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MBC in Press, published online ahead of print September 24, 2002
Mol. Biol. Cell 10.1091/mbc.E02-03-0128

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Submitted on March 6, 2002
Revised on July 30, 2002
Accepted on September 9, 2002

CHARACTERIZATION OF HUMAN ALPHA-DYSTROBREVIN ISOFORMS IN HL-60 HUMAN PROMYELOCYTIC LEUKEMIA CELLS UNDERGOING GRANULOCYTIC DIFFERENTIATION

Agné Kulyte1*, Ruta Navakauskiene2, Grazina Treigyte2, Arunas Gineitis3, Tomas Bergman4, and Karl-Eric Magnusson1

1 Division of Medical Microbiology, Linköpings Universitet, SE-581 85 Linköping, Sweden
2 Department of Developmental Biology, Institute of Biochemistry, 2600 Vilnius, Lithuania
3 Department of Biological Chemistry, School of Medicine, University of California at Davis, Davis, California 95616, USA
4 Protein Analysis Center, Karolinska Institutet, SE-171 77, Stockholm, Sweden

* Corresponding author. E-mail address: agne.kulyte{at}cgb.ki.se.

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 isofom (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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