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Research in Membrane Transporters—Unveiling the Molecular Mechanisms and Practical Application
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Research in Membrane Transporters—Unveiling the Molecular Mechanisms and Practical Application

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

Deadline for manuscript submissions: 20 March 2025 | Viewed by 3646

Special Issue Editors

Dr. Ewa Maciaszczyk-Dziubinska

E-Mail Website1 Website2
Guest Editor
Department of Genetics and Cell Physiology, Faculty of Biological Sciences, University of Wrocław, 50-328 Wroclaw, Poland
Interests: arsenic; antimony; molecular basis of metalloid toxicity and detoxification; yeast genetics and biology; membrane transporters; stress response; transport proteins; proteostasis
Dr. Donata Wawrzycka

E-Mail Website1 Website2
Guest Editor
Department of Genetics and Cell Physiology, Faculty of Biological Sciences, University of Wrocław, 50-328 Wroclaw, Poland
Interests: arsenic; antimony; molecular basis of metalloid toxicity and detoxification; yeast genetics and biology; membrane transporters; stress response; transport proteins; proteostasis

Special Issue Information

Dear Colleagues,

The International Journal of Molecular Sciences (IJMS) is pleased to present a Special Issue dedicated to furthering our understanding of membrane transporters and their complex roles in biological systems. The purpose of this Special Issue is to provide a comprehensive forum for researchers and academics to discuss their most recent discoveries, methodology, and opinions in membrane transporters research.

Membrane transporters play crucial roles in cellular processes, including the uptake, efflux, and distribution of various molecules. Understanding their molecular mechanisms is essential to unravel the complexities of physiological and pathological processes, drug delivery, and therapeutic interventions.

This Special Issue welcomes contributions that bridge the gap between clinical observations and biomolecular experiments. Although pure clinical studies may not align with the journal's focus, submissions integrating clinical aspects with biomolecular experimentation will be highly valued. Researchers are encouraged to explore the diverse aspects of membrane transporter research, including structure–function relationships, regulation, modulation, transport kinetics, and implications for human health and disease.

Dr. Ewa Maciaszczyk-Dziubinska
Dr. Donata Wawrzycka
Guest Editors

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 transporters
  • transporter function
  • transporter regulation
  • transporter-mediated drug transport
  • transport-related diseases
  • biomolecular studies
  • pharmacokinetics
  • membrane proteostasis

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Published Papers (4 papers)

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Research

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12 pages, 3139 KiB  
Article
Intestinal Epithelial Cell Brush Border Membrane Cl:HCO3 Exchanger Regulation by Mast Cells in Chronic Ileitis
by Raja Singh Paulraj, Sheuli Afroz, Balasubramanian Palaniappan, Usha Murughiyan, Soudamani Singh, Subha Arthur and Uma Sundaram
Int. J. Mol. Sci. 2024, 25(20), 11208; https://doi.org/10.3390/ijms252011208 - 18 Oct 2024
Abstract
Malabsorption of NaCl is the primary cause of diarrhea in inflammatory bowel disease (IBD). Coupled NaCl absorption occurs via the dual operation of Na:H and Cl:HCO3 exchange in the brush border membrane (BBM) of villus cells. Cl:HCO3 exchange is mediated by [...] Read more.
Malabsorption of NaCl is the primary cause of diarrhea in inflammatory bowel disease (IBD). Coupled NaCl absorption occurs via the dual operation of Na:H and Cl:HCO3 exchange in the brush border membrane (BBM) of villus cells. Cl:HCO3 exchange is mediated by BBM transporters DRA (downregulated in adenoma) and PAT1 (putative anion transporter 1) in the mammalian small intestine. DRA/PAT1-mediated Cl:HCO3 exchange was significantly downregulated in the BBM of villus cells in a rabbit model of chronic ileitis, while Na:H exchange was unaffected. The inhibition of Cl:HCO3 exchange was restored in the rabbits when treated with a broad-spectrum immunomodulator, i.e. a glucocorticoid, indicating that the downregulation of DRA/PAT1 is likely to be immune-mediated during chronic enteritis. Mucosal mast cells are one type of key immune cells that are known to proliferate and release immune inflammatory mediators, thus playing a significant role in the pathogenesis of IBD. However, how mast cells may regulate DRA- and PAT1-mediated Cl:HCO3 exchange in a rabbit model of chronic ileitis is unknown. In this study, treatment of rabbits with chronic intestinal inflammation with the mast cell stabilizer ketotifen did not affect the mucosal architecture of the inflamed intestine. However, ketotifen treatment reversed the inhibition of Cl:HCO3 activity in the BBM of villus cells. This restoration of Cl:HCO3 activity to normal levels by ketotifen was found to be secondary to restoring the affinity of the exchangers for its substrate chloride. This observation was consistent with molecular studies, where the mRNA and BBM protein expressions of DRA and PAT1 remained unaffected in the villus cells under all experimental conditions. Thus, this study indicates that mast cells mediated the inhibition of coupled NaCl absorption by inhibiting Cl:HCO3 exchange in a rabbit model of chronic enteritis. Full article
(This article belongs to the Special Issue Research in Membrane Transporters—Unveiling the Molecular Mechanisms and Practical Application)
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13 pages, 2481 KiB  
Article
Molecular Modification Enhances Xylose Uptake by the Sugar Transporter KM_SUT5 of Kluyveromyces marxianus
by Xiuyuan Luo, Xi Tao, Guangyao Ran, Yuanzhen Deng, Huanyuan Wang, Liyan Tan and Zongwen Pang
Int. J. Mol. Sci. 2024, 25(15), 8322; https://doi.org/10.3390/ijms25158322 - 30 Jul 2024
Cited by 1 | Viewed by 589
Abstract
This research cloned and expressed the sugar transporter gene KM_SUT5 from Kluyveromyces marxianus GX-UN120, which displayed remarkable sugar transportation capabilities, including pentose sugars. To investigate the impact of point mutations on xylose transport capacity, we selected four sites, predicted the suitable amino acid [...] Read more.
This research cloned and expressed the sugar transporter gene KM_SUT5 from Kluyveromyces marxianus GX-UN120, which displayed remarkable sugar transportation capabilities, including pentose sugars. To investigate the impact of point mutations on xylose transport capacity, we selected four sites, predicted the suitable amino acid sites by molecular docking, and altered their codons to construct the corresponding mutants, Q74D, Y195K, S460H, and Q464F, respectively. Furthermore, we conducted site-directed truncation on six sites of KM_SUT5p. The molecular modification resulted in significant changes in mutant growth and the D-xylose transport rate. Specifically, the S460H mutant exhibited a higher growth rate and demonstrated excellent performance across 20 g L−1 xylose, achieving the highest xylose accumulation under xylose conditions (49.94 μmol h−1 gDCW-1, DCW mean dry cell weight). Notably, mutant delA554-, in which the transporter protein SUT5 is truncated at position delA554-, significantly increased growth rates in both D-xylose and D-glucose substrates. These findings offer valuable insights into potential modifications of other sugar transporters and contribute to a deeper understanding of the C-terminal function of sugar transporters. Full article
(This article belongs to the Special Issue Research in Membrane Transporters—Unveiling the Molecular Mechanisms and Practical Application)
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25 pages, 6849 KiB  
Article
Structure-Based Analysis of Cefaclor Pharmacokinetic Diversity According to Human Peptide Transporter-1 Genetic Polymorphism
by Ji-Hun Jang and Seung-Hyun Jeong
Int. J. Mol. Sci. 2024, 25(13), 6880; https://doi.org/10.3390/ijms25136880 - 22 Jun 2024
Viewed by 848
Abstract
Cefaclor is a substrate of human-peptide-transporter-1 (PEPT1), and the impact of inter-individual pharmacokinetic variation due to genetic polymorphisms of solute-carrier-family-15-member-1 (SLC15A1) has been a topic of great debate. The main objective of this study was to analyze and interpret cefaclor pharmacokinetic [...] Read more.
Cefaclor is a substrate of human-peptide-transporter-1 (PEPT1), and the impact of inter-individual pharmacokinetic variation due to genetic polymorphisms of solute-carrier-family-15-member-1 (SLC15A1) has been a topic of great debate. The main objective of this study was to analyze and interpret cefaclor pharmacokinetic variations according to genetic polymorphisms in SLC15A1 exons 5 and 16. The previous cefaclor bioequivalence results were integrated with additional SLC15A1 exons 5 and 16 genotyping results. An analysis of the structure-based functional impact of SLC15A1 exons 5 and 16 genetic polymorphisms was recently performed using a PEPT1 molecular modeling approach. In cefaclor pharmacokinetic analysis results according to SLC15A1 exons 5 and 16 genetic polymorphisms, no significant differences were identified between genotype groups. Furthermore, in the population pharmacokinetic modeling, genetic polymorphisms in SLC15A1 exons 5 and 16 were not established as effective covariates. PEPT1 molecular modeling results also confirmed that SLC15A1 exons 5 and 16 genetic polymorphisms did not have a significant effect on substrate interaction with cefaclor and did not have a major effect in terms of structural stability. This was determined by comprehensively considering the insignificant change in energy values related to cefaclor docking due to point mutations in SLC15A1 exons 5 and 16, the structural change in conformations confirmed to be less than 0.05 Å, and the relative stabilization of molecular dynamic simulation energy values. As a result, molecular structure-based analysis recently suggested that SLC15A1 exons 5 and 16 genetic polymorphisms of PEPT1 were limited to being the main focus in interpreting the pharmacokinetic diversity of cefaclor. Full article
(This article belongs to the Special Issue Research in Membrane Transporters—Unveiling the Molecular Mechanisms and Practical Application)
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Review

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30 pages, 1600 KiB  
Review
Multilevel Regulation of Membrane Proteins in Response to Metal and Metalloid Stress: A Lesson from Yeast
by Kacper Zbieralski, Jacek Staszewski, Julia Konczak, Natalia Lazarewicz, Malgorzata Nowicka-Kazmierczak, Donata Wawrzycka and Ewa Maciaszczyk-Dziubinska
Int. J. Mol. Sci. 2024, 25(8), 4450; https://doi.org/10.3390/ijms25084450 - 18 Apr 2024
Cited by 2 | Viewed by 1367
Abstract
In the face of flourishing industrialization and global trade, heavy metal and metalloid contamination of the environment is a growing concern throughout the world. The widespread presence of highly toxic compounds of arsenic, antimony, and cadmium in nature poses a particular threat to [...] Read more.
In the face of flourishing industrialization and global trade, heavy metal and metalloid contamination of the environment is a growing concern throughout the world. The widespread presence of highly toxic compounds of arsenic, antimony, and cadmium in nature poses a particular threat to human health. Prolonged exposure to these toxins has been associated with severe human diseases, including cancer, diabetes, and neurodegenerative disorders. These toxins are known to induce analogous cellular stresses, such as DNA damage, disturbance of redox homeostasis, and proteotoxicity. To overcome these threats and improve or devise treatment methods, it is crucial to understand the mechanisms of cellular detoxification in metal and metalloid stress. Membrane proteins are key cellular components involved in the uptake, vacuolar/lysosomal sequestration, and efflux of these compounds; thus, deciphering the multilevel regulation of these proteins is of the utmost importance. In this review, we summarize data on the mechanisms of arsenic, antimony, and cadmium detoxification in the context of membrane proteome. We used yeast Saccharomyces cerevisiae as a eukaryotic model to elucidate the complex mechanisms of the production, regulation, and degradation of selected membrane transporters under metal(loid)-induced stress conditions. Additionally, we present data on orthologues membrane proteins involved in metal(loid)-associated diseases in humans. Full article
(This article belongs to the Special Issue Research in Membrane Transporters—Unveiling the Molecular Mechanisms and Practical Application)
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