AQP5
- Known as:
- AQP5
- Catalog number:
- 001809A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- AQP5
Ask about this productRelated genes to: AQP5
- Gene:
- AQP5 NIH gene
- Name:
- aquaporin 5
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 12q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 1994-07-25
- Date modifiied:
- 2016-10-05
Related products to: AQP5
Related articles to: AQP5
- The forensic determination of heatstroke (HS) death remains challenging due to the lack of specific autopsy findings and histopathological changes. The diagnostic biomarkers reported in previous studies have not yet been effectively applied in forensic practice. The skin forms the primary interface between the body and the external environment and is central to heat exchange and thermoregulation. Therefore, the skin may capture both local thermal injury and peripheral responses associated with fatal heatstroke, suggesting its potential value as a biological sample for forensic investigation. Additionally, individual biomarkers are often insufficient to fully reflect the complex processes underlying death, whereas integrating multimodal information may improve diagnostic accuracy. Herein, we conducted a preliminary multimodal analysis to evaluate the forensic potential of skin in a rat model of fatal heatstroke, using functional assessment, HE staining, toluidine blue staining, and immunohistochemical detection of HSP72, Caspase-3, and AQP5. HE staining revealed enlarged secretory lumens and apparent shrinkage of sweat gland secretory cells in HS rats, while toluidine blue staining showed increased dermal mast-cell degranulation. Immunohistochemistry demonstrated increased HSP72, total Caspase-3, and AQP5 immunoreactivity in sweat gland secretory cells, with HSP72 and total Caspase-3 also elevated in the epidermis. PCA suggested clearer group separation when morphological and immunohistochemical variables were considered jointly. Among the individual variables, the mast-cell degranulation ratio showed the best discriminatory performance, with an AUC of 0.9792 (95% CI, 0.9309-1.000). An exploratory random forest classifier integrating seven prespecified variables achieved an internally cross-validated AUC of 1.000 (95% CI, 1.000-1.000) using leave-one-out cross-validation. Overall, this study provides preliminary evidence that skin changes may contribute to forensic assessment of fatal heatstroke. - Source: PubMed
Publication date: 2026/09/18
Liu HuinePan MeichenMa ChuxiongSun ChangaoZhu WeiweiDong Hongmei - Chronic sleep deprivation (SD) is an increasing risk factor for dry eye disease (DED); however, effective nutritional interventions remain limited. In this study, we investigated the protective efficacy of a standardized wild green oat extract (GOE; L.), a polyphenol-enriched supplement with neuromodulatory and antioxidant properties, against SD-induced DED in mice. Mice were subjected to 16 days of SD and orally administered GOE (10 and 40 mg kg, twice daily) from days 5 to 16. SD significantly impaired tear secretion by downregulating lacrimal aquaporin 5 (AQP5) and compromised tear film stability by reducing meibomian PPAR-γ-driven lipogenesis. GOE treatment significantly increased tear secretion, enhanced tear film stability, and preserved tissue integrity. Mechanistically, GOE exerted a dual regulatory effect by modulating cAMP-mediated AQP5 trafficking in lacrimal glands and PPAR-γ/FASN-driven meibocyte differentiation in meibomian glands, restoring ocular surface and tear film homeostasis. These results demonstrate that GOE improves ocular surface health , suggesting its potential as a functional food intervention for SD-related dry eye. - Source: PubMed
Publication date: 2026/09/18
Chang Ya-TingLu LingWang Ping-HsunHsieh Yi-HsienCheng Chun-WenYeh Yong-QingChen Tzu-YuChen Hui-JuHuang Yu-ChunChen Bo-Yie - Salivary gland defects from tumors or trauma are often accompanied by irreversible secretory dysfunction and remain a clinical challenge. Alternative cell sources and suitable scaffolds for salivary gland regeneration remain lacking. A functionalized scaffold system is fabricated by three-dimensional printing combined with freeze-drying to prepare a collagen-silk fibroin-Matrigel scaffold. The scaffold exhibits high porosity and strong water absorption capacity. Its internal surface is coated with a basement membrane extract-rich layer that enhances hydrophilicity and creates a physiologically relevant cell niche. In vitro, a synergistic co-culture system incorporating urine-derived induced pluripotent stem cells (iPSCs), parotid mesenchymal stem cells, and parotid epithelial cells directs the differentiation of iPSCs into KRT18+/VIM+/AQP5+ iPSC-derived cells. These cells readily adhere to the scaffold, proliferate, and form acinar-like aggregates within its porous architecture. In a rat model of parotid gland trauma, implantation of the scaffold progressively promotes tissue regeneration and attenuates trauma-induced atrophy. Histological analysis reveals that the scaffold recruits host cells to organize within its pores, forming amylase-secreting acinar-like structures. This study provides a reliable seed cell source and a suitable scaffold for structural and functional parotid restoration, offering a potential strategy for salivary gland tissue engineering. - Source: PubMed
Publication date: 2026/09/11
Liu HanSun ZiyanJin YizhouLi RuixinShan Zhaochen - An adequate supply of protein and minerals, particularly nitrogen (N) and calcium (Ca), is essential for ruminant growth and metabolic function. The rumen and salivary glands are crucial for nutrient and electrolyte homoeostasis via specialised transport proteins. Dietary reductions in N and Ca may elicit adaptive molecular and physiological responses, but their effects on epithelial transport are still not entirely understood. This study investigated the effects of dietary N and Ca reductions on ruminal and salivary fluid composition and the mRNA expression of Ca-, phosphate (Pi)-, and urea-transporting proteins in the ruminal epithelium and salivary glands of young goats. Goats received diets with reduced N, reduced Ca, or combined N and Ca reduction. Ruminal and abomasal fluids, saliva, and tissue samples were analysed for mineral concentrations, urea, and short-chain fatty acids (SCFAs). mRNA expression of transporters, including CASR, TRPC3, TRPV3, PMCA, NCX1, UTB, SLC4A4, ATP1B1 (Na/K-ATPase β-subunit), AQP5, NaPi IIb, and PiT1 was quantified using qPCR. Dietary N reduction decreased ruminal and salivary urea concentrations, reduced mRNA expression of SLC4A4, AQP5, and NaPi IIb in salivary glands, and lowered ruminal SCFA concentrations, indicating impaired microbial fermentation. The dietary Ca reduction increased salivary Pi and induced upregulation of AQP5, ATP1B1, and PiT1. In the ruminal epithelium, N reduction increased PMCA and UTB expression, whereas Ca reduction had only minor effects on Ca transporters. Ruminal Pi and Ca concentrations remained stable, reflecting strong stabilisation of mineral concentrations in the ruminal environment, whereas abomasal fluid showed greater sensitivity to dietary changes. These results indicate tissue-specific transcriptional and compositional responses of ruminant epithelia to dietary N and Ca reduction. N reduction primarily affects the expression of genes related to nutrient and solute transport, whereas Ca reduction is associated with selective transcriptional changes in mineral-related transporters. These results provide evidence for adaptive epithelial responses to nutritional variation, although functional consequences at the protein or transport level require further investigation. - Source: PubMed
Publication date: 2026/09/08
Egler Christopher-YannikHeidelberg MadlinBurmester MarionHustedt KarinSchnepel NadineMuscher-Banse Alexandra S - Epithelial acinar cells of the salivary gland establish apical-basal polarity and secretory competence during development, processes that require tightly coordinated membrane trafficking. The Rho-family GTPase Cdc42 is a key regulator of epithelial polarity, but it has rarely been linked to the vesicle-fusion machinery in vivo. Using mice with acinar cell-specific deletion of Cdc42, we found that Cdc42 loss caused the accumulation of small vesicles near the apical surface, where the water channel AQP5 was retained in clusters and lumen formation was defective. Cdc42-deficient glands showed a selective reduction of two vesicle-associated SNAREs, VAMP2 and VAMP4, whereas VAMP8, the t-SNAREs, and an endocytic marker were unchanged. The corresponding mRNAs were not decreased, indicating that Cdc42 maintains these v-SNAREs through post-transcriptional mechanisms. Cdc42-deficient acinar cells also accumulated condensing vacuoles, a form of immature secretory granule, indicating impaired granule maturation. We propose that Cdc42 coordinates two distinct membrane-remodeling processes by maintaining these v-SNAREs: VAMP2 supports the fusion of AQP5-containing vesicles with the apical membrane, whereas VAMP4 supports secretory granule maturation. These findings identify the vesicle-fusion machinery as a target of Cdc42-dependent polarity control, with potential implications for secretory gland disorders. - Source: PubMed
Publication date: 2026/09/07
Shitara AkikoNagase HarunaBleck Christopher K EOhno YutaKataoka HideoSatoh KeitaroKashimata Masanori