Downregulation of Aquaporins (AQP1 and AQP5) and Na,K-ATPase in Porcine Reproductive and Respiratory Syndrome Virus-Infected Pig Lungs

Zhang, Jianping; Yan, Meiping; Gu, Wei; Chen, Ao; Liu, Jie; Li, Lexing; Zhang, Songlin; Liu, Guoquan

doi:10.1007/s10753-018-0762-2

Cited by 22 publications

(21 citation statements)

References 36 publications

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“…AQP5 is known to be mostly correlated with abnormal gland secretion in airway. Recent studies have supported the notion that the protein levels of AQP1 and AQP5 are decreased in inflammatory states [38,39]. Consistent with these, we observed that the protein levels of AQP1 and AQP5 were lower in the lung tissues of allergic mice than in normal control.…”

Section: Discussionsupporting

confidence: 91%

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Sevoflurane modulates AQPs (1,5) expression and endoplasmic reticulum stress in mice lung with allergic airway inflammation

et al. 2019

Bioscience Reports

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Sevoflurane was found to show protective roles in mice with asthma, however, the mechanism of which needs further exploring. Aquaporins (AQPs) have been demonstrated to be involved in the pathogenesis of asthma, while endoplasmic reticulum stress has been reported to be related to many inflammatory diseases and involved in protein processing, including AQPs. The present study aimed to determine the role of sevoflurane in AQPs (AQP1,3,4,5) expression in mice with allergic airway inflammation and the probable mechanism. The increased number of inflammatory cells infiltrating the lung tissue, and the elevated levels of tumor necrosis factor-α (TNF-α) and interleukin (IL) 13 (IL-13) were all decreased after sevoflurane treatment (all P<0.05). Meanwhile, mRNA levels of AQP1 and AQP5 but not AQP3 and AQP4 were decreased in ovalbumin (OVA)-induced allergic mice lung. Both the decreased mRNA expression and protein levels of AQP1 and AQP5 in allergic lung tissues were reversed by sevoflurane treatment. Furthermore, we established that sevoflurane inhibited the OVA-induced protein increase in the endoplasmic reticulum (ER) stress markers BiP and C/EBP homologous protein (CHOP). Collectively, these findings suggested that sevoflurane modulated the expression and protein level of AOPs (AQP1, AQP5) as well as inhibited ER stress response in OVA-induced allergic airway inflammation of mice.

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Section: Discussionsupporting

confidence: 91%

“…AQP5, together with AQP1, is the primary route for osmotic water transport between the capillary and the airspace [38,39], and is fundamental to lung water transport and normal lung function [44]. AQP1 is critically related to lung edema and involved in many inflammatory diseases [45–47].…”

Section: Discussionmentioning

confidence: 99%

Sevoflurane modulates AQPs (1,5) expression and endoplasmic reticulum stress in mice lung with allergic airway inflammation

et al. 2019

Bioscience Reports

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“…To the best of our knowledge, AQP-mediated fluid movement is regulated by an osmotic gradient 21 . To provide a basis for understanding the role of AQP5 in transepithelial ion transport, we examined whether these solute transporters modulate volume regulation of AQP5 in the salivary glands.…”

Section: Resultsmentioning

confidence: 99%

Carbonic anhydrase 12 mutation modulates membrane stability and volume regulation of aquaporin 5

Hwang

Kang

Kim

et al. 2018

Journal of Enzyme Inhibition and Medicinal Chemistry

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Patients carrying the carbonic anhydrase12 E143K mutation showed the dry mouth phenotype. The mechanism underlying the modulation of aquaporin 5 and function in the salivary glands by carbonic anhydrase12 remains unknown. In this study, we identified the mislocalised aquaporin 5 in the salivary glands carrying the E143K. The intracellular pH of E143K cells was more acidic than that of the cells carrying wild type. To evaluate the role of carbonic anhydrase12 on the volume regulation of aquaporin 5, the submandibular gland cells were subjected to hypotonic stimuli. E143K enhanced the extent of swelling of cells on hypotonicity. Aquaporin 5 modulates water influx through ion transporters to prevent osmotic imbalance. These results suggest that the carbonic anhydrase12 E143K, including acidification or inflammation, mediates volume dysregulation by the loss of aquaporin 5. Thus, carbonic anhydrase12 may determine sensible effects on the cellular osmotic regulation by modulating aquaporin 5.

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“…Water absorption through AQPs is driven by an osmotic gradient that is generated by transcellular Na + transport. Apical Na + entry in surface-absorptive cells of the colonic epithelium is mediated by the ENaC, and basolateral Na + exit is mediated through the Na + -K + -ATPase, sodium transporters that were identified in the mammalian colon and lung at the mRNA and protein levels 31,52 . We found the ENaC and Na + -K + -ATPase distribution in the colonic epithelium, small intestinal villus epithelium, gastric pit and fundic gland, implying the roles of these transporters in Na + absorption in the colon and small intestinal villus epithelium 31 .…”

Section: Discussionmentioning

confidence: 99%

Distribution of aquaporins and sodium transporters in the gastrointestinal tract of a desert hare, Lepus yarkandensis

Zhang

Deng

et al. 2019

Sci Rep

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Lepus yarkandensis is a desert hare of the Tarim Basin in western China, and it has strong adaptability to arid environments. Aquaporins (AQPs) are a family of water channel proteins that facilitate transmembrane water transport. Gastrointestinal tract AQPs are involved in fluid absorption in the small intestine and colon. This study aimed to determine the distribution of AQPs and sodium transporters in the gastrointestinal tract of L. yarkandensis and to compare the expression of these proteins with that in Oryctolagus cuniculus. Immunohistochemistry was performed to analyse the cellular distribution of these proteins, and the acquired images were analysed with IpWin32 software. Our results revealed that AQP1 was located in the colonic epithelium, central lacteal cells, fundic gland parietal cells, and capillary endothelial cells; AQP3 was located in the colonic epithelium, small intestinal villus epithelium, gastric pit and fundic gland; AQP4 was located in the fundic gland, small intestinal gland and colonic epithelium; and epithelial sodium channel (ENaC) and Na+-K+-ATPase were located in the epithelial cells, respectively. The higher expression levels of AQP1, AQP3, ENaC and Na+-K+-ATPase in the colon of L. yarkandensis compared to those in O. cuniculus suggested that L. yarkandensis has a higher capacity for faecal dehydration.

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Downregulation of Aquaporins (AQP1 and AQP5) and Na,K-ATPase in Porcine Reproductive and Respiratory Syndrome Virus-Infected Pig Lungs

Cited by 22 publications

References 36 publications

Sevoflurane modulates AQPs (1,5) expression and endoplasmic reticulum stress in mice lung with allergic airway inflammation

Sevoflurane modulates AQPs (1,5) expression and endoplasmic reticulum stress in mice lung with allergic airway inflammation

Carbonic anhydrase 12 mutation modulates membrane stability and volume regulation of aquaporin 5

Distribution of aquaporins and sodium transporters in the gastrointestinal tract of a desert hare, Lepus yarkandensis

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