Objective: To observe the ultrastructure of human oocytes at different maturity stages and morphologies before and after in vitro maturation.
Design: Case report.
Setting: University-based center for human reproduction.
Patient(s): A 28-year-old patient with polycystic ovary syndrome undergoing IVM/IVF-ET treatment.
Intervention(s): Human chorionic gonadotropin was given to the patient 36 hours before her oocytes were retrieved by transvaginal aspiration.
Main Outcome Measure(s): Ultrastructure of human oocytes matured in vitro.
Result(s): Obvious ultrastructural differences were found in oocytes at different maturity stages between those cultured in vitro and those matured in vivo. Degenerate structures were observed in abnormal oocytes. Granulosa cell apoptosis rates from abnormal oocytes were higher than those from normal oocytes. Cumulus cells surrounding morphologically abnormal oocytes had a significantly higher frequency of cell apoptosis, as compared with morphologically normal oocytes.
Conclusion(s): Obvious ultrastructural differences were found between the oocytes matured in vitro and in vivo.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.fertnstert.2009.02.010 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Synaptic Targets and Cellular Sources of CB1 Cannabinoid Receptor and Vesicular Glutamate Transporter-3 Expressing Nerve Terminals in Relation to GABAergic Neurons in the Human Cerebral Cortex.
Eur J Neurosci
January 2025
Department of Pharmacology, University of Oxford, Oxford, UK.
Cannabinoid receptor 1 (CB1) regulates synaptic transmission through presynaptic receptors in nerve terminals, and its physiological roles are of clinical relevance. The cellular sources and synaptic targets of CB1-expressing terminals in the human cerebral cortex are undefined. We demonstrate a variable laminar pattern of CB1-immunoreactive axons and electron microscopically show that CB1-positive GABAergic terminals make type-2 synapses innervating dendritic shafts (69%), dendritic spines (20%) and somata (11%) in neocortical layers 2-3.
View Article and Find Full Text PDFStructure of transmembrane AMPA receptor regulatory protein subunit γ2.
Nat Commun
January 2025
Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Transmembrane AMPA receptor regulatory proteins (TARPs) are claudin-like proteins that tightly regulate AMPA receptors (AMPARs) and are fundamental for excitatory neurotransmission. With cryo-electron microscopy (cryo-EM) we reconstruct the 36 kDa TARP subunit γ2 to 2.3 Å, which points to structural diversity among TARPs.
View Article and Find Full Text PDFElectron Tomography of Organelles and Vesicles in the Investigation of SNARE Function and Localization.
Methods Mol Biol
January 2025
Cambridge Institute for Medical Research (CIMR) and Department of Clinical Biochemistry, University of Cambridge School of Clinical Medicine, Cambridge, UK.
Electron tomography can provide additional morphological information not easily obtained by conventional transmission electron microscopy of thin sections. It uses a goniometer stage in the electron microscope to tilt the specimen and collect a series of 2D images from different orientations, which are combined to provide a 3D volume tomogram and a colored reconstruction of the morphological feature(s) of interest. Here we describe the protocols for its use in visualizing changes in organelle morphology after depletion of the SNARE proteins VAMP7 and VAMP8 and to study VAMP7 localization on endolysosomes/lysosomes.
View Article and Find Full Text PDFTargeted Activation of OGG1 Inhibits Paraptosis in Lens Epithelial Cells of Early Age-Related Cortical Cataract.
Invest Ophthalmol Vis Sci
January 2025
Eye Institute, Affiliated Hospital of Nantong University, Medical School of Nantong University, Nantong, Jiangsu, China.
Purpose: To investigate potential modes of programmed cell death in the lens epithelial cells (LECs) of patients with early age-related cortical cataract (ARCC) and to explore early-stage intervention strategies.
Methods: Anterior lens capsules were collected from early ARCC patients for comprehensive analysis. Ultrastructural examination of LECs was performed using transmission electron microscopy.
Cryo-EM structure of an activated GPR4-Gs signaling complex.
Nat Commun
January 2025
Shanghai Frontiers Science Center of Genome Editing and Cell Therapy, Shanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
Article Synopsis
- G protein-coupled receptor 4 (GPR4) is part of a group called proton-sensing GPCRs that respond to pH changes and regulate various physiological functions, with its overactivation noted in acidic tumor environments.
- Researchers used cryo-electron microscopy to determine the 3D structures of zebrafish GPR4 at different pH levels, revealing important histidine and acidic residues that affect its proton-sensing ability, alongside key triad residues.
- The study also identified a cluster of aromatic residues in GPR4's orthosteric pocket that may play a crucial role in transferring signals to the inside of the cell, laying the groundwork for further research on psGPCRs.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!