[The comparative analysis of subcellular fractionation methods for revealing of alpha-actinin 1 and alpha-actinin 4 in A431 cells].

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
  • Author(s): Bol'shakova AV; Petukhova OA; Pinaev GP; Magnusson KE
  • Source:
    Tsitologiia [Tsitologiia] 2009; Vol. 51 (2), pp. 122-9.
  • Publication Type:
    Comparative Study; English Abstract; Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    Russian
  • Additional Information
    • Source:
      Publisher: Rossiiskaia Akademiia Nauk Country of Publication: Russia (Federation) NLM ID: 0417363 Publication Model: Print Cited Medium: Print ISSN: 0041-3771 (Print) Linking ISSN: 00413771 NLM ISO Abbreviation: Tsitologiia Subsets: MEDLINE
    • Publication Information:
      Publication: Moskva : Rossiiskaia Akademiia Nauk
      Original Publication: Moskva, Akademiia nauk SSSR.
    • Subject Terms:
    • Abstract:
      Alpha-actinin 1 and alpha-actinin 4 belong to a family of actin-binding proteins with shared structural function and regulation of several processes in a cell. Based on previous data on different distribution of these proteins in the nucleus and cytoplasm, we have explored in detail the distribution of alpha-actinin 1 and alpha-actinin 4 in subcellular fractions in A431 cells spread on fibronectin. Several methods of subcellular fractionation were used. Complex approach allowed resuming that revealing of alpha-actinin isoforms in fractions depended on the composition of lysis buffer and preliminary low-temperature freezing of the cells. We have drawn a conclusion that alpha-actinin 4 can be found in all cytoplasmic and nuclear subfractions, while alpha-actinin 1 is characterized by cytoplasmic and membrane localization with specificity of its distribution tightly to the nuclear membrane.
    • Accession Number:
      0 (ACTN1 protein, human)
      0 (ACTN4 protein, human)
      0 (Buffers)
      0 (Reagent Kits, Diagnostic)
      11003-00-2 (Actinin)
    • Publication Date:
      Date Created: 20090418 Date Completed: 20090625 Latest Revision: 20100519
    • Publication Date:
      20240829
    • Accession Number:
      19371019