In vitro autoregulation of glucose utilization in rat soleus muscle

Diabetes ◽  
1987 ◽  
Vol 36 (9) ◽  
pp. 1041-1046 ◽  
Author(s):  
S. Sasson ◽  
D. Edelson ◽  
E. Cerasi
Keyword(s):  
Soleus Muscle ◽  
Glucose Utilization ◽  
Rat Soleus Muscle

scholarly journals Furosemide decreases the sensitivity of glucose transport to insulin in skeletal muscle in vitro

1998 ◽  
Vol 139 (1) ◽  
pp. 118-122 ◽  
Author(s):  
G Dimitriadis ◽  
B Leighton ◽  
M Parry-Billings ◽  
C Tountas ◽  
S Raptis ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glucose Transport ◽  
Soleus Muscle ◽  
Transport Process ◽  
Glucose Utilization ◽  
Glucose Disposal ◽  
Rat Soleus Muscle ◽  
Lactate Formation

The effects of the diuretic furosemide on the sensitivity of glucose disposal to insulin were investigated in rat soleus muscle in vitro. At basal levels of insulin, the rates of 3-O-methylglucose transport, 2-deoxyglucose phosphorylation and lactate formation were not affected significantly by furosemide (0.5 mmol/l). However, furosemide significantly decreased these rates at physiological and maximal levels of insulin. The contents of 2-deoxyglucose and glucose 6-phosphate in the presence of furosemide were not significantly different from those in control muscles at all levels of insulin studied. It is concluded that furosemide decreases the sensitivity of glucose utilization to insulin in skeletal muscle by directly inhibiting the glucose transport process.

In Vitro Autoregulation of Glucose Utilization in Rat Soleus Muscle

Diabetes ◽  
1987 ◽  
Vol 36 (9) ◽  
pp. 1041-1046 ◽  
Author(s):  
S. Sasson ◽  
D. Edelson ◽  
E. Cerasi
Keyword(s):  
Soleus Muscle ◽  
Glucose Utilization ◽  
Rat Soleus Muscle

scholarly journals The effects of amylin on carbohydrate metabolism in skeletal muscle in vitro and in vivo

1990 ◽  
Vol 269 (1) ◽  
pp. 19-23 ◽  
Author(s):  
B Leighton ◽  
E Foot
Keyword(s):  
Glucose Utilization ◽  
Glycogen Synthesis ◽  
Intraperitoneal Administration ◽  
Muscle Preparation ◽  
Glucose Incorporation ◽  
Rat Soleus Muscle ◽  
Lactate Formation ◽  
Human Amylin

1. The effects of synthetic human amylin on basal and insulin-stimulated (100 and 1000 microunits/ml) rates of lactate formation, glucose oxidation and glycogen synthesis were measured in the isolated rat soleus muscle preparation incubated in the presence of various concentrations of glucose (5, 11 and 22 mM). 2. The rate of glucose utilization was increased by about 2-fold by increasing the glucose concentration from 5 to 22 mM. 3. Synthetic human amylin (10 nM) significantly inhibited (by 46-56%) glycogen synthesis, irrespective of the concentration of insulin or glucose present in the incubation medium. 4. Amylin (10 nM) did not affect insulin-stimulated rates of 2-deoxy[3H]glucose transport and phosphorylation. 5. Intraperitoneal administration of insulin (100 micrograms/kg) to rats in vivo stimulated the rate of [U-14C]glucose incorporation into glycogen in the diaphragm by about 80-fold. This rate was decreased (by 28%) by co-administration of amylin (66 micrograms/kg).

Upregulation of HARP during in vitro myogenesis and rat soleus muscle regeneration

2004 ◽  
Vol 25 (1) ◽  
pp. 45-53 ◽  
Author(s):  
Danièle Caruelle ◽  
Zohra Mazouzi ◽  
Irene Husmann ◽  
Jean Delbé ◽  
Arlette Duchesnay ◽  
...  
Keyword(s):  
Soleus Muscle ◽  
Muscle Regeneration ◽  
Rat Soleus Muscle

Palmitic acid uptake by the rat soleus muscle in vitro

2001 ◽  
Vol 79 (4) ◽  
pp. 419-424 ◽  
Author(s):  
M Górecka ◽  
M Synak ◽  
L Budohoski ◽  
J Langfort ◽  
S Moskalewski ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Palmitic Acid ◽  
Soleus Muscle ◽  
Fatty Acid Uptake ◽  
Cellular Fatty Acid ◽  
Acid Uptake ◽  
Acid Complex ◽  
Rat Soleus Muscle

The rate of fatty acid uptake, oxidation, and deposition in skeletal muscles in relation to total and unbound to albumin fatty acids concentration in the medium were investigated in the incubated rat soleus muscle. An immunohistochemical technique was applied to demonstrate whether the albumin-bound fatty acid complex from the medium penetrates well within all areas of the muscle strips. It was found that the percentage of incorporation of palmitic acid into intramuscular lipids was fairly constant, independently of the fatty acid concentration in the medium, and amounted to 63–72% for triacylglycerols, 7–12% for diacylglycerols-monoacylglycerols, and 19–26% for phospholipids. Both palmitic acid incorporation into the muscle triacylglycerol stores and its oxidation to CO2closely correlated with an increase in both total and unbound to albumin fatty acid concentrations in the incubation medium. Under conditions of increased total but constant unbound to albumin palmitic acid concentrations, the incorporation of palmitic acid into triacylglycerols and its oxidation to CO2were also increased, but to a lower extent. This supports the hypothesis that the cellular fatty acid metabolism depends not only on the availability of fatty acids unbound to albumin, but also on the availability of fatty acids complexed to albumin.Key words: skeletal muscle, fatty acids, triacylglycerols, phospholipids.

scholarly journals Long term culture of rat soleus muscle in vitro

FEBS Letters ◽  
1990 ◽  
Vol 273 (1-2) ◽  
pp. 91-94 ◽  
Author(s):  
Pamela B. Stace ◽  
David R. Marchington ◽  
Alan L. Kerbey ◽  
Philip J. Randle
Keyword(s):  
Soleus Muscle ◽  
Long Term Culture ◽  
Rat Soleus Muscle

scholarly journals Effects of insulin and phorbol esters on MARCKS (myristoylated alanine-rich C-kinase substrate) phosphorylation (and other parameters of protein kinase C activation) in rat adipocytes, rat soleus muscle and BC3H-1 myocytes

1993 ◽  
Vol 295 (1) ◽  
pp. 155-164 ◽  
Author(s):  
T P Arnold ◽  
M L Standaert ◽  
H Hernandez ◽  
J Watson ◽  
H Mischak ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Soleus Muscle ◽  
Plasma Membranes ◽  
Phorbol Esters ◽  
Kinase Substrate ◽  
Rat Adipocytes ◽  
Kinase C ◽  
Rat Soleus Muscle

To evaluate the question of whether or not insulin activates protein kinase C (PKC), we compared the effects of insulin and phorbol esters on the phosphorylation of the PKC substrate, i.e. myristoylated alanine-rich C-kinase substrate (MARCKS). In rat adipocytes, rat soleus muscle and BC3H-1 myocytes, maximally effective concentrations of insulin and phorbol esters provoked comparable, rapid, 2-fold (on average), non-additive increases in the phosphorylation of immunoprecipitable MARCKS. These effects of insulin and phorbol esters on MARCKS phosphorylation in intact adipocytes and soleus muscles were paralleled by similar increases in the phosphorylation of an exogenous, soluble, 85 kDa PKC substrate (apparently a MARCKS protein) during incubation of post-nuclear membrane fractions in vitro. Increases in the phosphorylation of this 85 kDa PKC substrate in vitro were also observed in assays of both plasma membranes and microsomes obtained from rat adipocytes that had been treated with insulin or phorbol esters. These insulin-induced increases in PKC-dependent phosphorylating activities of adipocyte plasma membrane and microsomes were associated with increases in membrane contents of diacylglycerol, PKC-beta 1 and PKC-beta 2. Our findings suggest that insulin both translocates and activates PKC in rat adipocytes, rat soleus muscles and BC3H-1 myocytes.

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