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A case of metastatic prostate cancer initially presenting as chylothorax
( Yu-jin Yang ),( Minjung Seo ),( Hee-jeong Jeon ),( Jin-hee Noh ),( Seol Hoon Park ),( Yunsuk Choi ),( Jae-cheol Jo ),( Jin Ho Baek ),( Su-jin Koh ),( Hawk Kim ),( Young Joo Min ) 대한내과학회 2015 대한내과학회 추계학술대회 Vol.2015 No.1
Chylothorax is caused by disruption or obstruction of the thoracic duct, which results in leakage of chyle in the pleural space. The most common etiologies are malignancy and trauma. Among the causative malignancies, lymphoma is the most common, followed by primary lung cancer, mediastinal tumors, and other metastatic malignancies. Conversely, prostate cancer has rarely been reported as the cause of chylothorax. We here report a case of metastatic prostate cancer initially presenting as chylothorax, and being disappeared pleural effusion after androgen deprivation therapy. We also discuss the various rare manifestations of metastatic prostate cancer.
Zinc Control Asymmetric Cell Division by Regulation of Spire during Oocyte Maturation
Yu-Jin Jo,In-won Lee,Seong-min Jeong,Nam-Hyung Kim,Suk Namgoong 한국수정란이식학회 2016 한국수정란이식학회 학술대회 Vol.2016 No.10
Zinc (Zn2+) is one of essential factors during mammalian oocyte maturation and fertilization. Previous studies showed that depletion of cellular Zn by metalion chelator impair asymmetric division of oocyte. But the detailed mechanism of these phenomena is unclear. We found that depletions of zinc by cell-permeable heavy metal chelator N,N,N',N'-tetrakis(2-pyridylmethyl)ethane-1,2-diamine (TPEN) caused the decrease of cytoplasmic actin mesh level. Spire2-GFP is co-localized with zinc at the cortex and intracellular vesicle. By the treatment of TPEN, number of Spire2-GFP decorated vesicle is drastically decreased, indicating that Zn2+is essential for the localization of the spire in mouse oocyte. Two putative zinc-binding regions were located in the C-terminal part of Spire2. Mutations of zinc binding site on spire abolish its localization at the intracellular vesicle. Over expression of C-terminal region containing zinc binding site of spire impair oocyte maturations and decrease cytoplasmic actin mesh. Taken together, these results suggest that intracellular zinc is crucial for the proper localizations of spire in the mouse oocyte, and unraveling the novel regulatory mode of actin nucleator spire by Zn2+.
Actin-capping proteins play essential roles in the asymmetric division of maturing mouse oocytes
Jo, Yu-Jin,Jang, Woo-In,Namgoong, Suk,Kim, Nam-Hyung The Company of Biologists Ltd. 2015 Journal of cell science Vol.128 No.1
<P>Actin polymerization is essential for various stages of mammalian oocyte maturation, including spindle migration, actin cap formation, polar body extrusion and cytokinesis. The heterodimeric actin-capping protein is an essential element of the actin cytoskeleton. It binds to the fast-growing (barbed) ends of actin filaments and plays essential roles in various actin-mediated cellular processes. However, the roles of capping protein in mammalian oocyte maturation are poorly understood. We investigated the roles of capping protein in mouse oocytes and found that it is essential for correct asymmetric spindle migration and polar body extrusion. Capping protein mainly localized in the cytoplasm during maturation. By knocking down or ectopically overexpressing this protein, we revealed that it is crucial for efficient spindle migration and maintenance of the cytoplasmic actin mesh density. Expression of the capping-protein-binding region of CARMIL (also known as LRRC16A) impaired spindle migration and polar body extrusion during oocyte maturation and decreased the density of the cytoplasmic actin mesh. Taken together, these findings show that capping protein is an essential component of the actin cytoskeleton machinery that plays crucial roles in oocyte maturation, presumably by controlling the cytoplasmic actin mesh density.</P>
Jo, Hyun-Young,Lee, Hyo-Jung,Jo, Yu-Jin,Lee, Jong-Jae,Ban, Soojin,Lee, Jin-Ju,Chang, Lim-Seok,Heo, Gookyoung,Kim, Cheol-Hee Elsevier 2019 Atmospheric research Vol.225 No.-
<P><B>Abstract</B></P> <P>This study investigated the potential of fine nitrate (NO<SUB>3</SUB> <SUP>−</SUP> in PM<SUB>2.5</SUB>) formation in Seoul Metropolitan Area (SMA) by nighttime dinitrogen pentoxide (N<SUB>2</SUB>O<SUB>5</SUB>) heterogeneous chemistry during March 16–18, 2016, relatively dry and stagnant early spring days, by intervening N<SUB>2</SUB>O<SUB>5</SUB> uptake coefficients (reactive uptake probability, γN<SUB>2</SUB>O<SUB>5</SUB>) in modeling with WRF-CMAQ. Simulations of a base case and two sensitivity tests with default (Davis et al., 2008), zero and decupled (tenfold) γN<SUB>2</SUB>O<SUB>5</SUB> showed that impacts of γN<SUB>2</SUB>O<SUB>5</SUB> on NO<SUB>3</SUB> <SUP>−</SUP> and PM<SUB>2.5</SUB> are sensitive to relative humidity (RH) and sulfate-nitrate-ammonium (SNA) conditions. The base case simulation generally underestimated NO<SUB>3</SUB> <SUP>−</SUP> and PM<SUB>2.5</SUB> levels in comparison to observations. Even with decupled γN<SUB>2</SUB>O<SUB>5</SUB>, modeled NO<SUB>3</SUB> <SUP>−</SUP> and PM<SUB>2.5</SUB> concentrations showed relatively small increases under conditions that RH is relatively low in the range of 20 to 40% and SNA levels are severely underestimated (e.g., lower by one third) in the base case simulation. Comparisons of NO<SUB>3</SUB> <SUP>−</SUP> and PM<SUB>2.5</SUB> concentrations in SMA between simulations with differently specified γN<SUB>2</SUB>O<SUB>5</SUB> indicated that N<SUB>2</SUB>O<SUB>5</SUB> heterogeneous chemistry has potential to (1) form additional nitric acid (HNO<SUB>3</SUB>), (2) further react with ammonia (NH<SUB>3</SUB>) emitted from various sources including agricultural sources outside of SMA urban-core areas, and (3) contribute to NO<SUB>3</SUB> <SUP>−</SUP> and PM<SUB>2.5</SUB> formation in SMA. Additional modeling and observational studies on heterogeneous N<SUB>2</SUB>O<SUB>5</SUB> chemistry are needed to improve our understanding of NO<SUB>3</SUB> <SUP>−</SUP> and PM<SUB>2.5</SUB> formation and better forecast PM<SUB>2.5</SUB> pollution levels over SMA or other urban areas with abundant nitrogen oxides emissions and ammonia emissions such as agricultural emissions from surrounding areas.</P> <P><B>Highlights</B></P> <P> <UL> <LI> N<SUB>2</SUB>O<SUB>5</SUB> heterogeneous chemistry in the PM<SUB>2.5</SUB> formation was investigated by intervening the uptake coefficient (rN<SUB>2</SUB>O<SUB>5</SUB>). </LI> <LI> Simulations with the improved uptake coefficient (rN<SUB>2</SUB>O<SUB>5</SUB>) contributed to better PM<SUB>2.5</SUB> prediction in some conditons. </LI> <LI> Observational studies are needed to understand the nitare formation in the areas with abundant NO<SUB>x</SUB> and NH<SUB>3</SUB> emissions. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
Purification and Characterization of β-N-Acetylhexosaminidase from Rice Seeds
Jin, Yu-Lan,Jo, Yu-Young,Kim, Kil-Yong,Shim, Jae-Han,Kim, Yong-Woong,Park, Ro-Dong 생화학분자생물학회 2002 Journal of biochemistry and molecular biology Vol.35 No.3
N-Acetyl-$\beta$-D-hexosaminidase ($\beta$-HexNAc'ase) (EC 3.2.1.52) was purified from rice seeds (Oryza sative L. var. Dongjin) using ammonium sulfate (80%) precipitation, Sephadex G-150, CM-Sephadex, and DEAE-Sephadex chromatography, sequentially. The activities were separated into 7 fractions($F_1-F_7$) by CM-Sephadex chromatography. Among them, F6 was further purified to homogeneity with a 13.0% yield and 123.3 purification-fold. The molecular mass was estimated to be about 52 kDa on SDS-PAGE and 37.4 kDa on Sephacryl S-300 gel filtration. The enzyme catalyzed the hydrolysis of both p-nitrophenyl-N-acetyl-$\beta$-D-hexosaminide (pNP-GlcNAc) and p-nitrophenyl-N-acetyl-$\beta$-D-hexosaminide (pNP-GalNAc) as substrates, which are typical properties of $\beta$-HexNAc'ase. The ratio of the pNP-GlcNAc'ase activity to the pNP-GalNAc'ase activity was 4.0. However, it could not hydrolyze chitin, chitosan, pNP-$\beta$-glucopyranoside, or pNP-$\beta$-glucopyranoside. The enzyme showed $K_m$, $V_{max}$ and $K_{cat}$ for pNP-GlcNAc of 1.65 mM, $79.49\;mM\;min^{-1}$, and $4.79{\times}10^6\;min^{-1}$, respectively. The comparison of kinetic values for pNP-GlcNAc and pNP-GalNAc revealed that the two enzyme activities are associated with a single binding site. The purified enzyme exhibited optimum pH and temperature for pNP-GlcNAc of 5.0 and $50^{\circ}C$, respectively. The enzyme activity for pNP-GlcNAc was stable at pH 5.0-5.5 and $20-40^{\circ}C$. The enzyme activity was completely inhibited at a concentration of 0.1 mM $HgCl_$ and $AgNO_3$, suggesting that the intact thiol group is essential for activity. Chloramine T completely inhibited the activity, indicating the possible involvement of methionines in the mechanism of the enzyme.