PROTEIN KINASE ACTIVITY ASSOCIATED WITH THE FAT CELL PLASMA MEMBRANE

1981 ◽  
Vol 9 (2) ◽  
pp. 232P-232P
Author(s):  
G. J. Belsham ◽  
R. W. Brownsey ◽  
R. M. Denton
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Fat Cell ◽  
Cell Plasma Membrane ◽  
Cell Plasma

scholarly journals Effects of protein kinase C and phosphoprotein phosphatase modulators on Ehrlich cell plasma membrane redox system activity

1996 ◽  
Vol 1313 (2) ◽  
pp. 157-160 ◽  
Author(s):  
Antonio del Castillo-Olivares ◽  
Alicia Esteban del Valle ◽  
Javier Márquez ◽  
Ignacio Núñez de Castro ◽  
Miguel Angel Medina
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Redox System ◽  
Cell Plasma Membrane ◽  
System Activity ◽  
Phosphoprotein Phosphatase ◽  
Ehrlich Cell ◽  
Kinase C ◽  
Cell Plasma

scholarly journals The properties and extracellular location of 5′-nucleotidase of the rat fat-cell plasma membrane

1975 ◽  
Vol 146 (3) ◽  
pp. 625-633 ◽  
Author(s):  
A C Newby ◽  
J P Luzio ◽  
C N Hales
Keyword(s):  
Plasma Membrane ◽  
Fat Cells ◽  
Isolated Fat Cells ◽  
Fat Cell ◽  
Cell Plasma Membrane ◽  
Intact Cells ◽  
Low Concentrations ◽  
Cell Plasma ◽  
Atp Analogues ◽  
Extracellular Location

1. A phosphohydrolase specific for 5′-nucleotides was characterized by using a particulate fraction from isolated fat-cells. 2. The activity of intact cells towards 5′-AMP was studied. 3. The activity in either situation had the same KM for AMP (45 muM) and was inhibited by low concentrations of ATP (less than 50 muM), but less potently by the ATP analogues AMP-P(CH2)P(adenylyl (β γ-methylene)diphosphonate) and AMP-P)NH)P (adenylylimidodiphosphate). 4. Homogenization of intact fat-cells caused no increase in activity and at least 85% of the activity was recovered in the particulate preparation. 5. The preparation of fat-cells used in this work was not freely permeable to AMP. 6. The ability of intact fat-cells to hydrolyse AMP implies that 5′-nucleotidase is an ectoenzyme in fat-cells. 7. Concentrations of ATP 100 times lower than intracellular concentrations inhibit the enzyme when added extracellularly to intact fat-cells, implying that this effect is also medicated at the extracellular face of the membrane. 8. Antibodies raised to whole liver cells and whole fat-cells inhibit 5′-nucleotidase in intact cells. 9. Incubation of intact fat-cells with adrenaline (1 mug/ml) or insulin (50 mui.u./ml) failed to alter the KM or Vmax. of the enzyme.

Thiol-Dependent Subunit Interactions of a Major Fat Cell Plasma Membrane Glycoprotein

1978 ◽  
Vol 2 (1) ◽  
pp. 97-115 ◽  
Author(s):  
Carlene A. Hawksley ◽  
Nancy Z. Guggenheim ◽  
Michael P. Czech
Keyword(s):  
Plasma Membrane ◽  
Membrane Glycoprotein ◽  
Fat Cell ◽  
Subunit Interactions ◽  
Cell Plasma Membrane ◽  
Cell Plasma

scholarly journals Selective extraction of an intrinsic fat-cell plasma-membrane glycoprotein by Triton X-100

FEBS Letters ◽  
1977 ◽  
Vol 83 (1) ◽  
pp. 71-75 ◽  
Author(s):  
Carla J. Greenbaum ◽  
Michael F. Shanahan ◽  
Dennis J. Pillion ◽  
Michael P. Czech
Keyword(s):  
Plasma Membrane ◽  
Selective Extraction ◽  
Membrane Glycoprotein ◽  
Fat Cell ◽  
Cell Plasma Membrane ◽  
Cell Plasma ◽  
Triton X

scholarly journals Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation

1996 ◽  
Vol 315 (3) ◽  
pp. 709-713 ◽  
Author(s):  
Stephen R. JAMES ◽  
C. Peter DOWNES ◽  
Roy GIGG ◽  
Simon J. A. GROVE ◽  
Andrew B. HOLMES ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Surface Plasmon Resonance ◽  
Protein Kinase ◽  
Association Constant ◽  
Kinase Activity ◽  
Specific Binding ◽  
Protein Kinase Activity ◽  
L6 Myotubes ◽  
Subsequent Activation ◽  
Phosphoinositide 3 Kinase

Recent evidence has suggested that activation of phosphoinositide 3-kinase (PI 3-kinase) is required for the activation of Akt-1 by growth factors and insulin. Here we demonstrate by two independent methods that Akt-1 from L6 myotubes binds to PtdIns(3,4,5)P3, PtdIns(3,4)P2 and PtdIns(4,5)P2 when presented against a background of phosphatidylserine (PtdSer) or a 1:1 mixture of PtdSer and phosphatidylcholine (PtdCho). No binding was observed with the lipids PtdIns(3,5)P2, PtdIns4P and PtdIns3P or background lipids. Activated, hyperphosphorylated forms of Akt-1 from insulin-stimulated L6 myotubes bound to PtdIns(3,4,5)P3 in a similar manner as inactive Akt-1. Quantitative analysis using surface plasmon resonance showed that the equilibrium association constant for the binding of Akt-1 to PtdIns(3,4,5)P3 was submicromolar and that PtdIns(3,4)P2 and PtdIns(4,5)P2 bound to Akt-1 with 3- and 6-fold lower affinities respectively. Interaction of Akt-1 with PtdIns(3,4,5)P3 did not activate the protein kinase activity, either before or after incubation with MgATP. A model is presented in which PtdIns(3,4,5)P3 may prime Akt-1 for activation by another protein kinase, perhaps by recruiting it to the plasma membrane.

Topography of the fat cell plasma membrane

Biochemistry ◽  
1973 ◽  
Vol 12 (19) ◽  
pp. 3597-3601 ◽  
Author(s):  
Michael P. Czech ◽  
William S. Lynn
Keyword(s):  
Plasma Membrane ◽  
Fat Cell ◽  
Cell Plasma Membrane ◽  
Cell Plasma
Sign in / Sign up

Export Citation Format

Share Document