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1.
J Pers Med ; 14(4)2024 Apr 22.
Article in English | MEDLINE | ID: mdl-38673066

ABSTRACT

BACKGROUND: This study aimed to compare surgical outcomes between two new robotic single-site myomectomy (RSSM)-complementary techniques: coaxial robotic single-site myomectomy (Coaxial-RSSM) and hybrid robotic single-site myomectomy (Hybrid-RSSM). METHODS: Medical records for 132 women undergoing Coaxial-RSSM and 150 undergoing Hybrid-RSSM, consecutively, were retrospectively reviewed. Patient characteristics and surgical outcomes were assessed and compared after propensity score matching (PSM). RESULTS: In the outcomes of PSM, the Coaxial-RSSM group showed significantly reduced blood loss (79.71 vs. 163.75 mL, p < 0.001) and reduced hospital duration (4.18 ± 0.62 vs. 4.63 ± 0.90) relative to the Hybrid-RSSM group. Conversely, Hybrid-RSSM allowed for a shorter operative time compared with Coaxial-RSSM (119.19 vs. 156.01 min, p = 0.007). No conversions to conventional laparoscopy or laparotomy or any need for the multi-site robotic approach occurred in either group. Postoperative complications, including ileus, fever, and wound dehiscence, showed no statistically significant differences between the two groups. CONCLUSIONS: Blood loss was lower with Coaxial-RSSM, and operative time was shorter for Hybrid-RSSM. A follow-up prospective study is warranted for more comprehensive comparison of surgical outcomes between the two techniques.

2.
PLoS One ; 18(8): e0285159, 2023.
Article in English | MEDLINE | ID: mdl-37540725

ABSTRACT

PHRF1 is an E3 ligase that promotes TGF-ß signaling by ubiquitinating a homeodomain repressor TG-interacting factor (TGIF). The suppression of PHRF1 activity by PML-RARα facilitates the progression of acute promyelocytic leukemia (APL). PHRF1 also contributes to non-homologous end-joining in response to DNA damage by linking H3K36me3 and NBS1 with DNA repair machinery. However, its role in class switch recombination (CSR) is not well understood. In this study, we report the importance of PHRF1 in IgA switching in CH12F3-2A cells and CD19-Cre mice. Our studies revealed that Crispr-Cas9 mediated PHRF1 knockout and shRNA-silenced CH12F3-2A cells reduced IgA production, as well as decreased the amounts of PARP1, NELF-A, and NELF-D. The introduction of PARP1 could partially restore IgA production in PHRF1 knockout cells. Intriguingly, IgA, as well as IgG1, IgG2a, and IgG3, switchings were not significantly decreased in PHRF1 deficient splenic B lymphocytes isolated from CD19-Cre mice. The levels of PARP1 and NELF-D were not decreased in PHRF1-depleted primary splenic B cells. Overall, our findings suggest that PHRF1 may modulate IgA switching in CH12F3-2A cells.


Subject(s)
DNA-Binding Proteins , Immunoglobulin Class Switching , Mice , Animals , DNA-Binding Proteins/genetics , Immunoglobulin Class Switching/genetics , DNA Repair , DNA End-Joining Repair , Immunoglobulin A/genetics
3.
J Chin Med Assoc ; 85(11): 1038-1043, 2022 11 01.
Article in English | MEDLINE | ID: mdl-36343271

ABSTRACT

In mid-2022, the COVID-19 cases have reached close to 562 million, but its overall infection rate is hard to confirm. Even with effective vaccines, break-through infections with new variants occur, and safe and reliable testing still plays a critical role in isolation of infected individuals and in control of an outbreak of a COVID-19 pandemic. In response to this urgent need, the diagnostic tests for COVID-19 are rapidly evolving and improving these days. The health authorities of many countries issued requirements for detecting SARS-CoV-2 diagnosis tests during the pandemic and have timely access to these tests to ensure safety and effectiveness. In this study, we compared the requirements of EUA in Taiwan, Singapore, and the United States. For the performance evaluations of nucleic acid extraction, inclusivity, limit of detection (LoD), cross-reactivity, interference, cutoff, and stability, the requirements are similar in the three countries. The use of natural clinical specimens is needed for clinical evaluation in Taiwan and the United States. However, carry-over and cross-contamination studies can be exempted in Taiwan and the United States but are required in Singapore. This review outlines requirements and insight to guide the test developers on the development of IVDs. Considering the rapidly evolving viruses and severe pandemic of COVID-19, timely and accurate diagnostic testing is imperative to the management of diseases. As noted above, the performance requirements for SARS-CoV-2 nucleic acid tests are similar between Taiwan, Singapore and the United States. The differences are mainly in two points: the recommended microorganisms for cross-reactivity study, and the specimen requirement for clinical evaluation. This study provides an overview of current requirements of SARS-CoV-2 nucleic acid tests in Taiwan, Singapore, and the United States.


Subject(s)
COVID-19 , Nucleic Acids , United States , Humans , COVID-19/diagnosis , Pandemics , SARS-CoV-2 , COVID-19 Testing , Public Health , Taiwan/epidemiology , Singapore/epidemiology
4.
J Anat ; 241(6): 1477-1488, 2022 12.
Article in English | MEDLINE | ID: mdl-36073345

ABSTRACT

Although the level of neuroscience research is rapidly developing with the introduction of new technologies, the method of neuroanatomy education remains at the traditional level and requires improvement to meet the needs of educators and trainees. We developed a new three-dimensional (3D) printed device (human brain-cutting mold, HBCM) for creating human brain slices; moreover, we demonstrated a simple method for creating semi-permanent ultraviolet (UV) resin-mounted brain slice specimens for neuroanatomy education. We obtained brain slices of uniform thickness (3 mm) through the HBCM; the resultant brain slices were optimal for assessing morphological details of the human brain. Furthermore, we used an agar-embedding method for brain-slicing with the HBCM, which minimized geometrical distortions of the brain slices. Also, we prepared semi-permanent brain serial specimens using an acrylic brain slice frame and UV-curable resin, which was highly compatible with moist bio-specimens. During UV resin curing, neither air bubble formation nor color change occurred. The resultant UV resin-mounted brain slices produced definite coronal sections with high transparency and morphological accuracy. We also performed 3D modeling by stacking brain slice images that differentiated the cortical area and nine subcortical regions via manual segmentation. This method could be a reliable alternative for displaying high-quality human brain slices and would be helpful for students and trainee to understand anatomical orientation from 2D images to 3D structures. Also, this may present an innovative approach for preparing and preserving coronal sections of the normal or pathological human brain.


Subject(s)
Brain , Neuroanatomy , Humans , Brain/anatomy & histology , Imaging, Three-Dimensional
5.
PLoS One ; 16(8): e0256282, 2021.
Article in English | MEDLINE | ID: mdl-34407138

ABSTRACT

Human PUF-A/PUM3 is a RNA and DNA binding protein participating in the nucleolar processing of 7S to 5.8S rRNA. The nucleolar localization of PUF-A redistributes to the nucleoplasm upon the exposure to genotoxic agents in cells. However, little is known regarding the roles of PUF-A in tumor progression. Phosphoprotein database analysis revealed that Y259 phosphorylation of PUF-A is the most prevalent residue modified. Here, we reported the importance of PUF-A's phosphorylation on Y259 in tumorigenesis. PUF-A gene was knocked out by the Crispr/Cas9 method in human cervix epithelial HeLa cells. Loss of PUF-A in HeLa cells resulted in reduced clonogenic and lower transwell invasion capacity. Introduction of PUF-AY259F to PUF-A deficient HeLa cells was unable to restore colony formation. In addition, the unphosphorylated mutant of PUF-A, PUF-AY259F, attenuated PUF-A protein stability. Our results suggest the important role of Y259 phosphorylation of PUF-A in cell proliferation.


Subject(s)
Carcinogenesis/metabolism , Minor Histocompatibility Antigens/metabolism , Neoplasms/metabolism , Phosphoproteins/metabolism , Protein Processing, Post-Translational , Tyrosine/metabolism , Atlases as Topic , CRISPR-Cas Systems , Carcinogenesis/genetics , Carcinogenesis/pathology , Cell Movement , Cell Nucleolus/genetics , Cell Nucleolus/metabolism , Cell Proliferation , Databases, Genetic , Female , Gene Deletion , HeLa Cells , Humans , Minor Histocompatibility Antigens/genetics , Mutation , Neoplasms/genetics , Neoplasms/mortality , Neoplasms/pathology , Phosphoproteins/genetics , Phosphorylation , Protein Stability , Survival Analysis
6.
PLoS One ; 15(7): e0236876, 2020.
Article in English | MEDLINE | ID: mdl-32730336

ABSTRACT

PHRF1 (PHD and RING finger domain-containing protein 1) suppresses acute promyelocytic leukemia (APL) by promoting TGIF (TG-interacting factor) ubiquitination, while the PML-RARα protein interferes with PHRF1-mediated TGIF breakdown to facilitate APL. Beyond its role in APL tumorigenesis, PHRF1 contributes to non-homologous end-joining by linking H3K36 methylation and Nbs1 upon DNA damage insults. However, little is known regarding its function in tumor invasion. Here we highlight the unreported details of PHRF1 in the invasion of lung cancer cells by modulating the transcriptional level of ZEB1, a prominent regulator involved in epithelial-mesenchymal transition. PHRF1 associated with the phosphorylated C-terminal repeat domain of Rpb1, the large subunit of RNA polymerase II, through its C-terminal Set2 Rpb1 Interacting (SRI) domain. Chromatin immunoprecipitation revealed that PHRF1 bound to the proximal region adjacent to the transcription start site of ZEB1. SRI-deleted PHRF1 neither associated with Rpb1 nor increased ZEB1's expression. Collectively, PHRF1 might take the stage at migration and invasion by modulating the expression of ZEB1.


Subject(s)
Cell Movement , Lung Neoplasms/pathology , Membrane Proteins/metabolism , Zinc Finger E-box-Binding Homeobox 1/metabolism , Animals , Apoptosis , Biomarkers, Tumor , Cell Proliferation , Gene Expression Regulation, Neoplastic , Humans , Lung Neoplasms/genetics , Lung Neoplasms/metabolism , Membrane Proteins/genetics , Mice , Neoplasm Invasiveness , Prognosis , Tumor Cells, Cultured , Xenograft Model Antitumor Assays , Zinc Finger E-box-Binding Homeobox 1/genetics
7.
Sci Rep ; 7: 45646, 2017 04 03.
Article in English | MEDLINE | ID: mdl-28368047

ABSTRACT

Vilse/Arhgap39 is a Rho GTPase activating protein (RhoGAP) and utilizes its WW domain to regulate Rac/Cdc42-dependent morphogenesis in Drosophila and murine hippocampal neurons. However, the function of Vilse in mammalian dendrite architecture and synaptic plasticity remained unclear. In the present study, we aimed to explore the possible role of Vilse in dendritic structure and synaptic function in the brain. Homozygous knockout of Vilse resulted in premature embryonic lethality in mice. Changes in dendritic complexity and spine density were noticed in hippocampal neurons of Camk2a-Cre mediated forebrain-specific Vilse knockout (VilseΔ/Δ) mice. VilseΔ/Δ mice displayed impaired spatial memory in water maze and Y-maze tests. Electrical stimulation in hippocampal CA1 region revealed that the synaptic transmission and plasticity were defected in VilseΔ/Δ mice. Collectively, our results demonstrate that Vilse is essential for embryonic development and required for spatial memory.


Subject(s)
CA1 Region, Hippocampal/physiology , Dendrites/physiology , GTPase-Activating Proteins/metabolism , Neuronal Plasticity/physiology , Pyramidal Cells/physiology , Animals , CA1 Region, Hippocampal/cytology , CA1 Region, Hippocampal/metabolism , Dendrites/metabolism , Female , GTPase-Activating Proteins/genetics , Genes, Lethal/genetics , Male , Maze Learning/physiology , Mice, Inbred C57BL , Mice, Knockout , Mice, Transgenic , Neuronal Plasticity/genetics , Pyramidal Cells/metabolism , Spatial Memory/physiology , Synaptic Transmission/genetics , Synaptic Transmission/physiology
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