Kulyte Agné, Navakauskiene Ruta, Treigyte Grazina, Gineitis Arunas, Bergman Tomas, Magnusson Karl-Eric
Division of Medical Microbiology, Linköpings Universitet, SE-581 85 Linköping, Sweden.
Mol Biol Cell. 2002 Dec;13(12):4195-205. doi: 10.1091/mbc.e02-03-0128.
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.
研究了视黄酸（RA）诱导的人早幼粒细胞白血病细胞系HL-60粒细胞分化过程中，蛋白质α-肌营养不良蛋白及其他亚型的生化特性和空间定位。在这些细胞的胞质溶胶和细胞核中均检测到α-肌营养不良蛋白，并且在RA触发的分化开始后不久，一种短亚型（γ-肌营养不良蛋白）就被酪氨酸磷酸化修饰。在HL-60早幼粒细胞、RA分化的成熟粒细胞和人类中性粒细胞中，可以辨别出α-肌营养不良蛋白及其亚型的不同分布模式。此外，发现γ-肌营养不良蛋白亚型与肌动蛋白和肌球蛋白轻链相关。这些结果为α-肌营养不良蛋白及其剪接亚型在粒细胞分化诱导过程中以及在分化或吞噬细胞的承诺阶段的髓系细胞信号转导中的潜在参与提供了新信息。
