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Park, Sujin,Yang, Kyung-Min,Park, Yuna,Hong, Eunji,Hong, Chang Pyo,Park, Jinah,Pang, Kyoungwha,Lee, Jihee,Park, Bora,Lee, Siyoung,An, Haein,Kwak, Mi-Kyung,Kim, Junil,Kang, Jin Muk,Kim, Pyunggang,Xiao, Korean Society of Cancer Prevention 2018 Journal of cancer prevention Vol.23 No.1
<P><B>Background</B></P><P>Smad3 linker phosphorylation plays essential roles in tumor progression and metastasis. We have previously reported that the mutation of Smad3 linker phosphorylation sites (Smad3-Erk/Pro-directed kinase site mutant constructs [EPSM]) markedly reduced the tumor progression while increasing the lung metastasis in breast cancer.</P><P><B>Methods</B></P><P>We performed high-throughput RNA-Sequencing of the human prostate cancer cell lines infected with adenoviral Smad3-EPSM to identify the genes regulated by Smad3-EPSM.</P><P><B>Results</B></P><P>In this study, we identified genes which are differentially regulated in the presence of Smad3-EPSM. We first confirmed that Smad3-EPSM strongly enhanced a capability of cell motility and invasiveness as well as the expression of epithelial-mesenchymal transition marker genes, <I>CDH2</I>, <I>SNAI1</I>, and <I>ZEB1</I> in response to TGF-β1 in human pancreatic and prostate cancer cell lines. We identified <I>GADD45B</I>, <I>CTGF</I>, and <I>JUNB</I> genes in the expression profiles associated with cell motility and invasiveness induced by the Smad3-EPSM.</P><P><B>Conclusions</B></P><P>These results suggested that inhibition of Smad3 linker phosphorylation may enhance cell motility and invasiveness by inducing expression of <I>GADD45B</I>, <I>CTGF</I>, and <I>JUNB</I> genes in various cancers.</P>
Park, Daehun,Na, Myeongsu,Kim, Jung Ah,Lee, Unghwi,Cho, Eunji,Jang, Mirye,Chang, Sunghoe AAAS 2017 Science signaling Vol.10 No.487
<P><B>Amyloid-β and intersynaptic trafficking</B></P><P>Synaptic loss and dysfunction as well as neuronal accumulation of amyloid-β (Aβ) are classic features of Alzheimer’s disease (AD). Synaptic components are transported along axons in actin- and synapsin-associated vesicles to adjust synaptic strength in response to activity and to promote the formation of new synapses. Using hippocampal neurons isolated from rats and mouse models of AD, Park <I>et al</I>. found that a soluble form of Aβ impedes Ca<SUP>2+</SUP> clearance from neurons, which led to activation of the kinase CaMKIV. CaMKIV-mediated phosphorylation of synapsin caused its dissociation from synaptic vesicles and actin, thereby impairing vesicular transport. Targeting this pathway might suppress the pathological effects of Aβ in patients with AD.</P><P>The prefibrillar form of soluble amyloid-β (sAβ<SUB>1–42</SUB>) impairs synaptic function and is associated with the early phase of Alzheimer’s disease (AD). We investigated how sAβ<SUB>1–42</SUB> led to presynaptic defects using a quantum dot–based, single particle–tracking method to monitor synaptic vesicle (SV) trafficking along axons. We found that sAβ<SUB>1–42</SUB> prevented new synapse formation induced by chemical long-term potentiation (cLTP). In cultured rat hippocampal neurons, nanomolar amounts of sAβ<SUB>1–42</SUB> impaired Ca<SUP>2+</SUP> clearance from presynaptic terminals and increased the basal Ca<SUP>2+</SUP> concentration. This caused an increase in the phosphorylation of Ca<SUP>2+</SUP>/calmodulin-dependent protein kinase IV (CaMKIV) and its substrate synapsin, which markedly inhibited SV trafficking along axons between synapses. Neurons derived from a transgenic AD mouse model had similar defects, which were prevented by an inhibitor of CaMK kinase (CaMKK; which activates CaMKIV), by antibodies against Aβ<SUB>1–42</SUB>, or by expression a phosphodeficient synapsin mutant. The CaMKK inhibitor also abolished the defects in activity-dependent synaptogenesis caused by sAβ<SUB>1–42</SUB>. Our results suggest that by disrupting SV reallocation between synapses, sAβ<SUB>1–42</SUB> prevents neurons from forming new synapses or adjusting strength and activity among neighboring synapses. Targeting this mechanism might prevent synaptic dysfunction in AD patients.</P>
Optimization of Ceramide Analysis Method Using LC-MS in Cosmetics
Park Su-Jin,Yoo Hee-Jin,Kim Duck-Hyun,Park Ji-Won,Jeon Eunji,Mojumdar Abhik,Cho Kun 사단법인 한국질량분석학회 2024 Mass spectrometry letters Vol.15 No.1
Ceramide is a lipid in which sphingoid bases and fatty acids are linked by amide bonds. As a marker of skin disease in the human stratum corneum, its disease-causing and therapeutic effects have been partially confirmed, and it is therefore an important element in commercially available cosmetic formulations. However, structural diversity caused by differences in the chain length, number, and location of hydroxyl groups makes quality control difficult. In this study, a method was established to separate different ceramide species using reversed-phase LC-MS/MS and thus enable qualitative evaluation. Separation of four standards was achieved within a short retention time, and the accuracy and sensitivity of the method were demonstrated by the low limit of detection (LOD) calculated based on the calibration curve showing linearity, with R 2 > 0.994. After verification of reproducibility and reliability through intra- and inter-day analyses, the efficiency of the method was confirmed through analysis of commercial cosmetic raw materials.
Microbial Transformation of Trichostatin A to 2,3-Dihydrotrichostatin A
Park, Je Won,Park, Sung Ryeol,Han, Ah Reum,Ban, Yeon-Hee,Yoo, Young Ji,Kim, Eun Ji,Kim, Eunji,Yoon, Yeo Joon American Chemical Society and American Society of 2011 Journal of natural products Vol.74 No.5
<P>A new reduced hydroxamate, 2,3-dihydrotrichostatin A, was created from trichostatin A by employing a recombinant strain of <I>Streptomyces venezuelae</I> as a microbial catalyst. Compared with trichostatin A, 2,3-dihydrotrichostatin A showed similar antifungal activity against <I>Saccharomyces cerevisiae</I>, but, interestingly, approximately twice the cytostatic activity against human small-cell lung cancer cells. The production of 2,3-dihydrotrichostatin A via microbial biotransformation demonstrates that the regiospecific and substrate-flexible hydrogenation by <I>S. venezuelae</I> provides a new approach for creating natural product analogues with improved bioactive properties.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jnprdf/2011/jnprdf.2011.74.issue-5/np1006718/production/images/medium/np-2010-006718_0003.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/np1006718'>ACS Electronic Supporting Info</A></P>