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Channels and Transporters in Cells and Tissue 4.0
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Channels and Transporters in Cells and Tissue 4.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (20 March 2023) | Viewed by 6031

Special Issue Editor

Dr. Graça Soveral

E-Mail Website
Guest Editor
Faculdade de Farmacia, Universidaded de Lisboa, Research Institute for Medicines (iMed.ULisboa), Lisbon, Portugal
Interests: water and solute transport; membrane; pathophysiology; metabolism; cancer
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Channels and transporters are membrane proteins that mediate the traffic of water, ions, and solutes across biological membranes and are crucial to maintaining homeostasis, and thus assuring cell survival upon intracellular or environmental stress. The absence or dysfunction of channels and transporters may have dramatic consequences for cellular and tissue function and cause disease. Thus, the mechanisms of physiological regulation and chemical modulation of membrane proteins are an emergent topic in the field of biology, agriculture, and medicine that opens opportunities for drug discovery and new therapies.

This new version of Special Issue “Channels and Transporters in Cells and Tissue” will focus on the function and regulation of membrane transport proteins across all living organisms, including their potential as drug targets. Authors are invited to submit original research and review papers addressing the topic of this Special Issue.

Dr. Graça Soveral
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • membrane transport and regulation
  • structure–function relationship
  • water, ions, and solutes transportation
  • membrane permeability
  • osmoregulation
  • chemical modulation
  • therapeutic applications
  • drug discovery
  • disease
  • prokaryotic and eukaryotic cells

Published Papers (3 papers)

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Research

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17 pages, 3821 KiB  
Article
Unraveling the Aquaporin-3 Inhibitory Effect of Rottlerin by Experimental and Computational Approaches
by Inês Paccetti-Alves, Marta S. P. Batista, Catarina Pimpão, Bruno L. Victor and Graça Soveral
Int. J. Mol. Sci. 2023, 24(6), 6004; https://doi.org/10.3390/ijms24066004 - 22 Mar 2023
Cited by 1 | Viewed by 1904
Abstract
The natural polyphenolic compound Rottlerin (RoT) showed anticancer properties in a variety of human cancers through the inhibition of several target molecules implicated in tumorigenesis, revealing its potential as an anticancer agent. Aquaporins (AQPs) are found overexpressed in different types of cancers and [...] Read more.
The natural polyphenolic compound Rottlerin (RoT) showed anticancer properties in a variety of human cancers through the inhibition of several target molecules implicated in tumorigenesis, revealing its potential as an anticancer agent. Aquaporins (AQPs) are found overexpressed in different types of cancers and have recently emerged as promising pharmacological targets. Increasing evidence suggests that the water/glycerol channel aquaporin-3 (AQP3) plays a key role in cancer and metastasis. Here, we report the ability of RoT to inhibit human AQP3 activity with an IC50 in the micromolar range (22.8 ± 5.82 µM for water and 6.7 ± 2.97 µM for glycerol permeability inhibition). Moreover, we have used molecular docking and molecular dynamics simulations to understand the structural determinants of RoT that explain its ability to inhibit AQP3. Our results show that RoT blocks AQP3-glycerol permeation by establishing strong and stable interactions at the extracellular region of AQP3 pores interacting with residues essential for glycerol permeation. Altogether, our multidisciplinary approach unveiled RoT as an anticancer drug against tumors where AQP3 is highly expressed providing new information to aquaporin research that may boost future drug design. Full article
(This article belongs to the Special Issue Channels and Transporters in Cells and Tissue 4.0)
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21 pages, 2992 KiB  
Article
Interaction of Amphipathic Peptide from Influenza Virus M1 Protein with Mitochondrial Cytochrome Oxidase
by Ilya P. Oleynikov, Roman V. Sudakov, Victor A. Radyukhin, Alexander M. Arutyunyan, Natalia V. Azarkina and Tatiana V. Vygodina
Int. J. Mol. Sci. 2023, 24(4), 4119; https://doi.org/10.3390/ijms24044119 - 18 Feb 2023
Cited by 2 | Viewed by 1479
Abstract
The Bile Acid Binding Site (BABS) of cytochrome oxidase (CcO) binds numerous amphipathic ligands. To determine which of the BABS-lining residues are critical for interaction, we used the peptide P4 and its derivatives A1-A4. P4 is composed of two flexibly bound modified α-helices [...] Read more.
The Bile Acid Binding Site (BABS) of cytochrome oxidase (CcO) binds numerous amphipathic ligands. To determine which of the BABS-lining residues are critical for interaction, we used the peptide P4 and its derivatives A1-A4. P4 is composed of two flexibly bound modified α-helices from the M1 protein of the influenza virus, each containing a cholesterol-recognizing CRAC motif. The effect of the peptides on the activity of CcO was studied in solution and in membranes. The secondary structure of the peptides was examined by molecular dynamics, circular dichroism spectroscopy, and testing the ability to form membrane pores. P4 was found to suppress the oxidase but not the peroxidase activity of solubilized CcO. The Ki(app) is linearly dependent on the dodecyl-maltoside (DM) concentration, indicating that DM and P4 compete in a 1:1 ratio. The true Ki is 3 μM. The deoxycholate-induced increase in Ki(app) points to a competition between P4 and deoxycholate. A1 and A4 inhibit solubilized CcO with Ki(app)~20 μM at 1 mM DM. A2 and A3 hardly inhibit CcO either in solution or in membranes. The mitochondrial membrane-bound CcO retains sensitivity to P4 and A4 but acquires resistance to A1. We associate the inhibitory effect of P4 with its binding to BABS and dysfunction of the proton channel K. Trp residue is critical for inhibition. The resistance of the membrane-bound enzyme to inhibition may be due to the disordered secondary structure of the inhibitory peptide. Full article
(This article belongs to the Special Issue Channels and Transporters in Cells and Tissue 4.0)
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Review

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11 pages, 1315 KiB  
Review
Role of SNAREs and Rabs in Myelin Regulation
by Azzurra Margiotta
Int. J. Mol. Sci. 2023, 24(11), 9772; https://doi.org/10.3390/ijms24119772 - 5 Jun 2023
Viewed by 2200
Abstract
The myelin sheath is an insulating layer around the nerves of the brain and spinal cord which allows a fast and efficient nerve conduction. Myelin is made of protein and fatty substances and gives protection for the propagation of the electrical impulse. The [...] Read more.
The myelin sheath is an insulating layer around the nerves of the brain and spinal cord which allows a fast and efficient nerve conduction. Myelin is made of protein and fatty substances and gives protection for the propagation of the electrical impulse. The myelin sheath is formed by oligodendrocytes in the central nervous system (CNS) and by Schwann cells in the peripheral nervous system (PNS). The myelin sheath presents a highly organized structure and expands both radially and longitudinally, but in a different way and with a different composition. Myelin alterations determine the onset of several neuropathies, as the electrical signal can be slowed or stopped. Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) and ras (rat sarcoma)-associated binding proteins (rabs) have been proved to contribute to several aspects regarding the formation of myelin or dysmyelination. Here, I will describe the role of these proteins in regulating membrane trafficking and nerve conduction, myelin biogenesis and maintenance. Full article
(This article belongs to the Special Issue Channels and Transporters in Cells and Tissue 4.0)
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