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Circulatory System Esterases and Their Physiologic Roles in Health and Disease

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 (30 July 2024) | Viewed by 1111

Special Issue Editor

Special Issue Information

Dear Colleagues,

The esterases present in the circulatory system hydrolyse ester groups from a large variety of compounds with different molecular weights and lipophilicities that are present in blood as part of body homeostasis or that can appear transiently in circulation due to diet, different disfunctions, or diseases. Since alcohol and acid products are more polar than the parent ester, the action of circulatory esterases generates species with an increased water solubility as compared with the parent ones, speeding up the clearance of potentially harmful lipophilic esters from circulation. A plethora of circulatory system esterases, either present in blood/plasma, attached on the blood vessel walls or contained into various cells present in the bloodstream, ensures the efficient hydrolysis of ester groups in individual compounds or in supramolecular assemblies present in this environment. In this Special Issue, we are encouraging contributions detailing the structure, mechanism of action and physiologic role of different circulatory system esterases, relevance to various diseases, and their activity modulation (inhibition/activation) for therapeutic purposes. The impact of circulatory esterases on the pharmacokinetic of drugs, prodrugs, and drug delivery systems constitutes another focus area of this Special Issue.

Prof. Dr. Marc A. Ilies
Guest Editor

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Keywords

  • esterases and lipases
  • circulatory system
  • blood, plasma, blood vessels, and figurative elements of blood
  • physiopathology
  • structure and catalysis mechanism
  • substrate selectivity
  • activity assays
  • inhibition and activation
  • drugs in clinical use and under development
  • prodrugs
  • drug delivery systems
  • drug pharmacokinetics
  • toxicity and detoxification

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Published Papers (1 paper)

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Research

15 pages, 3829 KiB  
Article
Development and Optimization of a Bromothymol Blue-Based PLA2 Assay Involving POPC-Based Self-Assemblies
by Shibbir Ahmed Khan and Marc A. Ilies
Int. J. Mol. Sci. 2024, 25(17), 9517; https://doi.org/10.3390/ijms25179517 - 1 Sep 2024
Viewed by 479
Abstract
Phospholipase A2 (PLA2) is a superfamily of phospholipase enzymes that dock at the water/oil interface of phospholipid assemblies, hydrolyzing the ester bond at the sn-2 position. The enzymatic activity of these enzymes differs based on the nature of the substrate, its supramolecular assemblies [...] Read more.
Phospholipase A2 (PLA2) is a superfamily of phospholipase enzymes that dock at the water/oil interface of phospholipid assemblies, hydrolyzing the ester bond at the sn-2 position. The enzymatic activity of these enzymes differs based on the nature of the substrate, its supramolecular assemblies (micelle, liposomes), and their composition, reflecting the interfacial nature of the PLA2s and requiring assays able to directly quantify this interaction of the enzyme(s) with these supramolecular assemblies. We developed and optimized a simple, universal assay method employing the pH-sensitive indicator dye bromothymol blue (BTB), in which different POPC (3-palmitoyl-2-oleoyl-sn-glycero-1-phosphocholine) self-assemblies (liposomes or mixed micelles with Triton X-100 at different molar ratios) were used to assess the enzymatic activity. We used this assay to perform a comparative analysis of PLA2 kinetics on these supramolecular assemblies and to determine the kinetic parameters of PLA2 isozymes IB and IIA for each supramolecular POPC assembly. This assay is suitable for assessing the inhibition of PLA2s with great accuracy using UV-VIS spectrophotometry, being thus amenable for screening of PLA2 enzymes and their substrates and inhibitors in conditions very similar to physiologic ones. Full article
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