Identification of two molecular chaperons (HSX70, HSC70) in mature human erythrocytes

Exp Cell Res. 1991 Aug;195(2):556-9. doi: 10.1016/0014-4827(91)90412-n.

Abstract

Two-dimensional gel electrophoresis of cytosolic proteins from mature human erythrocytes combined with immunoblotting revealed the presence of a group of heat shock proteins (HSPs) that included two molecular chaperons of the HSP70 family (HSX70, inducible; HSC70, constitutively expressed) and HSP90. As expected for cells devoid of organelles, erythrocytes do not contain stress proteins that are localized either in the mitochondria (HSP60, glucose-regulated protein (GRP 75) or in the endoplasmic reticulum (GRP78 or Ig heavy chain-binding protein, endoplasmin). Since red cells are unable to replace proteins whose structure has been damaged by environmental changes the results are taken to imply a role for chaperons in monitoring, protecting, and maintaining the structure and stability of erythrocyte proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Electrophoresis, Gel, Two-Dimensional
  • Erythrocytes / chemistry*
  • Heat-Shock Proteins / analysis*
  • Humans
  • Immunoblotting

Substances

  • Heat-Shock Proteins