Ask about this productRelated genes to: NLRP5 Blocking Peptide
- Gene:
- NLRP5 NIH gene
- Name:
- NLR family pyrin domain containing 5
- Previous symbol:
- NALP5
- Synonyms:
- PYPAF8, MATER, PAN11, CLR19.8
- Chromosome:
- 19q13.43
- Locus Type:
- gene with protein product
- Date approved:
- 2003-10-28
- Date modifiied:
- 2016-06-01
Related products to: NLRP5 Blocking Peptide
Related articles to: NLRP5 Blocking Peptide
- Human preimplantation embryo arrest (PREMBA) represents a significant clinical hurdle in assisted reproductive technology (ART), in which approximately 10% of in vitro fertilized (IVF) embryos arrest at the cleavage stages. Whole-exome sequencing (WES) studies have discovered numerous genetic mutations associated with preimplantation embryo arrest. These mutations often disrupt critical biological milestones such as maternal mRNA clearance (, , ), subcortical maternal complex (, , , , , , ), DNA double-strand break formation and homologous recombination (, , , , ), spindle assembly ( and ) and cell cycle and checkpoints (, , , , ), as well as nuclear transport and translational regulation (, ). However, the cause of most clinical cases remains genetically unexplained. Studies investigating these unexplained arrests have uncovered widespread multi-omics abnormalities, including transcriptional arrest, DNA hypermethylation, higher chromatin accessibility, aberrant histone modification, chromosomal aneuploidy and senescent-like states. This review provides a comprehensive overview of the molecular mechanisms underlying PREMBA, categorized into those that are attributable to known genetic mutations and those with unexplained reasons. - Source: PubMed
Publication date: 2026/02/25
Jiang JiananPeng JunhuaLi LinXu Min - Early embryonic arrest (EEA) can result in repeated failures of assisted reproductive technology, with genetic variation being the primary cause. The maternal protein nucleotide-binding oligomerization domain-like receptor protein 5 (NLRP5) plays a role in oocyte maturation and embryonic development before the blastocyst stage. Mutations in the NLRP5 gene can lead to various reproductive outcomes, including oocyte maturation disorder, fertilization failure, and EEA. We discovered a new homozygous nonsense mutation (c.779G > A; p.Trp260*) in NLRP5 in two sisters from a Chinese family. This clinically presented as halted embryonic development at the 2-7 cell stage. The parents and brother were heterozygous carriers and exhibited normal fertility, indicating that the pathogenic gene was inherited in an autosomal recessive manner. Analyses revealed significantly decreased expression of NLRP5 at the 3' end of the mRNA and the C-terminal of the protein ( < 0.05). This suggests that NLRP5 protein dysfunction is the primary cause of EEA in this case. Additionally, the expression levels are inconsistent with those of previous studies, indicating that different mutation sites lead to variations in NLRP5 protein expression and distinct pathogenic mechanisms. Our finding expands the spectrum of pathogenic variants in EEA caused by the NLRP5 gene. - Source: PubMed
Publication date: 2026/02/17
Xu QinDeng YumeiHuo JingjingYan YuanlongZhang YangjiaMa YaxianZhuan Li - Ovarian aging is considered the "pacemaker" and "biological clock" of systemic female aging, with early manifestations that are often insidious. In this study, we analyzed the shared and distinct molecular signatures between physiological and pathological ovarian aging models using proteomic approaches, with the aim of identifying early predictive markers and therapeutic targets for ovarian aging, evaluating model fidelity, and elucidating underlying molecular mechanisms. - Source: PubMed
Publication date: 2025/11/28
Bai MengyingZhang LiujuanWu WenboWeng RuoxinWu HaifengLi YuanLing ShuyiZheng Yuehui - Nlrp5 encodes a core component of the subcortical maternal complex (SCMC), a cytoplasmic protein structure unique to the mammalian oocyte and cleavage-stage embryo. NLRP5 mutations have been identified in patients presenting with early embryo arrest, recurrent molar pregnancies, and imprinting disorders. Correct patterning of DNA methylation over imprinted domains during oogenesis is necessary for faithful imprinting of genes. It was previously shown that oocytes with mutation in the human SCMC gene KHDC3L had globally impaired methylation, indicating that integrity of the SCMC is essential for correct establishment of DNA methylation at imprinted regions. Here, we present a multi-omic analysis of an Nlrp5-null mouse model, which in germinal vesicle (GV)-stage oocytes displays a misregulation of a broad range of maternal proteins, including proteins involved in several key developmental processes. This misregulation likely underlies impaired oocyte developmental competence. Amongst impacted proteins are several epigenetic modifiers, including a substantial reduction in DNMT3L; we show that de novo DNA methylation is attenuated in Nlrp5-null oocytes, including at some imprinting control regions. This provides evidence for a mechanism of epigenetic impairment in oocytes, which could contribute to downstream misregulation of imprinted genes. - Source: PubMed
Nic Aodha LeahPokhilko AlexandraRosen Leah UGalatidou StylianiWalewska EdytaBelton ChristianGalvao AntonioOkkenhaug HannekeYu LuNakhuda AsifMansfield BillKhan SoumenOxley DavidBarragán MontserratKelsey Gavin - The subcortical maternal complex (SCMC) is essential for mammalian preimplantation development, yet how SCMC (MATER/NLRP5, TLE6, FLOPED/OOEP) engages regulatory partners remains unclear. We determined cryo-EM structures of mouse SCMC bound to ZBED3 and human SCMC bound to NLRP2. Our structure reveals that ZBED3 interacts with all three SCMC subunits via its zinc finger domain, with conserved residue Phe73 mediating specific contacts. In contrast, human NLRP2 only binds to the WD40 domain of TLE6 through its leucine-rich repeat (LRR) domain. Similar interactions were also confirmed for NLRP7 with TLE6. These findings were cross-validated by in vivo proximity ligation and in vitro pull-down assays. Our work proposes a paradigmatic "Lego-like" assembly model, where the SCMC sequentially recruits different partners through diverse molecular interfaces. These findings provide critical structural insights into the SCMC's architecture and its multifaceted regulatory roles in early mammalian embryogenesis. - Source: PubMed
Publication date: 2025/10/20
Ou GuojinLiu QingtingJiao HaizhanHan ZhuoLi JinhongMin LingChi PengliangLiu SibeiLi JialuQi QianqianZhang ZihanGuo LiWang XiangLi LeiChen JingHu HongliDeng Dong