Ultrastructural studies of the intracellular translocation of endocytosed alpha-foetoprotein (AFP) by cytochemistry and of the uptake of 3H-arachidonic acid bound to AFP by autoradiography in rat rhabdomyosarcoma cells

J Cell Physiol. 1986 Sep;128(3):389-96. doi: 10.1002/jcp.1041280307.

Abstract

A covalent conjugate of alpha-foetoprotein (AFP) and horseradish peroxidase (HRP) has been used to follow, at the ultrastructural level, the pathway of AFP uptake and translocation in a rat rhabdomyosarcoma cell line. The cells were incubated for several times at 4 degrees C and/or 37 degrees C, and fixed. AFP-HRP was found to enter the cells via coated pits and receptosomes and to move to tubular elements of the trans-reticular portion of the Golgi. Some observations suggest that AFP can be recycled back to the cell surface. On the other hand, the cells were incubated with a noncovalent conjugate of AFP and 3H-arachidonic acid [3H-(20:4)], and the uptake of the fatty acid molecules studied by ultrastructural autoradiography. The cytoplasmic labeling, very low after an incubation in the presence of [3H-(20:4)]-AFP for 2 hours at 4 degrees C, increased rapidly after transfer of the cells for 5 minutes to 37 degrees C. These observations support the hypothesis that AFP plays a role in the intracellular delivery of polyunsaturated fatty acids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arachidonic Acid
  • Arachidonic Acids / metabolism*
  • Endocytosis*
  • Horseradish Peroxidase
  • Rats
  • Receptors, Cell Surface / analysis
  • Receptors, Peptide*
  • Rhabdomyosarcoma / metabolism
  • Rhabdomyosarcoma / ultrastructure*
  • alpha-Fetoproteins / metabolism*

Substances

  • Arachidonic Acids
  • Receptors, Cell Surface
  • Receptors, Peptide
  • alpha-Fetoproteins
  • alpha-fetoprotein receptor, rat
  • Arachidonic Acid
  • Horseradish Peroxidase