Ask about this productRelated genes to: RAB37 antibody
- Gene:
- RAB37 NIH gene
- Name:
- RAB37, member RAS oncogene family
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 17q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-26
- Date modifiied:
- 2016-10-05
Related products to: RAB37 antibody
Related articles to: RAB37 antibody
- The systematic aggregation of distinct admixed subpopulations into broad racial categories creates genomic blind spots that undermine the promise of precision medicine. Black Hawaiians (BH) exemplify this exclusion. Characterized by a unique tri-continental ancestry (African, European, and Native Hawaiian/Pacific Islander) and disproportionate cardiometabolic burden, their population-specific risk drivers remain masked by systematic conflation with broader ancestral cohorts. - Source: PubMed
Publication date: 2026/01/27
Vand KasraBadía NelsonKhomtchouk Bohdan B - Tumor-associated Macrophages (TAMs) are highly plastic immune cells that shape the tumor microenvironment (TME) and influence cancer progression. However, the molecular determinants governing their functional heterogeneity remain incompletely understood. In this study, we identify Rab37 as a key regulator that remodels the states of macrophages within the lung TME. Single-cell RNA sequencing revealed that Rab37 wild-type (WT) tumors were enriched in immunosuppressive Spp1 TAMs, whereas Rab37 knockout (KO) tumors contained a higher proportion of Thbs1 TAMs, suggesting Rab37-dependent shifts in macrophage programming. Mechanistically, Rab37 promoted osteopontin (OPN) secretion, which activated STAT3 signaling to establish an autocrine feedback loop that sustained Spp1 expression and induced M2-like polarization. Paracrine OPN signaling further enhanced lung cancer cell proliferation, migration, and invasion. In clinical lung cancer specimens, CD163/Rab37/OPN TAMs correlated with recurrence and poor survival, and multivariate analysis confirmed their independent prognostic value. Together, these findings demonstrate that Rab37 governs macrophage phenotype and function by orchestrating OPN/STAT3 signaling, thereby reinforcing an immunosuppressive TME and promoting lung cancer progression. Targeting the Rab37-OPN axis may thus represent a promising therapeutic strategy. - Source: PubMed
Publication date: 2026/01/14
Yang You-EnLin Yu-AnLing Lun-LingKuo I-YingKuo Wan-TingLiu HsuanWang Yi-Ching - Ventilator-induced diaphragmatic dysfunction (VIDD) is characterized by diaphragmatic atrophy and contractile failure, leading to prolonged intensive care unit (ICU) stays and increases mortality. While phrenic nerve stimulation (PNS) has demonstrated efficacy in mitigating VIDD by preserving diaphragmatic activity, its underlying molecular mechanisms remain unclear. This study aimed to elucidate the role of competing endogenous RNA (ceRNA) networks in PNS-mediated protection against VIDD through integrated miRNA-Seq and RNA-Seq analyses in a rabbit model. Eleven adult male New Zealand white rabbits were divided into control (n = 4), MV (n = 3) and PNS groups (n = 4). MV and PNS groups underwent 24 h of MV, with intermittent bilateral transvenous PNS applied only to the PNS group. Differentially expressed (DE) analysis of mRNAs, miRNAs and circRNAs across pairwise group comparisons was performed via RNA-seq and miRNA-seq. Functional enrichment analyses (Gene Ontology and Kyoto Encyclopedia of Genes and Genomes) identified key pathways. Potential miRNA targets and interacting circRNAs were computationally predicted. An integrated ceRNA network was constructed using major DE RNAs to identify PNS-associated core regulators. CeRNA network was validated by quantitative real-time polymerase chain reaction (RT-qPCR) and dual-luciferase assays. High-throughput sequencing revealed significant dysregulation of miRNAs, circRNAs and mRNAs in the diaphragm following MV which was partially reversed by PNS. Bioinformatic screening identified a ceRNA network, wherein two key miRNAs emerged: miR-500-3p (targeting RAB37, an autophagy-related gene) and miR-133b-3p (targeting L-selectin, a cell adhesion molecule regulating immune responses and fibrosis). Both miRNAs were down-regulated after MV and restored by PNS. Computational prediction also identified five circRNAs (circRNA_12437, 24673, 14127, 14942, 12463) as putative sponges for these miRNAs, although this interaction lacks experimental confirmation. Dual-luciferase assays confirmed direct binding of miR-500-3p to RAB37 and miR-133b-3p to L-selectin, functionally linking them to PNS-mediated VIDD protection. Enrichment analyses indicated that DE genes were predominantly enriched in phagosome activity and cell adhesion molecule pathways. Collectively, these findings suggest that PNS preserves diaphragmatic function by modulating ceRNA networks to suppress excessive autophagy and immune cell infiltration. This study identifies the first PNS-responsive ceRNA network in VIDD pathogenesis. Our data highlight the potential critical roles of miR-500-3p-RAB37 and miR-133b-3p-L-selectin axes in regulating autophagy and immune responses. These results provide mechanistic insights and suggest potential therapeutic targets for diaphragm dysfunction. - Source: PubMed
Publication date: 2025/12/15
Zhang MingmingLi FangyuanWang MinLi LeiHao WenyanDuan XuejiaoZhang Dong - Glioblastoma (GBM), a highly vascularized and aggressive primary brain tumor, presents unresolved questions regarding the functional significance of angiogenesis-related genes (ARGs) in disease progression. To systematically investigate this, we employed univariate Cox regression followed by LASSO regression analysis to identify prognosis-associated ARGs. These candidates were subsequently evaluated using six machine learning-derived survival prediction algorithms, with model interpretability achieved through SHapley Additive exPlanations (SHAP) analysis. Our studies revealed that six hub ARGs (BMP2, FSCN1, NET1, AEBP1, SEMA3G, and RAB37) were identified and incorporated into a novel risk stratification model (high and low risk groups). High-risk patients demonstrated significantly poorer overall survival in the CGGA-GBM, GSE43378, and GSE7696 cohorts. Moreover, the high-risk group exhibited an immunosuppressive tumor microenvironment profile (e.g., elevated Treg infiltration, P < 0.0001), increased extracellular matrix stiffness (via mechanosensing markers) and differential drug sensitivity (OncoPredict analysis). Immunofluorescence confirmed co-localization of the hub protein FSCN1 with vascular (CD31⁺), stromal (α-SMA⁺), and mesenchymal (Vimentin⁺) compartments, suggesting its multifunctional role in GBM pathobiology. In summary, our research established the ARG-derived prognostic signature validated across independent GBM cohorts and revealed concomitant immune and mechanical niche dysregulation in high-risk patients. The rationale for combined angiogenesis/stroma/immune modulation strategies was provided, with FSCN1 proposed as the potential therapeutic target. - Source: PubMed
Publication date: 2025/11/24
Yang FanPeng ChiYang SisiBian XiuwuYao Xiaohong - DENN/MADD (mitogen-activated protein kinase-activating death domain), a differentially expressed in normal and neoplastic cells (DENN) domain-containing protein functions in membrane trafficking. DENN domain-bearing proteins have guanine nucleotide exchange factor activity toward Rab GTPases. Here, we identify Rab GTPase substrates for DENN/MADD using a cell-based assay involving DENN domain-mediated recruitment of Rab substrates to mitochondria. We confirmed known interactions of DENN/MADD with Rab3A, Rab3B, Rab3C, Rab3D, and Rab27B and identified four new potential substrates, Rab8B, Rab15, Rab26, and Rab37, results confirmed with biochemical experiments. Mutations in the DENN domain of DENN/MADD result in diverse pathophysiological manifestations, ranging from predominant neurological dysfunction to a multisystem disorder. Structural analysis using AlphaFold suggested that these mutations affect DENN/MADD's interaction with Rab GTPases. Introducing such mutations into DENN/MADD's DENN domain influenced the mitochondrial recruitment of Rabs. This study identifies new DENN/MADD protein interactions and cellular pathways, the disruption of which results in human disorders. - Source: PubMed
Publication date: 2025/08/12
Khan MaleehaKumar RahulTrempe Jean-FrançoisFrancis VincentBanks EmilyAyoubi RihamLuna Luis AguileraMcPherson Peter S