Biosynthesis and turnover of the mannose 6-phosphate receptor in cultured Chinese hamster ovary cells

J Biol Chem. 1983 Jun 10;258(11):7121-8.

Abstract

The natural history of the mannose 6-phosphate receptor was examined by radiolabeling cells in monolayers or in suspension; the receptor was isolated by immuno- or affinity precipitation followed by polyacrylamide gel electrophoresis. The receptor was found to contain asparagine-linked oligosaccharide chains and phosphorylated serine residues. Newly made receptor was sensitive to endo-beta-N-acetylglucosaminidase H (endo-H) and was slowly converted to a mature endo-H resistant form; phosphate was found on the mature receptor only. The receptor had an apparent molecular weight of 215,000 at all times, as determined under reducing and denaturing conditions; unreduced receptor had a greater electrophoretic mobility, suggesting the presence of intrachain disulfide linkages. The synthesis of immunoreactive receptor occurred with a lag of 50 min and of functional receptor with a lag of 70 min, indicating a requirement for some post-translational event(s) for acquisition of immunoreactivity and binding activity. Maturation of asparagine-linked oligosaccharides was not the requisite modification, since endo-H sensitive or deglycosylated receptor bound to both antibody and to insoluble phosphomannan; however, much less immunoreactive and functional receptor was detected in the presence of tunicamycin. Immunoprecipitable [3H]leucine-labeled receptor was degraded with a t1/2 of 16 h and 6 h for cells in monolayers and suspension, respectively, whereas 32P was lost with a corresponding t1/2 of 2.3 and 4 h. A pool of cell surface mannose 6-phosphate receptor was identified by separation on Percoll gradients as well as by iodination of cells with 125I; receptor in this pool was resistant to endo-H and had a t1/2 similar to that of the total [3H]leucine-labeled receptor, even in the presence of a saturating concentration of ligand. During endocytosis, ligand (beta-galactosidase) and 125I-receptor separated, the ligand accumulating within lysosomes. These results are consistent with current concepts of recycling of the mannose 6-phosphate receptor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Cricetinae
  • Cricetulus
  • Female
  • Galactose / metabolism
  • Kinetics
  • Leucine / metabolism
  • Mannose / metabolism
  • Ovary
  • Phosphorus Radioisotopes
  • Receptor, IGF Type 2
  • Receptors, Cell Surface / metabolism*
  • Tritium

Substances

  • Phosphorus Radioisotopes
  • Receptor, IGF Type 2
  • Receptors, Cell Surface
  • Tritium
  • Leucine
  • Mannose
  • Galactose