Proteomic analysis of breast cancer tissue reveals upregulation of actin-remodeling proteins and its relevance to cancer invasiveness
- Proteomic analysis of breast cancer tissue reveals upregulation of actin-remodeling proteins and its relevance to cancer invasiveness
- 김동현; 배진희; 이종원; 김선영; 김용학; 배지연; 이재교; 유명희; 노동영; 이철주
- Arp2/3 complex subunit 2; Breast cancer; Coronin-1A; DIGE; Invasion assay
- Issue Date
- Proteomics Clinical applications.
- VOL 3, NO 1, 30-40
- There is an emerging interest in protein expression profiling with the aim of identifying
novel diagnostic markers and therapeutic targets in breast cancer. We analyzed breast cancer
tissues by 2-D DIGE using a narrow range IPG strip (pH 5.5–6.7) after the immunodepletion
of serum albumin and Ig. Sixty-three protein spots were detected with more than 61.8-fold
differences (p ,0.05 for three technical replicates) from a set of tissue samples in which
three tumor and three nontumor samples were randomly selected from six breast cancer
subjects and pooled separately. Of these, 53 proteins were successfully identified by MS.
Among the proteins whose levels were increased, we identified three novel WD-repeat-motifbearing proteins that have been known to be involved in actin remodeling: Arp2/3 complex
subunit 2 (p34-Arc), coronin-1A and WD-repeat protein 1 (Wdr1). Significantly increased
amounts of p34-Arc and coronin-1A in breast cancer were also shown by Western blot analysis
of matched tumor and nontumor tissue samples (N = 11, p ,0.05), and were consistent
with the mRNA levels retrieved from publicly available microarray databases. The siRNA
knockdown of p34-Arc attenuated the invasion of SK-BR3 breast cancer cells into Matrigel.
In contrast, the overexpression of coronin-1A increased this invasive activity. Taken together,
the cellular levels of p34-Arc and coronin-1A were linked to cancer development and migration.
The data obtained from the present study provides new insight into the management of
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