RAB5A Antibody
- Known as:
- RAB5A Antibody
- Catalog number:
- 32209
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- RAB5A Antibody
Related genes to: RAB5A Antibody
- Gene:
- RAB5A NIH gene
- Name:
- RAB5A, member RAS oncogene family
- Previous symbol:
- RAB5
- Synonyms:
- -
- Chromosome:
- 3p24.3
- Locus Type:
- gene with protein product
- Date approved:
- 1990-01-22
- Date modifiied:
- 2015-06-29
Related products to: RAB5A Antibody
Related articles to: RAB5A Antibody
- Visceral white-nodules disease (VWND), caused by , poses a severe threat to the large yellow croaker () aquaculture industry. Although breeding resistant strains is a promising strategy, the molecular basis of disease resistance in this host remains poorly understood. Here, 1500 fish were artificially infected, and extreme phenotypes (30 resistant, RL; 30 susceptible, SL) were selected based on survival time and liver pathogen load. Liver histopathology revealed that RL fish maintained intact architecture with only mild vacuolation, whereas SL fish exhibited widespread necrosis, inflammation, and hemosiderin deposition. Consistently, RL fish showed lower MDA levels and higher GSH-Px activity and TAC. Transcriptomic analysis identified 172 differentially expressed genes (DEGs): RL fish were characterized by upregulation of anti-inflammatory and tissue-protective genes (, ) and downregulation of pro-coagulant factors (, ). Proteomic analysis identified 111 differentially expressed proteins, with significantly enriched pathways including the peroxisome, pentose phosphate, and phagosome pathways. Integrated cross-omics analysis revealed eight co-enriched KEGG pathways; among them, arginine/proline metabolism, phagosome, oxidative phosphorylation, and focal adhesion were consistently upregulated in the RL group. These findings suggest that effective resistance to VWND in may involve a coordinated, multi-layered defense program encompassing redox balance, regulated immune responses, metabolic reprogramming, and cellular homeostasis. Cross-omics-supported candidate factors (e.g., , COX6B, RAB5A, ) represent promising targets for functional validation via DNA-level experiments in independent sample sets, and the prominent enrichment of arginine-proline metabolism indicates a potential target for dietary intervention that merits further investigation. - Source: PubMed
Publication date: 2026/08/12
Ye TingZhu JiajieLiang XiaoGuo DandanZhou YilianLou BaoLiu Feng - Neurodegenerative tauopathies, including Alzheimer's disease, appear to be driven by propagation of tau assemblies, which must access the cytoplasm to recruit monomer and self-replicate, a process termed "seeding." The prevailing model holds that tau seeds enter cells via macropinocytosis and reach the cytosol through lysosomal rupture or micro-perforation. Our findings revise this model by revealing that endocytosis is not required for seeding. Using genome-scale CRISPR screening, we identified multiple v-ATPase components whose loss reduced tau uptake (measured by flow cytometry) yet paradoxically increased seeding (measured by FRET biosensors). Acute v-ATPase inhibition with bafilomycin A1 produced the same effect in v2L tau biosensors and iPSC-derived neurons. Among regulators of endosome maturation, dominant-negative Rab5a decreased internalization while enhancing cytoplasmic templating. Cholesterol depletion produced identical results. Strikingly, transient hypothermia eliminated virtually all detectable tau uptake and dramatically increased seeding, without affecting subsequent tau monomer or aggregate degradation. We conclude that efficient endolysosomal trafficking does not appear to be required for cytoplasmic seeding under the conditions studied here. Across diverse perturbations, reduced endolysosomal flux consistently enhanced tau seeding, consistent with prior work indicating that most internalized aggregates are routed toward degradation rather than amplification. To seed effectively, tau must cross the plasma or vesicular membranes into the cytoplasm. We have found that proper endolysosomal trafficking suppresses cytoplasmic tau seeding, as all perturbations augmented this process. These findings reframe the role of the endolysosomal system in tau seeding and identify membrane transit rather than macropinocytosis itself as a critical gateway to cytoplasmic tau amplification. - Source: PubMed
Publication date: 2026/08/26
Dodd Dana ALaCroix Michael SValdez ClarissaMendoza-Oliva AydeBeaver Joshua DVega Anthony RKumar AshwaniXing ChaoWhite Charles LDiamond Marc I - Major depressive disorder (MDD) and schizophrenia (SCZ) are severe psychiatric disorders, the molecular mechanisms of which remain incompletely understood. Increasing evidence implicates neuroinflammatory signaling, autophagy dysregulation, and unfolded protein response (UPR) alterations in their pathophysiology. Here, we analyzed dorsolateral prefrontal cortex (DLPFC) samples from postmortem human brains of 28 MDD subjects, 28 SCZ subjects, and 28 matched controls. Gene expression levels of key inflammatory, autophagy, and UPR-related markers were assessed by RT-qPCR, while selected proteins were quantified by Western blot and ELISA. Logistic and linear regression models were applied to evaluate disease-associated alterations and the influence of sex, age, and cause of death. Transcriptional analyses revealed pathway-specific alterations in both disorders, with IRE1α emerging as the most consistently upregulated marker across MDD and SCZ. Sex-stratified analyses indicated that risk-associated transcriptional changes were more prominent in men with MDD, whereas women with SCZ showed broader transcriptional alterations. Age-related effects were mainly detected at the mRNA level, particularly in autophagy-related genes. In contrast, protein analyses showed a generalized downregulation of several inflammatory (AIM2, NLRP3), autophagy (ATG7, mTOR, RAB5A), and UPR-related (IRE1α) proteins in both disorders. In SCZ subjects who died by suicide, increased IL18, CASPASE-5, and IRE1α transcription, together with increased CASPASE-8 protein levels, suggested enhanced inflammatory and stress-related signaling. Overall, these findings reveal a marked transcription-protein dissociation in key cellular stress pathways in the DLPFC of MDD and SCZ subjects, supporting multilayer regulation of inflammatory, autophagy-related, and UPR responses in the psychiatric brain. - Source: PubMed
Publication date: 2026/08/17
Ulecia-Morón CristinaBris Álvaro GInglada-Pérez LucíaCallado Luis FMeana J JavierMartín-Hernández DavidMacDowell Karina SFiguero ElenaCaso Javier RLeza Juan C - The journal retracts the article "The Autophagic Process Occurs in Human Bone Metastasis and Implicates Molecular Mechanisms Differently Affected by Rab5a in the Early and Late Stages" [...]. - Source: PubMed
Publication date: 2026/07/22
Maroni PaolaBendinelli PaolaResnati MassimoMatteucci EmanuelaMilan EnricoDesiderio Maria Alfonsina - Seed storage proteins (SSPs), which accumulate specifically during seed development, constitute a major source of plant-derived protein in the human diet. Despite their critical role in determining crop quality, the molecular mechanisms underlying the intracellular trafficking of SSPs remain poorly understood. Here, we characterize the rice glutelin precursor accumulation16 (gpa16) mutant, which exhibits defective dense vesicle (DV)-mediated post-Golgi trafficking of proglutelins, resulting in their overaccumulation in the apoplast. GPA16 encodes OsOSCA2.4, a member of the reduced hyperosmolality-induced Ca2+ increase channel (OSCA) family. OsOSCA2.4 localizes to post-Golgi compartments including the trans-Golgi network (TGN) and prevacuolar compartment (PVC) in vegetative tissue, and DVs in the endosperm. The OsOSCA2.4(P397L) variant disrupts the formation of the Rab5a molecular module, a process influenced by intracellular Ca2+ homeostasis. Ca2+ imaging assays indicate that OsOSCA2.4 functions as a regulator of Ca2+ homeostasis of PVCs/DVs, the primary sites of Rab5a module activity. Genetic analyses reveal functional redundancy between OsOSCA2.4 and OsOSCA4.1 in modulating post-Golgi trafficking of proglutelins. Collectively, our findings identify OSCA-mediated Ca2+ homeostasis as a previously unrecognized regulatory layer governing post-Golgi trafficking of SSPs and uncover an unexpected role for OSCA proteins in vesicular trafficking in eukaryotes. - Source: PubMed
Zhang YuZhu YunZhang PengchengTian WangDong HuiLiu ZebinChen YuBao XiuhaoPan TianXiong YehuiWang XinRen ZhijieJiang XiaokangHan XiaohangJing RuonanWu HongmingGu ChuanweiChen RongboChen XiaoliLei JieDuan ErchaoLei CailinCheng ZhijunWang JiachangBao YiqunWu ChuanyinWang HaiyangWang YihuaRen YulongWan Jianmin