title: Differential binding of mutant (R116C) and wildtype alphaA crystallin to actin.
abstract: OBJECTIVE
  Quantitate the interaction of mutant (R116C) and wildtype human alphaA crystallins with actin.
  
  
  METHODS
  AlphaA crystallins, expressed in a recombinant system, were purified, followed by passage through an actin affinity column.
  
  
  RESULTS
  Binding of mutant alphaA crystallin was significantly less than binding of wildtype alphaA crystallin.
  
  
  CONCLUSIONS
  The R116C mutation of alphaA crystallin found in human cataracts binds less to the cytoskeletal component actin. Since both alphaA crystallin and actin are necessary for proper development of the lens, decreased binding of the mutant protein to actin may perturb normal differentiation processes of lens cells which are necessary for transparency.
authors: Division of Biology, Kansas State University, Manhattan 97239, USA.
authors: Zachery
authors: Z
authors: Brown
authors: Aldo
authors: A
authors: Ponce
authors: Kirsten
authors: K
authors: Lampi
authors: Lynn
authors: L
authors: Hancock
authors: Larry
authors: L
authors: Takemoto
mesh_terms: D000199:Actins / Q000378:metabolism*; D002846:Chromatography, Affinity; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006801:Humans; D007223:Infant; D009154:Mutation; D011485:Protein Binding; D011994:Recombinant Proteins; D021241:Spectrometry, Mass, Electrospray Ionization; D038202:alpha-Crystallin A Chain / Q000235:genetics / Q000378:metabolism*
chemical_list: D000199:Actins; D011994:Recombinant Proteins; D038202:alpha-Crystallin A Chain