Methods for studying mammalian aquaporin biology DOI Creative Commons
Shohini Banerjee, Ian M. Smith,

Autumn Hengen

et al.

Biology Methods and Protocols, Journal Year: 2023, Volume and Issue: 8(1)

Published: Jan. 1, 2023

Aquaporins (AQPs), transmembrane water-conducting channels, have earned a great deal of scrutiny for their critical physiological roles in healthy and disease cell states, especially the biomedical field. Numerous methods been implemented to elucidate involvement AQP-mediated water transport downstream signaling activation eliciting whole cell, tissue, organ functional responses. To modulate these responses, other employed investigate AQP druggability. This review discusses standard

Language: Английский

Aquaporins in Glandular Secretion DOI
Giuseppe Calamita, Christine Delporte

Advances in experimental medicine and biology, Journal Year: 2023, Volume and Issue: unknown, P. 225 - 249

Published: Jan. 1, 2023

Language: Английский

Citations

3

Molecular dynamics simulation of the effect of AQP1 on the transmembrane transport of plasma RONS across cancer cell membranes DOI Open Access
Yanxiu Cui, Tong Zhao, Zichen Wang

et al.

Physics of Plasmas, Journal Year: 2023, Volume and Issue: 30(6)

Published: June 1, 2023

In the cold atmospheric plasma (CAP)-assisted cancer treatment, increase in concentration of reactive oxygen species (ROS) and nitrogen (RNS) produced by CAP is believed to be related overexpression aquaporins (AQPs) on cell membranes. this paper, using classical molecular dynamics simulations, transmembrane behavior RNS ROS a pure phospholipid bilayer or AQP1-phospholipid model was studied. The research shows that hydrophobic tend transported through phospholipids. AQP1 can significantly improve efficiency hydrophilic ROS. Our simulation fills gap for RNS-related provides guidance precise targeting cells therapy.

Language: Английский

Citations

3

Aquaporin-0-protein interactions elucidated by crosslinking mass spectrometry DOI Creative Commons

Carla Vt O'Neale,

Minh H. Tran, Kevin L. Schey

et al.

Biochemical and Biophysical Research Communications, Journal Year: 2024, Volume and Issue: 727, P. 150320 - 150320

Published: June 27, 2024

Aquaporin-0 (AQP0) constitutes 50 % of the lens membrane proteome and plays important roles in fiber cell adhesion, water permeability, transparency. Previous work has shown that specific proteins, such as calmodulin (CaM), interact with AQP0 to modulate its permeability; however, these studies often used peptides, rather than full-length protein, probe interactions. Furthermore, regions interaction several known interacting partners, i.e. αA αB-crystallins, phakinin (CP49) remain unknown. The purpose this study was use crosslinking mass spectrometry (XL-MS) identify proteins crude cortical fractions determine protein interaction. Our results demonstrate, for first time, N-terminus can engage Specific are elucidated partners including phakinin, α-crystallin, connexin-46, connexin-50. In addition, two new vimentin were identified.

Language: Английский

Citations

0

Methods for studying mammalian aquaporin biology DOI Creative Commons
Shohini Banerjee, Ian M. Smith,

Autumn Hengen

et al.

Biology Methods and Protocols, Journal Year: 2023, Volume and Issue: 8(1)

Published: Jan. 1, 2023

Aquaporins (AQPs), transmembrane water-conducting channels, have earned a great deal of scrutiny for their critical physiological roles in healthy and disease cell states, especially the biomedical field. Numerous methods been implemented to elucidate involvement AQP-mediated water transport downstream signaling activation eliciting whole cell, tissue, organ functional responses. To modulate these responses, other employed investigate AQP druggability. This review discusses standard

Language: Английский

Citations

0