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Special Issue "Carbonic Anhydrase and Biomarker Research 2020"

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

Deadline for manuscript submissions: 31 July 2020.

Special Issue Editor

Prof. Dr. Maria Giulia Lionetto
Website
Guest Editor
Department of Biological and Environmental Sciences and Technologies, University of Salento, 73100 Lecce, Itay
Special Issues and Collections in MDPI journals

Special Issue Information

Dear colleagues,

Carbonic anhydrase is a widely distributed metalloenzyme catalysing the reversible hydration of CO2 to HCO3- and H+. It plays a fundamental role in a number of physiological processes, including gas exchange, pH homeostasis, electrolyte transport, metabolic reactions, bone resorption, and calcification. Recently, its involvement in several pathological conditions, as well as sensitivity to chemical pollutants, has advanced the research on carbonic anhydrase in the biomarker discovery field.

A biomarker is defined as a cellular, biochemical, or molecular alteration that is measurable in biological media as an indicator of normal biological process, pathogenic processes, or response to an exposure or intervention. Biomarkers are useful tools in a wide range of fields, including medicine, drug discovery, environmental health, and ecotoxicology.

In recent years, alteration in the expression of specific carbonic anhydrase isoforms has been proposed as diagnostic or prognostic biomarkers in the clinical field, mainly in cancer research.

Moreover, the sensitivity of specific carbonic anhydrase isoforms to environmental pollutants has given rise to new perspectives in the potential use of carbonic anhydrase as a pollution biomarker.

This Special Issue of IJMS is aimed to cover the more recent insights into the research of carbonic anhydrase as a promising biomarker in several areas of interest, from human health to environmental sciences, opening new perspectives for the translation of advances in basic sciences on this ancient enzyme into innovative applications.

Prof. Dr. Maria Giulia Lionetto
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 papers will be 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

  • carbonic anhydrase
  • biomarker
  • pH regulation
  • cancer
  • tumor microenvironment
  • heavy metals
  • pollutant
  • biomonitoring

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Published Papers (3 papers)

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Research

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Open AccessArticle
Synthetic Strategies and Computational Inhibition Activity Study for Triazinyl-Substituted Benzenesulfonamide Conjugates with Polar and Hydrophobic Amino Acids as Inhibitors of Carbonic Anhydrases
Int. J. Mol. Sci. 2020, 21(10), 3661; https://doi.org/10.3390/ijms21103661 - 22 May 2020
Abstract
Various sulfonamide derivatives are intensively studied as anticancer agents owing to their inhibitory activity against human tumor-associated carbonic anhydrase isoforms. In this work, different synthetic procedures for the series of 1,3,5-triazinyl-aminobenzenesulfonamide conjugates with amino acids, possessing polar uncharged, negatively charged, and hydrophobic side [...] Read more.
Various sulfonamide derivatives are intensively studied as anticancer agents owing to their inhibitory activity against human tumor-associated carbonic anhydrase isoforms. In this work, different synthetic procedures for the series of 1,3,5-triazinyl-aminobenzenesulfonamide conjugates with amino acids, possessing polar uncharged, negatively charged, and hydrophobic side chain, were studied and optimized with respect to the yield/purity of the synthesis/product as well as the time of synthetic reaction. These procedures were compared to each other via characteristic HPLC-ESI-DAD/QTOF/MS analytical product profiles, and their benefits as well as limitations were discussed. For new sulfonamide derivatives, incorporating s-triazine with a symmetric pair of polar and some less-polar proteinogenic amino acids, inhibition constants (KIs) against four human carboanhydrases (hCAs), namely cytosolic hCA I, II, transmembrane hCA IV, and the tumor-associated, membrane-bound hCA IX isoforms, were computationally predicted applying various methods of the advanced statistical analysis. Quantitative structure-activity relationship (QSAR) analysis indicated an impressive KI ratio (hCA II/hCA IX) 139.1 and hCA IX inhibition constant very similar to acetazolamide (KI = 29.6 nM) for the sulfonamide derivative disubstituted with Gln. The derivatives disubstituted with Ser, Thr, and Ala showed even lower KIs (8.7, 13.1, and 8.4 nM, respectively). Full article
(This article belongs to the Special Issue Carbonic Anhydrase and Biomarker Research 2020)
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Review

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Open AccessReview
Carbonic Anhydrase Sensitivity to Pesticides: Perspectives for Biomarker Development
Int. J. Mol. Sci. 2020, 21(10), 3562; https://doi.org/10.3390/ijms21103562 - 18 May 2020
Abstract
Carbonic anhydrase (CA) is a widespread metalloenzyme playing a pivotal role in several physiological processes. Many studies have demonstrated the in vitro and in vivo sensitivity of CA to the exposure to several classes of pesticides in both humans and wildlife. This review [...] Read more.
Carbonic anhydrase (CA) is a widespread metalloenzyme playing a pivotal role in several physiological processes. Many studies have demonstrated the in vitro and in vivo sensitivity of CA to the exposure to several classes of pesticides in both humans and wildlife. This review aims to analyze and to discuss the literature available in this field, providing a comprehensive view useful to foresee perspectives for the development of novel CA-based pesticide biomarkers. The analysis of the available data highlighted the ability of several pesticide molecules to interact directly with the enzyme in humans and wildlife and to inhibit CA activity in vitro and in vivo, with possible alterations of key physiological functions. The analysis disclosed key areas of further research and, at the same time, identified some perspectives for the development of novel CA-based sensitive biomarkers to pesticide exposure, suitable to be used in several fields from human biomonitoring in occupational and environmental medicine to environmental monitoring on non-target species. Full article
(This article belongs to the Special Issue Carbonic Anhydrase and Biomarker Research 2020)
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Open AccessReview
Characterization of Carbonic Anhydrase In Vivo Using Magnetic Resonance Spectroscopy
Int. J. Mol. Sci. 2020, 21(7), 2442; https://doi.org/10.3390/ijms21072442 - 01 Apr 2020
Abstract
Carbonic anhydrase is a ubiquitous metalloenzyme that catalyzes the reversible interconversion of CO2/HCO3. Equilibrium of these species is maintained by the action of carbonic anhydrase. Recent advances in magnetic resonance spectroscopy have allowed, for the first time, in [...] Read more.
Carbonic anhydrase is a ubiquitous metalloenzyme that catalyzes the reversible interconversion of CO2/HCO3. Equilibrium of these species is maintained by the action of carbonic anhydrase. Recent advances in magnetic resonance spectroscopy have allowed, for the first time, in vivo characterization of carbonic anhydrase in the human brain. In this article, we review the theories and techniques of in vivo 13C magnetization (saturation) transfer magnetic resonance spectroscopy as they are applied to measuring the rate of exchange between CO2 and HCO3 catalyzed by carbonic anhydrase. Inhibitors of carbonic anhydrase have a wide range of therapeutic applications. Role of carbonic anhydrases and their inhibitors in many diseases are also reviewed to illustrate future applications of in vivo carbonic anhydrase assessment by magnetic resonance spectroscopy. Full article
(This article belongs to the Special Issue Carbonic Anhydrase and Biomarker Research 2020)
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