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Characterization of...
Characterization of human alpha-dystrobrevin isoforms in HL-60 human promyelocytic leukemia cells undergoing granulocytic differentiation
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Kulyte, A (author)
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Navakauskiene, R (author)
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Treigyte, G (author)
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Gineitis, A (author)
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- Bergman, T (author)
- Karolinska Institutet
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Magnusson, KE (author)
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(creator_code:org_t)
- American Society for Cell Biology (ASCB), 2002
- 2002
- English.
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In: Molecular biology of the cell. - : American Society for Cell Biology (ASCB). - 1059-1524 .- 1939-4586. ; 13:12, s. 4195-4205
- Related links:
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https://europepmc.or...
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http://kipublication...
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https://doi.org/10.1...
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Abstract
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- The biochemical properties and spatial localization of the protein alpha-dystrobrevin and other isoforms were investigated in cells of the human promyelocytic leukemia line HL-60 granulocytic differentiation as induced by retinoic acid (RA). Alpha-dystrobrevin was detected both in the cytosol and the nuclei of these cells, and a short isoform (gamma-dystrobrevin) was modified by tyrosine phosphorylation soon after the onset of the RA-triggered differentiation. Varying patterns of distribution of alpha-dystrobrevin and its isoforms could be discerned in HL-60 promyelocytes, RA-differentiated mature granulocytes, and human neutrophils. Moreover, the gamma-dystrobrevin isoform was found in association with actin and myosin light chain. The results provide new information about potential involvement of alpha-dystrobrevin and its splice isoforms in signal transduction in myeloid cells during induction of granulocytic differentiation and/or at the commitment stage of differentiation or phagocytic cells.
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- ref (subject category)
- art (subject category)
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