Translocation of beta crystallin in neural cells in response to stress.

While extralenticular expression of proteins in the alpha crystallin (small heat shock protein) family is well documented, that for proteins in the beta/gamma-superfamily is less well established. Here we show, using SDS-PAGE, Western blotting and confocal microscopy, that there is a constitutive level of beta crystallin expression in mouse N1E-115 neural cells. Furthermore, upon heat shock at 43 degrees C or 55 degrees C, or cold shock at 30 degrees C, beta crystallin immunoreactivity translocated predominantly from the nuclear region into the cytoplasmic region of the cells. In conditions of stress, it may be important for beta crystallin to be recruited into the cytoplasm to stabilise other proteins via its high beta-sheet content, and/or to ensure that storage levels of cytoplasmic Ca2+ are maintained.
AuthorsA Coop, K E Wiesmann, M J Crabbe
JournalFEBS letters (FEBS Lett) Vol. 431 Issue 3 Pg. 319-21 (Jul 24 1998) ISSN: 0014-5793 [Print] NETHERLANDS
PMID9714534 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Crystallins
  • Animals
  • Biological Transport
  • Blotting, Western
  • Crystallins (metabolism)
  • Immunohistochemistry
  • Mice
  • Microscopy, Confocal
  • Neuroblastoma (metabolism, pathology)
  • Neurons (metabolism)
  • Oxidative Stress

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