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USP14 inhibition regulates tumorigenesis by inducing apoptosis in gastric cancer
Mi Yea Lee,Min-Jee Kim,Jun-O Jin,Peter Chang-Whan Lee 생화학분자생물학회 2023 BMB Reports Vol.56 No.8
Deubiquitinases (DUBs) are an essential component of theubiquitin-proteasome system (UPS). They trim ubiquitin fromsubstrate proteins, thereby preventing them from degradation,and modulate different cellular processes. Ubiquitin-specificprotease 14 (USP14) is a DUB that has mainly been studied forits role in tumorigenesis in several cancers. In the present study,we found that the protein levels of USP14 were remarkablyhigher in gastric cancer tissues than in the adjacent normaltissues. We also demonstrated that the inhibition of USP14activity using IU1 (an USP14 inhibitor) or the inhibition ofUSP14 expression using USP14-specific siRNA markedly reducedthe viability of gastric cancer cells and suppressed their migratoryand invasive abilities. The reduction in gastric cancercell proliferation due to the inhibition of USP14 activity was aresult of the increase in the degree of apoptosis, as evidencedby the increased expression levels of cleaved caspase-3 andcleaved PARP. Furthermore, an experiment using the USP14inhibitor IU1 revealed that the inhibition of USP14 activitysuppressed 5-fluorouracil (5-FU) resistance in GC cells. Collectively,these findings indicate that USP14 plays critical roles ingastric cancer progression and suggest its potential to serve asa novel therapeutic target for gastric cancer treatment.
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USP14 Inhibition Regulates Tumorigenesis by Inducing Autophagy in Lung Cancer In Vitro
Han, Kyung Ho,Kwak, Minseok,Lee, Tae Hyeong,Park, Min-soo,Jeong, In-ho,Kim, Min Ji,Jin, Jun-O,Lee, Peter Chang-Whan MDPI AG 2019 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES Vol.20 No.21
<P>The ubiquitin-proteasome system is an essential regulator of several cellular pathways involving oncogenes. Deubiquitination negatively regulates target proteins or substrates linked to both hereditary and sporadic forms of cancer. The deubiquitinating enzyme ubiquitin-specific protease 14 (USP14) is associated with proteasomes where it trims the ubiquitin chain on the substrate. Here, we found that USP14 is highly expressed in patients with lung cancer. We also demonstrated that USP14 inhibitors (IU1-47 and siRNA-USP14) significantly decreased cell proliferation, migration, and invasion in lung cancer. Remarkably, we found that USP14 negatively regulates lung tumorigenesis not only through apoptosis but also through the autophagy pathway. Our findings suggest that USP14 plays a crucial role in lung tumorigenesis and that USP14 inhibitors are potent drugs in lung cancer treatment.</P>
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반상호침투 구조체 형성을 이용한 막대형 양자물질의 분산과 안정화
리스티아나 옥타비아(Listiana Oktavia),김성진(Seong-Jin Kim),김종형(Jong Hyung Kim),박해인(Haein Park),이창환(Peter Chang-Whan Lee),곽민석(Minseok Kwak) 한국고분자학회 2016 폴리머 Vol.40 No.1
PEO-b-PPO-b-PEO를 기본 구조로 한 F127, L64 등의 pluronic은 수용액에서 미세상분리에 의하여 자기조립하고 그 중심부에 소수성의 분자들을 담지할 수 있는 응용가능성이 높은 고분자이다. 수십 나노 미터의 길이를 가진 막대모양 나노결정인 막대형 양자물질(quantum rod; QR) 콜로이드를 소수성 상호작용으로 담지한 뒤, 곧바로 반상호침투 구조체를 제조하여 장기간 형광 세기의 현저한 저하가 없는 안정한 유-무기 복합 나노소재를 수월하게 만들 수 있다. 우리가 제조한 F127-QR-sIPN 나노구조체는 표면이 poly(ethylene oxide)(PEO)로 둘러싸여 생체적합성이 우수하며 형광특성을 가진 QR이 세포섭취됨에 따라 형광 이미징도 가능함을 보였다. Pluronics (e.g. F127 and L64) are linear triblock copolymers capable of loading hydrophobic moieties within the core of aggregates via micro-phase separation. We demonstrate semi-interpenetrating network formation of organicinorganic hybrid composites consist of quantum rod (QR) firmly encapsulated by F127. The stabilized nanoobjects are stable for a long period. Furthermore, we report that QR-IPN is promising material applicable in fluorescent cell-imaging with guaranteed biocompatibility.
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