Human aquaporin-11 guarantees efficient transport of H2O2 across the endoplasmic reticulum membrane

Bestetti, Stefano; Galli, M; Sorrentino, Ilaria; Pinton, Paolo; Rimessi, Alessandro; Sitia, Roberto; Medraño-Fernández, Iria

doi:10.1016/j.redox.2019.101326

Cited by 98 publications

(95 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Aquaporin (AQP) channels, first established to mediate the diffusion of water across membranes [ 10 , 11 ], have been shown to facilitate transmembrane H 2 O 2 movement [ 12 ]. The mammalian AQP11 has been localized to the ER and established to serve as a “peroxiporin”, facilitating the movement of H 2 O 2 across the ER membrane [ 13 , 14 ]. A role for mammalian AQP8 in the movement of H 2 O 2 at the ER has been shown as well [ 15 ]; however, localization data suggest that the ER activity of AQP8 reflects a subset of the AQP8 found in the ER in transit to the plasma membrane [ 13 ].…”

Section: Properties Of H 2 Omentioning

confidence: 99%

“…The mammalian AQP11 has been localized to the ER and established to serve as a “peroxiporin”, facilitating the movement of H 2 O 2 across the ER membrane [ 13 , 14 ]. A role for mammalian AQP8 in the movement of H 2 O 2 at the ER has been shown as well [ 15 ]; however, localization data suggest that the ER activity of AQP8 reflects a subset of the AQP8 found in the ER in transit to the plasma membrane [ 13 ]. Many aquaporins are regulated at the post-translational level in response to cellular or environmental changes [ 16 , 17 ].…”

Section: Properties Of H 2 Omentioning

confidence: 99%

See 1 more Smart Citation

Pathways for Sensing and Responding to Hydrogen Peroxide at the Endoplasmic Reticulum

Roscoe

Sevier

2020

Cells

View full text Add to dashboard Cite

The endoplasmic reticulum (ER) has emerged as a source of hydrogen peroxide (H2O2) and a hub for peroxide-based signaling events. Here we outline cellular sources of ER-localized peroxide, including sources within and near the ER. Focusing on three ER-localized proteins—the molecular chaperone BiP, the transmembrane stress-sensor IRE1, and the calcium pump SERCA2—we discuss how post-translational modification of protein cysteines by H2O2 can alter ER activities. We review how changed activities for these three proteins upon oxidation can modulate signaling events, and also how cysteine oxidation can serve to limit the cellular damage that is most often associated with elevated peroxide levels.

show abstract

Section: Properties Of H 2 Omentioning

confidence: 99%

Section: Properties Of H 2 Omentioning

confidence: 99%

Pathways for Sensing and Responding to Hydrogen Peroxide at the Endoplasmic Reticulum

Roscoe

Sevier

2020

Cells

View full text Add to dashboard Cite

show abstract

“…Due to the transported molecules, the family of these 13 proteins can be divided into two subgroups, those that transport only water and those that additionally have the ability to carry glycerol [94]. Regardless of belonging to one of the two described subgroups, aquaporins can participate in H 2 O 2 transport, which, as it turns out, is of considerable importance in the neoplastic process ( Figure 6) [95,96]. Research conducted on various types of cancer cells, including colon [97], ovarian, [98] brain, [99] lung [100], and pancreatic cancers [101], have shown a correlation between increased aquaporin expression and the level of tumor growth [102].…”

Section: Aqps: Aquaporinsmentioning

confidence: 99%

Important players in carcinogenesis as potential targets in cancer therapy: an update

2020

View full text Add to dashboard Cite

The development of cancer is a problem that has accompanied mankind for years. The growing number of cases, emerging drug resistance, and the need to reduce the serious side effects of pharmacotherapy are forcing scientists to better understand the complex mechanisms responsible for the initiation, promotion, and progression of the disease. This paper discusses the modulation of the particular stages of carcinogenesis by selected physiological factors, including: acetylcholine (ACh), peroxisome proliferator-activated receptors (PPAR), fatty acid-binding proteins (FABPs), Bruton's tyrosine kinase (Btk), aquaporins (AQPs), insulin-like growth factor-2 (IGF-2), and exosomes. Understanding their role may contribute to the development of more effective and safer therapies based on new binding sites.

show abstract

“…Some of them, have been recognized to allow the transmembrane diffusion of H2O2 [1,3,7] and for this reason named peroxiporins. To date five AQPs showed H2O2 permeability: AQP3 [8][9][10][11], AQP5 [12], AQP8 [4,13], AQP9 [14] and AQP11 [15].…”

Section: Introductionmentioning

confidence: 99%

“…As a consequence, this boosts nicotinamide adenine dinucleotide cofactor (NADH) levels through the tricarboxylic acid cycle, essential for ATP production by oxidative phosphorylation. Interestingly, it has been demonstrated that also AQP8 and AQP11 are localized in mitochondria [29,30] and ER [15], respectively and possess H2O2 permeability.…”

Section: Introductionmentioning

confidence: 99%

Dual Aquaporin and Sigma1 Receptor (DAS) Modulators: New Tools for Counteracting Oxidative Stress

Pellavio¹,

Rossino²,

Gastaldi³

et al. 2020

Preprint

View full text Add to dashboard Cite

Specific aquaporins (AQP), called peroxyporins, play a relevant role in controlling H2O2 permeability and ensure reactive oxygen species wasting during oxidative stress. Another target involved in oxidative stress is the Sigma1 Receptor (S1R), since its activation is triggered by oxidative or endoplasmic reticulum stress. Herein we evaluated the effect of S1R modulators on AQP-dependent water permeability in the presence and in the absence of oxidative stress. Applying stopped-flow light scattering and fluorescent probe methods, water and hydrogen peroxide permeability in Hela cells have been studied. Results evidenced that S1R agonists can restore water permeability in heat-stressed cells and the co-administration with a S1R antagonist totally counteracted the ability to restore the water permeability. All compounds except one were able to counteract the oxidative stress of HeLa cells specifically knocked down for S1R. Taken together, our results support the hypothesis that the investigated compounds act as dual aquaporin and Sigma1 receptor (DAS) modulators. The finding that small molecules can modulate both AQP and S1R opens a new direction toward the identification of innovative drugs able to regulate cell survival during oxidative stress in pathologic conditions, like cancer and degenerative diseases.

show abstract

Human aquaporin-11 guarantees efficient transport of H2O2 across the endoplasmic reticulum membrane

Cited by 98 publications

References 38 publications

Pathways for Sensing and Responding to Hydrogen Peroxide at the Endoplasmic Reticulum

Pathways for Sensing and Responding to Hydrogen Peroxide at the Endoplasmic Reticulum

Important players in carcinogenesis as potential targets in cancer therapy: an update

Dual Aquaporin and Sigma1 Receptor (DAS) Modulators: New Tools for Counteracting Oxidative Stress

Contact Info

Product

Resources

About