Jun S

References (2)

Title : ABHD12 Knockdown Suppresses Breast Cancer Cell Proliferation, Migration and Invasion - Jun_2020_Anticancer.Res_40_2601
Author(s) : Jun S , Kim SW , Lim JY , Park SJ
Ref : Anticancer Research , 40 :2601 , 2020
Abstract : BACKGROUND/AIM: Alpha/beta-hydrolase domain containing 12 (ABHD12) is a serine hydrolase that regulates immunological and neurological mechanisms. This study aimed to elucidate the oncogenic effect of ABHD12 on human breast cancer. MATERIALS AND METHODS: ABHD12 expression was confirmed in breast cancer tissues and breast cancer cell lines by immunohistochemistry and quantitative RT-PCR. To determine the role of ABHD12, ABHD12 siRNA-suppressed breast cancer cells (MCF7 and MDA-MB-231 cells) were investigated for cell proliferation, migration, and invasion capabilities using MTT assays, EdU assays, colony formation assays, and Boyden chamber assays. RESULTS: Immunohistochemical staining showed a higher ABHD12 expression in breast cancer tissues than in normal tissues. Additionally, ABHD12 knockdown was found to inhibit cell growth, proliferation, migration, and invasion in breast cancer cells. CONCLUSION: ABHD12 plays a crucial role in cell proliferation, migration, and invasion of breast cancer cells.
ESTHER : Jun_2020_Anticancer.Res_40_2601
PubMedSearch : Jun_2020_Anticancer.Res_40_2601
PubMedID: 32366405
Gene_locus related to this paper: human-ABHD12

Title : Expression, purification, crystallization, and diffraction analysis of a selenomethionyl lipase Lip8 from Yarrowia lipolytica - Jun_2018_Prep.Biochem.Biotechnol_48_213
Author(s) : Jun S , XiaoFeng J , Yuan Z , Mi S
Ref : Preparative Biochemistry & Biotechnology , 48 :213 , 2018
Abstract : Yarrowia lipolytica is a nonconventional model micro-organism with multiple biotechnological applications. It is also considered to be an excellent producer for lipase. Genome survey shows that Y. lipolytica possesses various paralogs of genes coding for extracellular, cell-bound, and intracellular lipolytic enzymes. However, little structural information on these isoenzymes is available. With the aim to facilitate crystal structure solution of Lip8, one of the most valuable lipases from Y. lipolytica, a less conventional protein expression technique-selenomethionyl protein expression was used to produce recombinant selenomethionine (SeMet)-Lip8 in Escherichia coli. Finally, three Met residues of Lip8 were all substituted with SeMet. A total of 72 mg of SeMet-Lip8 was obtained from a liter of the SeMet medium. Using sodium acetate as a precipitant and ammonium sulfate as an additive, crystals of the SeMet-Lip8 with 1.9 A were successfully cultured through hanging-drop vapor diffusion method. The estimated crystal dimensions were 0.11 x 0.11 x 0.14 mm(2). The crystal belonged to the space group I4 with unit cell parameters a = b = 128.87 A, c = 171.77 A, alpha = beta = gamma = 90 degrees . It is the second member of lipase crystal family from Y. lipolytica. This work will provide a platform for further studying lipases from a structural insight.
ESTHER : Jun_2018_Prep.Biochem.Biotechnol_48_213
PubMedSearch : Jun_2018_Prep.Biochem.Biotechnol_48_213
PubMedID: 27380164
Gene_locus related to this paper: yarli-LIP8