[논문]Induction of Cyclin D1 Proteasomal Degradation by Branch Extracts from Abeliophyllum distichum Nakai in Human Colorectal Cancer Cells

Park, Gwang Hun; Park, Jae Ho; Jeong, Jin Boo

doi:10.7732/kjpr.2015.28.6.682

Induction of Cyclin D1 Proteasomal Degradation by Branch Extracts from Abeliophyllum distichum Nakai in Human Colorectal Cancer Cells 원문보기

韓國資源植物學會誌 = Korean journal of plant resources, v.28 no.6, 2015년, pp.682 - 689

Park, Gwang Hun (Department of Bioresource Sciences, Andong National University) , Park, Jae Ho (Department of Medicinal Plant Science, Jungwon University) , Jeong, Jin Boo (Department of Bioresource Sciences, Andong National University)

Abstract ▼ AI-Helper

Abeliophyllum distichum Nakai (A. distichum) has been reported to exert the inhibitory effect on angiotensin converting enzyme and aldose reductase. Recently, our group found that branch extracts of A. distichum (EAFAD-B) induce apoptosis through ATF3 activation in human colon cancer cells. However, anti-cancer reagents exert their activity through the regulation of various molecular targets. Therefore, the elucidation of potential mechanisms of EAFAD-B for anti-cancer activity may be necessary. To elucidate the potential mechanism of EAFAD-B for anti-cancer activity, we evaluated the regulation of cyclin D1 in human colon cancer cells. EAFAD-B decreased cellular accumulation of cyclin D1 protein. However, cyclin D1 mRNA was not changed by EAFAD-B. Inhibition of proteasomal degradation by MG132 attenuated EAFAD-B-mediated cyclin D1 downregulation and the half-life of cyclin D1 was decreased in the cells treated with EAFAD-B. In addition, EAFAD-B induced cyclin D1 phosphorylation at threonine-286 and the point mutation of threonine-286 to alanine attenuated EAFAD-B-mediated cyclin D1 proteasomal degradation. Inhibitions of both ERK1/2 by PD98059 and NF-κB by a selective inhibitor, BAY 11-7082 suppressed cyclin D1 downregulation by EAFAD-B. From these results, we suggest that EAFAD-B-mediated cyclin D1 downregulation may result from proteasomal degradation through its threonine-286 phosphorylation via ERK1/2-dependent NF-κB activation. The current study provides new mechanistic link between EAFAD-B and anti-cancer activity in human colon cancer cells.

주제어

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제안 방법

In light of the preventive potential of A. distichum in colon cancer, this study was performed to elucidate the biological mechanism by which EAFAD-B induces the inhibition of cell growth in human colon cancer cells. Here, for the first time, we report that the branch extracts from A.
, 2014a). To investigate if EAFAD-B affects the level of cyclin D1 protein in human colon cancer cells, HCT116 and SW480 cells were treated with 0, 50, 100 and 200 ㎍/㎖ of EAFAD-B for 24 h. As shown in Fig.

대상 데이터

BAY 11-7082 were purchased from Sigma Aldrich (St. Louis, MO, USA). PD98059 were purchased from Calbiochem (San Diego, CA, USA).
Cell culture media, Dulbecco's Modified Eagle medium (DMEM)/F-12 1:1 Modified medium (DMEM/F-12) was purchased from Lonza (Walkersville, MD, USA). BAY 11-7082 were purchased from Sigma Aldrich (St.

데이터처리

A statistical analysis was performed with the Student’s unpaired t-test and one-way ANOVA followed by Dunnett’s test. Differences with *P < 0.

성능/효과

To determine the upstream kinases involved in EAFAD-B-mediated proteasomal degradation of cyclin D1, HCT116 cells were pretreated with PD98059 as an ERK1/2 inhibitor or BAY 11-7082 as a selective NF-κB inhibitor, and then exposured to EAFAD-B. As a result (Fig. 4A and 4B), inhibition of both ERK1/2 and NF-κB attenuated cyclin D1 proteasomal degradation by EAFAD-B in both HCT116 and SW480 cells, which indicates that activation of ERK1/2 and NF-κB by EAFAD-B can contribute to cyclin D1 proteasomal degradation. Thus, we investigated if EAFAD- B activates ERK1/2 and NF-κB, and found that EAFAD-B increased the phosphorylation levels of ERK1/2 and IκK-α, and NF-κB luciferase activity (Fig.

후속연구

However, it is not clear that the reduction of cyclin D1 protein level by acteoside results from transcriptional regulation or proteasomal degradation. Therefore, the further mechanistic study will be required to investigate if acteoside- mediated decrease of cyclin D1 is resulted from proteasomal degradation.

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