Degradation of endocytosed proteins is unaltered in senescent human fibroblasts

Cell Biol Int Rep. 1988 Oct;12(10):885-94. doi: 10.1016/0309-1651(88)90052-5.

Abstract

We compared the abilities of young and senescent fibroblasts to take up and degrade [3H]ribonuclease A (native and oxidized), [3H]ribonuclease4-13, [3H]hemoglobin, [3H]glyceraldehyde-3-phosphate dehydrogenase, [3H]beta-galactosidase, [3H]glycogen phosphorylase, and [125I]serum albumin. The endocytic uptake of these proteins ranged from fluid-phase to predominantly absorptive. Intralysosomal degradation rates of the different endocytosed proteins varied by an order of magnitude, but in no case was there a difference between cultures of young and senescent fibroblasts.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aging / metabolism*
  • Cells, Cultured
  • Endocytosis
  • Fibroblasts / metabolism*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism
  • Glyceraldehyde-3-Phosphate Dehydrogenases / pharmacokinetics
  • Hemoglobins / metabolism
  • Hemoglobins / pharmacokinetics
  • Humans
  • Lysosomes / metabolism
  • Phosphorylases / metabolism
  • Phosphorylases / pharmacokinetics
  • Proteins / metabolism*
  • Proteins / pharmacokinetics
  • Ribonuclease, Pancreatic / metabolism
  • Ribonuclease, Pancreatic / pharmacokinetics
  • Ribonucleases / metabolism
  • Ribonucleases / pharmacokinetics
  • Serum Albumin / metabolism
  • Serum Albumin / pharmacokinetics
  • Sucrose / metabolism
  • Sucrose / pharmacokinetics
  • beta-Galactosidase / metabolism
  • beta-Galactosidase / pharmacokinetics

Substances

  • Hemoglobins
  • Proteins
  • Serum Albumin
  • Sucrose
  • Glyceraldehyde-3-Phosphate Dehydrogenases
  • Phosphorylases
  • Ribonucleases
  • Ribonuclease, Pancreatic
  • beta-Galactosidase