Ask about this productRelated genes to: RPL38 antibody
- Gene:
- RPL38 NIH gene
- Name:
- ribosomal protein L38
- Previous symbol:
- -
- Synonyms:
- L38
- Chromosome:
- 17q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-07-28
- Date modifiied:
- 2015-08-25
Related products to: RPL38 antibody
Related articles to: RPL38 antibody
- Pronuclear Envelope Breakdown (PNEB) failure is a critical factor contributing to the early developmental arrest of intracytoplasmic sperm injection (ICSI) embryos; however, its molecular mechanism remains inadequately understood. This study aimed to elucidate the core regulatory network underlying PNEB failure occurrence and its impact on embryonic development. Single-cell sequencing was used to identify differentially expressed genes (DEGs) between PNEB‑type two pronuclei (2PN) zygotes and 3PN control zygotes, and weighted gene coexpression network analysis (WGCNA) was performed to identify module genes associated with PNEB failure. The least absolute shrinkage and selection operator was applied to model disease types and screen core genes, thereby establishing a multiomics integration strategy. Reactive oxygen species (ROS) and 5,5',6,6'-tetrachloro-1,1',3,3'-tetraethylbenzimidazolocarbocyanine iodide (JC-1) fluorescence staining were conducted to analyze oxidative stress and mitochondrial function. A total of 1294 DEGs were identified, including genes involved in the oxidative phosphorylation pathway. Mitochondrially encoded reduced nicotinamide adenine dinucleotide dehydrogenase 1 (MT-ND1) and mitochondrially encoded cytochrome c oxidase III (MT-CO3) were significantly upregulated, whereas genes associated with the DNA repair pathway were downregulated. WGCNA revealed a light-green module strongly associated with PNEB failure (r = 0.89, P = 1.2e - 5). Hub genes, ribosomal protein L10a (RPL10A) and ribosomal protein L38 (RPL38), within this module were implicated in ribosome biogenesis. The PPI network confirmed functional interactions between MT-ND1 and RPL10A, suggesting that dysregulated mitochondrial function and ribosomal assembly are central to PNEB failure. ROS and JC-1 fluorescence staining showed a significant decrease in the JC-1 red/green fluorescence intensity ratio in the PNEB failure group (p < 0.05), while ROS levels were significantly elevated (p < 0.01). This study reveals that mitochondrial metabolic dysfunction and ribosomal assembly abnormalities contribute to PNEB failure, thereby disrupting nuclear envelope stability. Furthermore, it identifies the MT-ND1-RPL10A/RPL38 axis as a potential novel molecular marker for assessing ICSI embryo quality. - Source: PubMed
Wang ChaoyingFang JunnanYang GuangJiang RanJin HaixiaSong WenyanShi SenlinZhai JunWang HuihuiZhang TongweiYao Guidong - Members of the Ribosomal Protein L (RPL) family are involved in diverse biological processes and cancer biology, yet their precise functions and clinical implications in lung adenocarcinoma (LUAD) remain incompletely understood. - Source: PubMed
Publication date: 2026/02/12
Zhang LuTeng FeiWang YuanChen YangLiu QiuxiaDai FengshengYu LiangYao ChenguoWang Zhiqiang - Oral squamous cell carcinoma (OSCC) is one of the most common malignant tumors worldwide. This necessitates the development of innovative drugs with high efficiency, low toxicity, and good tolerance. Bitter melon extract has been reported to have potent anticancer activity against OSCC. We evaluated the effects of nine triterpenoids from bitter melon extract on OSCC using cell counting kit-8 (CCK-8) proliferation and Transwell migration assays. Among the nine triterpenoids, momordicine I (MI) exhibited the strongest anticancer activity against OSCC. Animal experiments also showed that MI inhibited OSCC cell growth in vivo. Additionally, MI decreased the mitochondrial membrane potential and promoted apoptosis in OSCC. RNA-sequencing (RNA-seq) analysis revealed that MI induced an unfolded protein response (UPR) and endoplasmic reticulum (ER) stress, which was confirmed by western blotting and reverse transcription-quantitative polymerase chain reaction (RT-qPCR). Cellular thermal shift assay (CETSA) and mass spectrometry (MS) analysis, combined with molecular docking, identified ribosomal proteins (ribosomal protein L7 (RPL7), RPL11, RPL12, RPL18, RPL30, RPL38, RPS13, and RPS25) as MI targets. By targeting ribosomal proteins, MI likely disrupts ribosome-mediated protein folding, leading to the UPR and ER stress. In summary, MI targets ribosomal proteins to induce ER stress and inhibit OSCC, highlighting its therapeutic potential. - Source: PubMed
Publication date: 2025/12/22
Kong JianluZhu ZiyuHu YijieZhou SiyiGu TianyiShen XiaoWang HuimingYu MengfeiLiu Yu - Triple-negative breast cancer (TNBC) is the most aggressive form of breast cancer that is associated with poor prognosis and a high risk of relapse, with limited treatment options. While the induction of senescence, a state of arrested cell growth, is generally achieved by available anticancer treatments, senescence can adversely promote tumorigenesis through an upheld augmented inflammatory state called senescence-associated secretory phenotype (SASP). Thus, the precise delineation of underlying regulatory mechanisms governing senescence is urgently needed. Herein, we investigated the beneficial anticancer senescence response elicited by silencing the expression of the promyelocytic leukemia protein (PML) in TNBC, where it exerts an oncogenic role. Functional genomics studies implicated the downregulation of a specific set of ribosomal protein (RP) genes tied to poor clinical outcome. Re-introduction of RPL38 or RPL39L alone, but not RPS14, a favorable outcome-associated RP, was sufficient to block the senescence phenotype induced by PML knockdown. RP gene regulation by PML was found to involve the assembly of a previously unrecognized PML-mTOR-RONIN transcriptional complex at their promoters. Furthermore, we show that RONIN levels are elevated in TNBC and that RONIN silencing can recapitulate the senescent phenotype of PML-deficient cells. This work offers new therapeutic insights for TNBC that involve senescence-inducing therapies or senolytics. - Source: PubMed
Publication date: 2025/11/08
Medkour YounesDufour Catherine RosaHan LingweiHutton PhillipeFarhat MirnaAlfonso AnthonyRambur AmandineVernier MathieuGiguère Vincent - The fate of hematopoietic stem cells (HSCs) is determined by a complex regulatory network supporting self-renewal and quiescence within a niche. Umbilical cord mesenchymal stromal cells (UC-MSCs) are classified as an alternative niche for the expansion of hematopoietic stem and progenitor cells (HSPCs). The molecular mechanisms by which UC-MSCs regulate hematopoiesis are still not fully understood. In this study, the cocultures of UC-MSCs and umbilical cord blood CD34+ (UCB-CD34+) cells were established. Immunophenotype, cell proliferation, and hematopoietic function of UCB-CD34+ cells were evaluated on days 0 to 7. UC-MSCs promoted UCB-CD34+ cell proliferation but were less effective at preserving their stemness. Notably, UC-MSCs promoted the myeloid lineage commitment, significantly observed on day 3. Integrative transcriptomic analysis highlighted the molecular signature and regulatory networks of UC-MSCs. The long non-coding RNA (lncRNA)-RNA binding protein (RBP) interaction network and lncRNA cis- and trans-regulatory networks were evident. The significant 3-gene modules and a set of 10-hub genes were identified in the protein-protein interaction (PPI) network, including RPS16, CD74, RPL35, COX7C, RPL38, RPS28, RPS27, RPS10, TARDBP, and TOMM7. These findings exemplify the niche activity of UC-MSCs in regulating cell differentiation, genomic stability maintenance, and modulation of the hematopoietic supportive niche. The transcriptional landscape, together with the identified regulatory networks, gene modules, and key hub genes provide new insights into the molecular mechanisms of UC-MSCs and establish a basis for refining ex vivo culture systems for therapeutic HSC expansion. - Source: PubMed
Srimorkun PornprapaSuanpan KittisakAtjanasuppat KorakotSawaisorn PiamsiriSomchit WerapathSiriboonpiputtana TeerapongNathalang OytipHongeng SuradejPetvises SawangAnurathapan Usanarat