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Characterization of human alpha-dystrobrevin isoforms in HL-60 human promyelocytic leukemia cells undergoing granulocytic differentiation.

Abstract
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.
AuthorsAgné Kulyte, Ruta Navakauskiene, Grazina Treigyte, Arunas Gineitis, Tomas Bergman, Karl-Eric Magnusson
JournalMolecular biology of the cell (Mol Biol Cell) Vol. 13 Issue 12 Pg. 4195-205 (Dec 2002) ISSN: 1059-1524 [Print] United States
PMID12475945 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Actins
  • Cytoskeletal Proteins
  • Dystrophin-Associated Proteins
  • Membrane Proteins
  • Myosin Light Chains
  • Protein Isoforms
  • dystrobrevin
  • Tyrosine
  • Trypsin
Topics
  • Actins (metabolism)
  • Cell Differentiation
  • Cell Nucleus (metabolism)
  • Cytoskeletal Proteins (chemistry, metabolism)
  • Cytosol (metabolism)
  • Dystrophin-Associated Proteins
  • Electrophoresis, Polyacrylamide Gel
  • Granulocytes (cytology, metabolism)
  • HL-60 Cells
  • Humans
  • Immunoblotting
  • Membrane Proteins (chemistry, metabolism)
  • Microscopy, Confocal
  • Microscopy, Fluorescence
  • Myosin Light Chains (metabolism)
  • Neutrophils (metabolism)
  • Phagocytosis
  • Phosphorylation
  • Precipitin Tests
  • Protein Isoforms
  • Signal Transduction
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Time Factors
  • Trypsin (pharmacology)
  • Tyrosine (metabolism)

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