An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein

Cell. 1986 Jul 18;46(2):291-300. doi: 10.1016/0092-8674(86)90746-4.


We have characterized a cDNA clone that encodes a protein related to the 70 kd heat shock protein, but is expressed in normal rat liver. This protein has a hydrophobic leader and is secreted into the endoplasmic reticulum. We show that it is identical with two previously described proteins: GRP78, whose synthesis is induced by glucose starvation, and BiP, which is found bound to immunoglobulin heavy chains in pre-B cells. This protein, which is abundant in antibody-secreting cells, can be released from heavy chains by ATP, a reaction analogous to the release of hsp70 from heat shocked nuclear structures. We propose a specific role for this protein in the assembly of secreted and membrane-bound proteins.

MeSH terms

  • Adenosine Triphosphate / physiology
  • Animals
  • Antibody-Producing Cells / metabolism
  • Carrier Proteins / metabolism*
  • Cloning, Molecular
  • DNA / genetics
  • Endoplasmic Reticulum / metabolism*
  • HSP70 Heat-Shock Proteins*
  • Heat-Shock Proteins / isolation & purification*
  • Heat-Shock Proteins / metabolism
  • Immunoglobulin Heavy Chains / isolation & purification*
  • Immunoglobulin Heavy Chains / metabolism
  • Membrane Proteins / isolation & purification*
  • Membrane Proteins / metabolism
  • Molecular Weight
  • Protein Sorting Signals / physiology
  • Rats


  • Carrier Proteins
  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Immunoglobulin Heavy Chains
  • Membrane Proteins
  • Protein Sorting Signals
  • glucose-regulated proteins
  • Adenosine Triphosphate
  • DNA

Associated data

  • GENBANK/M14050