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Effects of zinc oxide nanoparticle dispersants on cytotoxicity and cellular uptake
Jo, Mi-Rae,Chung, Hae-Eun,Kim, Hyun-Jin,Bae, Song-Hwa,Go, Mi-Ran,Yu, Jin,Choi, Soo-Jin THE KOREAN SOCIETY OF TOXICOGENOMICS AND TOXICOPRP 2016 MOLECULAR AND CELLULAR TOXICOLOGY Vol. No.
Dispersion critically affects the physicochemical properties of nanoparticles and their interactions with biological systems. In this study, the effects of different zinc oxide nanoparticle (ZnO-NP) dispersants, that is, bovine serum albumin, citrate, carboxymethyl cellulose, fetal bovine serum, and cell culture medium, were investigated with respect to cytotoxicity and cellular uptake. Parallel comparative studies were also conducted with <TEX>$Zn^{2+}$</TEX> ions. The results demonstrated that ZnO-NPs dispersed in citrate exhibited the greatest cytotoxicity to human lung cells, probably related to their high cellular uptake via the citrate internalization mechanism, whereas, the energy-dependent endocytosis pathway of ZnO-NP internalization in cells was unaffected by dispersant type. These results emphasize that dispersant choice is important when evaluating the toxicity of nanoparticles and that results should be interpreted with caution.
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>
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.
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.