Results 31 to 40 of about 1,989 (206)

Endo-Porter–mediated delivery of phosphorodiamidate morpholino oligos (PMOs) in erythrocyte suspension cultures from Cope's gray treefrog Hyla chrysoscelis

BioTechniques, 2011
Cope's gray treefrog, Hyla chrysoscelis, is a freeze-tolerant anuran that accumulates cryoprotective glycerol during cold acclimation. H. chrysoscelis erythrocytes express the aquaglyceroporin HC-3, which facilitates transmembrane glycerol and water ...
Venkateshwar Mutyam, Matthew V. Puccetti, James Frisbie, David L. Goldstein, Carissa M. Krane   +4 more
doaj   +1 more source

Aquaglyceroporin Modulators as Emergent Pharmacological Molecules for Human Diseases

Frontiers in Molecular Biosciences, 2022
Aquaglyceroporins, a sub-class of aquaporins that facilitate the diffusion of water, glycerol and other small uncharged solutes across cell membranes, have been recognized for their important role in human physiology and their involvement in multiple ...
Catarina Pimpão, Catarina Pimpão, Darren Wragg, Inês V. da Silva, Inês V. da Silva, Angela Casini, Graça Soveral, Graça Soveral   +7 more
doaj   +1 more source

Involvement of aquaglyceroporins in energy metabolism in health and disease [PDF]

Biochimie, 2021
Aquaglyceroporins are a group of the aquaporin (AQP) family of transmembrane water channels. While AQPs facilitate the passage of water, small solutes, and gases across biological membranes, aquaglyceroporins allow passage of water, glycerol, urea and some other solutes.
Giuseppe Calamita, Christine Delporte
openaire   +4 more sources

Trypanosoma brucei aquaglyceroporin 2 is a high-affinity transporter for pentamidine and melaminophenyl arsenic drugs and the main genetic determinant of resistance to these drugs [PDF]

, 2013
Objectives: Trypanosoma brucei drug transporters include the TbAT1/P2 aminopurine transporter and the high-affinity pentamidine transporter (HAPT1), but the genetic identity of HAPT1 is unknown. We recently reported that loss of T.
Lee, Rebecca S, Burchmore, Richard J S, Natto, Manal J, Eze, Anthonius, Graf, Fabrice, Burchmore, Richard JS, Lee, Rebecca, de Koning, Harry, Glover, Lucy, Mäser, Pascal, Teka, Ibrahim, Barrett, Michael P., Munday, Jane C., Teka, Ibrahim A., De Koning, Harry P., Eze, Anthonius A, Graf, Fabrice E., De Koning, Harry P, Ludin, Philipp, McDonald, Jennifer, MacLeod, Annette, Turner, C Michael R., Munday, Jane C, Natto, Manal J., Lee, Rebecca S., Tait, Andy, Horn, David, Baker, Nicola, Munday, Jane, Turner, C Michael R, Aguinaga Andres, David, Barrett, Michael P, Andrés, David Aguinaga, Burchmore, Richard, Clucas, Caroline, Graf, Fabrice E, Horn, David; id_orcid, Burchmore, Richard J. S., Teka, Ibrahim A, Eze, Anthonius A., Natto, Manal, Turner, C. Michael R., Barrett, Michael   +42 more
core   +1 more source

Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes

Physiological Reports, 2023
Marine teleosts ingest large amounts of seawater containing various ions, including 0.4 mM boric acid, which can accumulate at toxic levels in the body. However, the molecular mechanisms by which marine teleosts absorb and excrete boric acid are not well
Shiori Kumagai, Erika Watanabe, Naoko Hayashi, Yuuri Kimura, Takehiro Kamiya, Ayumi Nagashima, Kazutaka Ushio, Genki Imaizumi, Juhyun Kim, Keijiro Munakata, Takahiro Umezawa, Shigehisa Hirose, Koji Kasai, Toru Fujiwara, Michael F. Romero, Akira Kato   +15 more
doaj   +1 more source

Aquaglyceroporins: Drug Targets for Metabolic Diseases? [PDF]

Frontiers in Physiology, 2018
Aquaporins (AQPs) are a family of transmembrane channel proteins facilitating the transport of water, small solutes, and gasses across biological membranes. AQPs are expressed in all tissues and ensure multiple roles under normal and pathophysiological conditions.
Calamita G, Perret J, Delporte C
openaire   +5 more sources

Methylarsonous Acid Transport by Aquaglyceroporins

Environmental Health Perspectives, 2006
Many mammals methylate trivalent inorganic arsenic in liver to species that are released into the bloodstream and excreted in urine and feces. This study addresses how methylated arsenicals pass through cell membranes. We have previously shown that aquaglyceroporin channels, including Escherichia coli GlpF, Saccharomyces cerevisiae Fps1p, AQP7, and ...
Liu, Zijuan, Styblo, Miroslav, Rosen, Barry P.   +2 more
openaire   +2 more sources

Aquaglyceroporin permeability values for hepatic (AQP9) and adipose (AQP7) glycerol transport. [PDF]

, 2014
Aquaglyceroporin permeability values for hepatic (AQP9) and adipose (AQP7) glycerol transport.
Carmelo De Maria (674948), Francesca Montemurro (674949), Giovanni Vozzi (674950), Chiara Andreoni (674946), Gianni Orsi (674947)   +4 more
core   +1 more source

Molecular Basis of Aquaporin-7 Permeability Regulation by pH

Cells, 2018
The aquaglyceroporin AQP7, a family member of aquaporin membrane channels, facilitates the permeation of water and glycerol through cell membranes and is crucial for body lipid and energy homeostasis.
Andreia F. Mósca, Andreia de Almeida, Darren Wragg, Ana P. Martins, Farzana Sabir, Stefano Leoni, Teresa F. Moura, Catarina Prista, Angela Casini, Graça Soveral   +9 more
doaj   +1 more source

Mammalian aquaglyceroporin function in metabolism

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2016
Aquaglyceroporins are integral membrane proteins that are permeable to glycerol as well as water. The movement of glycerol from a tissue/organ to the plasma and vice versa requires the presence of different aquaglyceroporins that can regulate the entrance or the exit of glycerol across the plasma membrane.
Laforenza U., Bottino C., Gastaldi G.
openaire   +3 more sources