Receptor-mediated endocytosis of apamin by liver cells
Article first published online: 3 MAR 2005
European Journal of Biochemistry
Volume 163, Issue 2, pages 267–273, March 1987
How to Cite
STRONG, P. N. and EVANS, W. H. (1987), Receptor-mediated endocytosis of apamin by liver cells. European Journal of Biochemistry, 163: 267–273. doi: 10.1111/j.1432-1033.1987.tb10797.x
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received July 22/October 27, 1986) – EJB 86 0778
The binding and uptake of the bee venom toxin apamin, by guinea-pig and rat liver were studied.
Guinea-pig liver plasma membranes contain inhibitable, high-affinity binding sites for [125I]monoiodoapamin: Kd= 12.6±0.8 pM (SE); Bmax= 4.2±0.2 fmol/mg protein. No binding sites for [125I]monoiodoapamin on rat liver plasma membranes were detected in agreement with the absence of a physiological response to the toxin by rat hepatocytes.
[125I]Monoiodoapamin, injected into the portal vein of guinea-pigs, was recovered in an undegraded form in a liver endosome fraction. The uptake of [125I]monoiodoapamin by rat livers was less than 4% of that taken up by guinea-pig livers and there was little evidence of radiolabelled toxin appearing in isolated rat endocytic vesicles.
Inhibitable, high-affinity binding sites for [125I]monoiodoapamin were also identified on isolated guinea-pig liver endosomal membranes; Kd= 10.6±3.3 pM; Bmax= 2.5±0.6 fmol/mg protein. No inhibitable apamin binding sites were detected on rat endosomal membranes.
Plasma membranes and endosomal membranes isolated from guinea-pig liver showed a similar spectrum of polypeptides to that previously reported for plasma membranes and endosomal membranes isolated from rat liver. The enzymatic composition of guinea-pig endosomes was also similar to that previously reported for rat endosomes.
The results indicate that apamin was internalised by receptor-mediated endocytosis by guinea-pig liver cells in an analogous manner to that already shown for a variety of endogenous ligands.