Inositol 1,4,5-Trisphosphate But Not Ryanodine-Receptor Agonists Induces Calcium Release from Rat Liver Golgi Apparatus Membrane Vesicles

2000 ◽  
Vol 177 (3) ◽  
pp. 243-249 ◽  
Author(s):  
A. Surroca ◽  
D. Wolff
1988 ◽  
Vol 256 (2) ◽  
pp. 363-369 ◽  
Author(s):  
S B Shears ◽  
W H Evans ◽  
C J Kirk ◽  
R H Michell

Previous studies have shown that most of the inositol 1,4,5-trisphosphate/inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activity of rat hepatocytes is associated with the plasma membrane [Shears, Parry, Tang, Irvine, Michell & Kirk (1987) Biochem. J. 246, 139-147]. We now show that the specific activity of this enzyme is highest in the bile-canalicular domain of the plasma membrane, at the opposite pole of the hepatocyte from the presumed site of receptor-mediated formation of inositol 1,4,5-trisphosphate. In intact hepatocytes and in sealed membrane vesicles originating from the bile-canalicular domain of the plasma membrane, the 5-phosphatase activity was mostly latent and therefore located at the cytoplasmic surface. A substantial amount of 5-phosphatase was also found in rat liver endosomal fractions, particularly a ‘late’ endosomal subfraction, indicating that this enzyme may be transported between the sinusoidal plasma membrane and other cellular membranes.


1987 ◽  
Vol 931 (2) ◽  
pp. 251-254 ◽  
Author(s):  
Gergely L. Lukács ◽  
György Hajnóczky ◽  
László Hunyady ◽  
András Spät

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