) and phosphoenolpyruvate carboxykinase (PEPCK), 2 key enzymes of glycolysis and gluconeogenesis, respectively, play a crucial role in this glucose homeostasis along with skeletal muscle glucose transporter (GLUT4). In the diabetic state, this balance is disturbed owing to the absence of insulin, the principal factor controlling this regulation. In the present study, alloxan-diabetic animals having high glucose levels of more than 300 mmol/L have been taken and the administration of Trigonella seed powder (TSP) to the diabetic animals was assessed for its effect on the expression of PK and PEPCK in liver and GLUT4 distribution in skeletal muscle of alloxan-diabetic rats. TSP treatment to the diabetic animals resulted in a marked decrease in the plasma glucose levels. Trigonella treatment partially restored the altered expression of PK and PEPCK. TSP treatment also corrected the alterations in the distribution of GLUT4 in the skeletal muscle.

scholarly journals Phosphorylation of the adipose/muscle-type glucose transporter (GLUT4) and its relationship to glucose transport activity

1992 ◽  
Vol 285 (1) ◽  
pp. 223-228 ◽  
Author(s):  
A Schürmann ◽  
G Mieskes ◽  
H G Joost
Keyword(s):  
Protein Kinase ◽  
Glucose Transport ◽  
Plasma Membranes ◽  
Glucose Transporter ◽  
Low Density ◽  
Transport Activity ◽  
Muscle Type ◽  
Kinase C ◽  
Glucose Transporter Glut4

The effects of protein phosphorylation and dephosphorylation on glucose transport activity reconstituted from adipocyte membrane fractions and its relationship to the phosphorylation state of the adipose/muscle-type glucose transporter (GLUT4) were studied. In vitro phosphorylation of membranes in the presence of ATP and protein kinase A produced a stimulation of the reconstituted glucose transport activity in plasma membranes and low-density microsomes (51% and 65% stimulation respectively), provided that the cells had been treated with insulin prior to isolation of the membranes. Conversely, treatment of membrane fractions with alkaline phosphatase produced an inhibition of reconstituted transport activity. However, in vitro phosphorylation catalysed by protein kinase C failed to alter reconstituted glucose transport activity in membrane fractions from both basal and insulin-treated cells. In experiments run under identical conditions, the phosphorylation state of GLUT4 was investigated by immunoprecipitation of glucose transporters from membrane fractions incubated with [32P]ATP and protein kinases A and C. Protein kinase C stimulated a marked phosphate incorporation into GLUT4 in both plasma membranes and low-density microsomes. Protein kinase A, in contrast to its effect on reconstituted glucose transport activity, produced a much smaller phosphorylation of the GLUT4 in plasma membranes than in low-density microsomes. The present data suggest that glucose transport activity can be modified by protein phosphorylation via an insulin-dependent mechanism. However, the phosphorylation of the GLUT4 itself was not correlated with changes in its reconstituted transport activity.

scholarly journals Development of insulin sensitivity in rat skeletal muscle Studies of glucose transporter and insulin receptor mRNA levels

FEBS Letters ◽  
1992 ◽  
Vol 301 (1) ◽  
pp. 69-72 ◽  
Author(s):  
Shona Wallace ◽  
Gillian Campbell ◽  
Rachel Knott ◽  
Gwyn W. Gould ◽  
John Hesketh
Keyword(s):  
Skeletal Muscle ◽  
Insulin Sensitivity ◽  
Insulin Receptor ◽  
Glucose Transporter ◽  
Mrna Levels ◽  
Rat Skeletal Muscle ◽  
Receptor Mrna
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