Ask about this productRelated genes to: MRPS25 antibody
- Gene:
- MRPS25 NIH gene
- Name:
- mitochondrial ribosomal protein S25
- Previous symbol:
- -
- Synonyms:
- MRP-S25, FLJ00023, DKFZp313H0817, RPMS25
- Chromosome:
- 3p25.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-01-26
- Date modifiied:
- 2016-10-05
Related products to: MRPS25 antibody
Related articles to: MRPS25 antibody
- Chronic kidney disease (CKD) is associated with increased atherosclerotic burden and vascular risk, particularly in patients with established coronary artery disease (CAD). Circulating microRNAs may reflect renal dysfunction and systemic vascular injury. We investigated whether plasma miR-148b-3p is associated with renal function and carotid plaque burden in patients with established CAD. - Source: PubMed
Publication date: 2026/08/12
Yang WenboFan HezeZhang WenjiaoXu YiruiKang QiZhang ShumeiFeng XueyingHu ErweiZhang PeiyaoWang JiandongYuan HaoWang LijunYuan ZuyiZhou Juan - Heart failure (HF) is a complex clinical condition characterized by impaired cardiac function and progressive structural remodeling. To elucidate the molecular mechanisms driving HF, this study aimed to identify key regulatory hub genes, explore their functional relevance, and assess their diagnostic and therapeutic potential. - Source: PubMed
Publication date: 2025/08/07
Juncheng JiangLei ChenHao LinFei Liang - Mitochondrial ribosomal proteins (MRPs) are essential components for the structural and functional integrity of the mitoribosome complex. Throughout evolution, the mammalian mitoribosome has acquired new Mrp genes to compensate for loss of ribosomal RNA. More than 80 MRPs have been identified in mammals. Here we document expression pattern of 79 Mrp genes during mouse development and adult tissues and find that these genes are consistently expressed throughout early embryogenesis with little stage or tissue specificity. Further investigation of the amino acid sequence reveals that this group of proteins has little to no protein similarity. Recent work has shown that the majority of Mrp genes are essential resulting in early embryonic lethality, suggesting no functional redundancy among the group. Taken together, these results indicate that the Mrp genes are not a gene family descended from a single ancestral gene, and that each MRP has unique and essential role in the mitoribosome complex. The lack of functional redundancy is surprising given the importance of the mitoribosome for cellular and organismal viability. Further, these data suggest that genomic variants in Mrp genes may be causative for early pregnancy loss and should be evaluated as clinically. - Source: PubMed
Publication date: 2020/09/25
Cheong AgnesLingutla RanjanaMager Jesse - Mitochondria are essential for energy production and although they have their own genome, many nuclear-encoded mitochondrial ribosomal proteins (MRPs) are required for proper function of the organelle. Although mutations in MRPs have been associated with human diseases, little is known about their role during development. Presented here are the null phenotypes for 21 nuclear-encoded mitochondrial proteins and in-depth characterization of mouse embryos mutant for the Mrp genes , , , and Loss of each MRP results in successful implantation and egg-cylinder formation, followed by severe developmental delay and failure to initiate gastrulation by embryonic day 7.5. The robust and similar single knockout phenotypes are somewhat surprising given there are over 70 MRPs and suggest little functional redundancy. Metabolic analysis reveals that Mrp knockout embryos produce significantly less ATP than controls, indicating compromised mitochondrial function. Histological and immunofluorescence analyses indicate abnormal organelle morphology and stalling at the G2/M checkpoint in Mrp null cells. The nearly identical pre-gastrulation phenotype observed for many different nuclear-encoded mitochondrial protein knockouts hints that distinct energy systems are crucial at specific time points during mammalian development. - Source: PubMed
Publication date: 2020/05/26
Cheong AgnesArchambault DanielleDegani RinatIverson ElizabethTremblay Kimberly DMager Jesse - Mitochondrial disorders are clinically and genetically heterogeneous and are associated with a variety of disease mechanisms. Defects of mitochondrial protein synthesis account for the largest subgroup of disorders manifesting with impaired respiratory chain capacity; yet, only a few have been linked to dysfunction in the protein components of the mitochondrial ribosomes. Here, we report a subject presenting with dyskinetic cerebral palsy and partial agenesis of the corpus callosum, while histochemical and biochemical analyses of skeletal muscle revealed signs of mitochondrial myopathy. Using exome sequencing, we identified a homozygous variant c.215C>T in MRPS25, which encodes for a structural component of the 28S small subunit of the mitochondrial ribosome (mS25). The variant segregated with the disease and substitutes a highly conserved proline residue with leucine (p.P72L) that, based on the high-resolution structure of the 28S ribosome, is predicted to compromise inter-protein contacts and destabilize the small subunit. Concordant with the in silico analysis, patient's fibroblasts showed decreased levels of MRPS25 and other components of the 28S subunit. Moreover, assembled 28S subunits were scarce in the fibroblasts with mutant mS25 leading to impaired mitochondrial translation and decreased levels of multiple respiratory chain subunits. Crucially, these abnormalities were rescued by transgenic expression of wild-type MRPS25 in the mutant fibroblasts. Collectively, our data demonstrate the pathogenicity of the p.P72L variant and identify MRPS25 mutations as a new cause of mitochondrial translation defect. - Source: PubMed
Bugiardini EnricoMitchell Alice LRosa Ilaria DallaHorning-Do Hue-TranPitmann Alan MPoole Olivia VHolton Janice LShah SachitWoodward CathyHargreaves IainQuinlivan RosalineAmunts AlexeyWiesner Rudolf JHoulden HenryHolt Ian JHanna Michael GPitceathly Robert D SSpinazzola Antonella