These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Proteolytic degradation of vimentin and glial fibrillary acidic protein in rat astrocytes in primary culture.
    Author: Ciesielski-Treska J, Goetschy JF, Aunis D.
    Journal: Eur J Biochem; 1984 Feb 01; 138(3):465-71. PubMed ID: 6319134.
    Abstract:
    Vimentin and glial fibrillary acidic (GFA) protein in rat astrocytes in primary culture were identified with their respective specific antisera on electroblots of one-dimensional and two-dimensional polyacrylamide gels. Each antiserum revealed respectively vimentin (58 kDa, pI 5.3), GFA protein (50 kDa, pI 6-5.8) and several more acidic, lower molecular mass vimentin-immunoreactive and GFA protein-immunoreactive polypeptides. These were more apparent when astrocyte proteins were extracted in the absence of EGTA and in the presence of Ca2+ ions suggesting that the lower immunoreactive polypeptides result from a Ca2+-sensitive proteolytic degradation of vimentin and GFA protein. The extent of proteolysis of GFA protein was higher when the differentiation of astrocytes was induced with 1,N6-dibutyryl-adenosine 3',5'-monophosphate (Bt2cAMP). In contrast, the proteolysis of vimentin was not affected by the state of differentiation of astrocytes. The results indicate the existence of at least two distinct degradative pathways for intermediate filament proteins in astrocytes in primary culture and suggest that in differentiated astrocytes the activity of proteinase(s) involved in the degradation of GFA protein increases.
    [Abstract] [Full Text] [Related] [New Search]