Oocyte activation deficiency leads to female infertility. [Ca ] oscillations are required for mitochondrial energy supplement transition from the resting to the excited state, but the underlying mechanisms are still very little known. Three mitochondrial Ca channels, Mitochondria Calcium Uniporter (MCU), Na /Ca Exchanger (NCLX) and Voltage-dependent Ca Channel (VDAC), were deactivated by inhibitors RU360, CGP37157 and Erastin, respectively. Both Erastin and CGP37157 inhibited mitochondrial activity significantly while attenuating [Ca ] and [Ca ] oscillations, which caused developmental block of pronuclear formation. Thus, NCLX and VDAC are two mitochondria-associated Ca transporter proteins regulating oocyte activation, which may be used as potential targets to treat female infertility. SIGNIFICANCE OF THE STUDY: NCLX and VDAC are two mitochondria-associated Ca transporter proteins regulating oocyte activation.
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http://dx.doi.org/10.1002/cbf.3571 | DOI Listing |
Alzheimers Dement
December 2024
Indiana University, Bloomington, IN, USA.
Background: The roles of Aβ in the pathogenesis of Alzheimer 's disease (AD) include disruption of synaptic communication/function and synaptic plasticity mechanisms thought to underlie learning and memory. Exactly how these abnormal processes arise is incompletely understood, but evidence suggests that dysregulation of intracellular Ca levels is involved in alterations of neuronal excitability, synaptic remodeling, and neurodegeneration in AD. Our lab has focused on the potential involvement of voltage-gated potassium channels (VGKCs) in these processes, particularly Kv1.
View Article and Find Full Text PDFAndrology
January 2025
Institute for Advanced Biosciences, INSERM U 1209, CNRS UMR 5309, Université Grenoble Alpes, Team "Physiopathology and Pathophysiology of Sperm Cells", Grenoble, France.
Background: In mammals, sperm fertilization potential relies on efficient progression within the female genital tract to reach and fertilize the oocyte. This fundamental property is supported by the flagellum, an evolutionarily conserved organelle, which contains dynein motor proteins that provide the mechanical force for sperm propulsion and motility. Primary motility of the sperm cells is acquired during their transit through the epididymis and hyperactivated motility is acquired throughout the journey in the female genital tract by a process called capacitation.
View Article and Find Full Text PDFCell Commun Signal
January 2025
Key Laboratory of Research on Clinical Molecular Diagnosis for High Incidence Diseases in Western Guangxi of Guangxi Higher Education Institutions, Reproductive Medicine of Guangxi Medical and Health Key Discipline Construction Project, Affiliated Hospital of Youjiang Medical University for Nationalities, Baise, China.
Leucine-rich repeat kinase 2 (LRRK2) is a ROCO family member which its mutation is closely related with Parkinson's disease, and LRRK2 is widely involved into the regulation of autophagy, vesicle transport and neuronal proliferation. However, the roles of LRRK2 during mammalian oocyte maturation are still largely unclear. In present study, we disturbed the activity of LRRK2 and showed its essential roles in porcine oocytes.
View Article and Find Full Text PDFCell Commun Signal
January 2025
Laboratory of Theriogenology, College of Veterinary Medicine, Chungnam National University, Daejeon, 34134, Republic of Korea.
Background: Although the Notch signaling pathway is known to play an important role in ovarian follicle development in mammals, whether it is involved in oocyte maturation remains unclear. Therefore, this study was performed to elucidate the existence and role of the Notch signaling pathway during oocyte maturation in a porcine model.
Methods: Reverse transcription-polymerase chain reaction (RT-PCR) and immunocytochemical assays were used to determine the existence of Notch signaling pathway-related transcripts and proteins in porcine cumulus-oocyte complexes (COCs).
Nat Commun
January 2025
Key Laboratory of Epigenetic Regulation and Intervention, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
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