Morgana/CHP-1 is a novel chaperone able to protect cells from stress

Biochim Biophys Acta. 2010 Sep;1803(9):1043-9. doi: 10.1016/j.bbamcr.2010.05.005. Epub 2010 May 20.

Abstract

Morgana/CHP-1 (CHORD containing protein-1) has been recently shown to be necessary for proper cell divisions. However, the presence of the protein in postmitotic tissues such as brain and striated muscle suggests that morgana/CHP-1 has additional cellular functions. Here we show that morgana/CHP-1 behaves like an HSP90 co-chaperone and possesses an independent molecular chaperone activity towards denatured proteins. The expression time profile of morgana/Chp-1 in NIH3T3 cells in response to heat stress is similar to that of Hsp70, a classical effector of Heat Shock Factor-1 mediated stress response. Moreover, overexpression of morgana/CHP-1 in NIH3T3 cells leads to the increased stress resistance of the cells. Interestingly, morgana/Chp-1 upregulation in response to transient global brain ischemia lasts longer in ischemia-resistant regions of the gerbil hippocampus than in vulnerable ones, suggesting the involvement of morgana/CHP-1 in natural protective mechanisms in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brain Ischemia / genetics
  • Brain Ischemia / pathology
  • Carrier Proteins / genetics
  • Carrier Proteins / physiology*
  • Cells / metabolism*
  • Cells, Cultured
  • Cytoprotection / genetics*
  • Gerbillinae
  • HSP90 Heat-Shock Proteins / metabolism
  • HSP90 Heat-Shock Proteins / physiology
  • Heat-Shock Response / genetics
  • Heat-Shock Response / physiology
  • Hot Temperature
  • Mice
  • Molecular Chaperones / genetics
  • Molecular Chaperones / physiology
  • NIH 3T3 Cells
  • Stress, Physiological / genetics*

Substances

  • Carrier Proteins
  • Chp-1 protein, mouse
  • HSP90 Heat-Shock Proteins
  • Molecular Chaperones