Subcellular localization of WD40 repeat 1 protein in PC12 rat pheochromocytoma cells
- Authors
- Shin, DH; Lee, E; Chung, YH; Mun, GH; Park, JY; Lomax, MI; Oh, SH
- Issue Date
- Sep-2004
- Publisher
- ELSEVIER IRELAND LTD
- Keywords
- WD40 repeat 1 protein (WDR1); PC12; immunocytochemistry; electron microscope; actin
- Citation
- NEUROSCIENCE LETTERS, v.367, no.3, pp 399 - 403
- Pages
- 5
- Journal Title
- NEUROSCIENCE LETTERS
- Volume
- 367
- Number
- 3
- Start Page
- 399
- End Page
- 403
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24767
- DOI
- 10.1016/j.neulet.2004.06.053
- ISSN
- 0304-3940
1872-7972
- Abstract
- The dynamics of actin filament protein is crucial for various physiological processes of the cells. Among the proteins correlating with actin dynamics, a novel 67-kDa WD40 repeat protein 1 (WDR1) was the vertebrate homologue of actin-interacting protein 1 (Aip1). Even though previous studies have provided the clues on the function of WDR1 in specific organs under pathological conditions, the exact subcellular localization of WDR1 is not known. Therefore, in the present study, we undertook to determine the distribution of WDR1 within PC12 pheochromocytoma cells (PC12 cells) using light and electron microscopic techniques. Double immunocytochemistry clearly showed that WDR1 immunoreactivities (IRs) were co-localized with anti-actin antibody, suggesting the involvement of WDR1 in actin dynamics. WDR1 immunoreactivities (IRs) in PC12 cells showed different distribution patterns as nerve growth factor (NGF) concentrations varied. During active proliferation, the distribution of WDR1 IRs seemed to be similar to those found in cortical actin patches, whereas WDR1 IR was observed in cytoplasmic actin cables after PC12 cells were induced to differentiate by treating with NGE Though further studies are necessary to determine the function of WDR1, the current data represents a first step towards the in vitro study of WDR1 protein. (C) 2004 Elsevier Ireland Ltd. All rights reserved.
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