isolated fat cells
Recently Published Documents


TOTAL DOCUMENTS

222
(FIVE YEARS 0)

H-INDEX

33
(FIVE YEARS 0)

2001 ◽  
Vol 280 (6) ◽  
pp. R1772-R1780 ◽  
Author(s):  
Iordanes Karagiannides ◽  
Tamara Tchkonia ◽  
Deborah E. Dobson ◽  
Claire M. Steppan ◽  
Patrice Cummins ◽  
...  

Fat mass, adipocyte size and metabolic responsiveness, and preadipocyte differentiation decrease between middle and old age. We show that expression of CCAAT/enhancer binding protein (C/EBP)-α, a key regulator of adipogenesis and fat cell function, declined substantially with aging in differentiating preadipocytes cultured under identical conditions from rats of various ages. Overexpression of C/EBPα in preadipocytes cultured from old rats restored capacity to differentiate into fat cells, indicating that downstream differentiation-dependent genes maintain responsiveness to regulators of adipogenesis. C/EBPα-expression also decreased with age in fat tissue from three different depots and in isolated fat cells. The overall level of C/EBPβ, which modulates C/EBPα-expression, did not change with age, but the truncated, dominant-negative C/EBPβ-liver inhibitory protein (LIP) isoform increased in cultured preadipocytes and isolated fat cells. Overexpression of C/EBPβ-LIP in preadipocytes from young rats impaired adipogenesis. C/EBPδ, which acts with full-length C/EBPβ to enhance adipogenesis, decreased with age. Thus processes intrinsic to adipose cells involving changes in C/EBP family members contribute to impaired adipogenesis and altered fat tissue function with aging. These effects are potentially reversible.


1991 ◽  
Vol 279 (2) ◽  
pp. 545-551 ◽  
Author(s):  
T A Diggle ◽  
C Schmitz-Peiffer ◽  
A C Borthwick ◽  
G I Welsh ◽  
R M Denton

Casein kinase 2 activity as measured by phosphorylation of the peptide substrate Arg-Arg-Arg-Glu-Glu-Glu-Thr-Glu-Glu-Glu is increased by about 50% in extracts from insulin-treated epididymal fat-pads or isolated fat-cells after purification by Mono Q chromatography. Insulin acts to increase the Vmax. of the kinase. An acid-soluble protein with an apparent subunit molecular mass of about 22 kDa appears to be a substrate for casein kinase 2. The protein possesses a number of properties in common with the acid-soluble heat-stable 22 kDa protein which exhibits increased phosphorylation in rat adipose tissue exposed to insulin.


1991 ◽  
Vol 275 (3) ◽  
pp. 597-600 ◽  
Author(s):  
B Vogt ◽  
J Mushack ◽  
E Seffer ◽  
H U Häring

Insulin stimulates glucose transport in isolated fat cells by activation of glucose transporters in the plasma membranes and through translocation of the glucose transporter sub-types GLUT4 (insulin-regulatable) and GLUT1 (HepG2 transporter). The protein kinase C-stimulating phorbol ester phorbol 12-myristate 13-acetate (PMA) is able to mimic partially the effect of insulin on glucose transport, apparently through stimulation of carrier translocation. In order to ascertain whether protein kinase C is involved in the translocation signal to both carrier sub-types, we determined the effect of PMA on the subcellular distribution of GLUT1 and GLUT4 by immunoblotting with specific antibodies directed against these transporters. Isolated rat fat cells (4 x 10(6) cells/ml) were stimulated for 20 min with insulin (6 nM) or PMA (1 nM). 3-O-Methylglucose transport was determined and plasma membranes and low-density microsomes were prepared for Western blotting. 3-O-Methylglucose transport was stimulated 8-9-fold by insulin, and 3-4-fold by PMA (basal, 5.6 +/- 2.3%; insulin, 43.6 +/- 7.3%; PMA, 18.4 +/- 4.9%, n = 9). PMA was able to increase the amount of GLUT4 in the plasma membrane fraction by 2.5(+/- 0.9)-fold (n = 6) whereas insulin stimulation was 4.4(+/- 1.7)-fold (n = 6), paralleled by a corresponding decrease of transport in the low-density microsomes (insulin, 50 +/- 5% of basal; PMA, 63 +/- 11% of basal, n = 6). Although PMA regulates the translocation of GLUT4, it has no effect on GLUT1 in the same cell fractions (increase in plasma membranes: insulin, 1.7 +/- 0.5-fold; PMA, 0.91 +/- 0.1-fold, n = 4; decrease in low-density microsomes: insulin, 53 +/- 11% of basal; PMA, 101 +/- 5% of basal, n = 4). These data are in favour of a role for protein kinase C in signal transduction to GLUT4 but not to GLUT1 in fat cells.


1989 ◽  
Vol 4 (2) ◽  
pp. 142-148
Author(s):  
Bong Yun Cha ◽  
Kwan Su Hong ◽  
Kwang Woo Lee ◽  
Ho Young Son ◽  
Sung Ku Kang

Diabetes ◽  
1989 ◽  
Vol 38 (2) ◽  
pp. 237-243 ◽  
Author(s):  
F. D. Newby ◽  
F. Bayo ◽  
S. V. Thacker ◽  
M. Sykes ◽  
M. Digirolamo

Diabetes ◽  
1989 ◽  
Vol 38 (2) ◽  
pp. 237-243 ◽  
Author(s):  
F. D. Newby ◽  
F. Bayo ◽  
S. V. Thacker ◽  
M. Sykes ◽  
M. DiGirolamo

1986 ◽  
Vol 61 (4) ◽  
pp. 1546-1551 ◽  
Author(s):  
K. A. Kenno ◽  
J. L. Durstine ◽  
R. E. Shepherd

Fat cells were isolated from sedentary and exercise trained female Sprague-Dawley rats and cyclic AMP phosphodiesterase (cyclic AMP-PDE) activities were determined from crude homogenates of the fat cells in the whole homogenate, P5, P48, and S48 fractions. Exercise training resulted in a significant increase in the mean specific activity of cyclic AMP-PDE (pmol X min-1 X mg-1) from the whole homogenate and S48 fraction at cyclic AMP concentrations of 4, 8, and 16 microM and in the P48 fraction at 8 and 16 microM cyclic AMP. Cyclic AMP-PDE kinetic plots according to Lineweaver-Burk for the calculation of Michaelis constants (Km) and maximum enzyme velocities (Vmax) were nonlinear, indicating both a low and high enzyme form. The Michaelis constants were significantly lower in trained rats than those of its control for the high Km form of cyclic AMP-PDE in the whole and soluble fractions and for the low Km form of the P5 particulate fraction. The Vmax of the high Km form of the P48 particulate fraction from trained animals was also significantly higher than that found in its control. Phosphodiesterase inhibition by methylxanthines in the various fractions was similar in both trained and sedentary animals. These changes in specific activity, Michaelis constants, and Vmax of cyclic AMP-PDE from crude homogenates of isolated fat cells from exercise trained animals may account for the decreased intracellular levels of cyclic AMP following catecholamine stimulation of isolated fat cells from trained rats.


Sign in / Sign up

Export Citation Format

Share Document