Strategies for quantifying the enzymatic activities of glycoside hydrolases within cells and in vivo.

Aggregation-induced emission Bioluminescence imaging Cell imaging Enzyme kinetics Fluorescence imaging Fluorescence quenching Glycosidase Glycoside hydrolase High content imaging Photoacoustic imaging Ratiometric substrate Substrate synthesis

Journal

Current opinion in chemical biology
ISSN: 1879-0402
Titre abrégé: Curr Opin Chem Biol
Pays: England
ID NLM: 9811312

Informations de publication

Date de publication:
Dec 2023
Historique:
received: 11 03 2023
revised: 21 09 2023
accepted: 22 09 2023
medline: 1 12 2023
pubmed: 20 10 2023
entrez: 19 10 2023
Statut: ppublish

Résumé

Within their native milieu of the cell, the activities of enzymes are controlled by a range of factors including protein interactions and post-translational modifications. The involvement of these factors in fundamental cell biology and the etiology of diseases is stimulating interest in monitoring enzyme activities within tissues. The creation of synthetic substrates, and their use with different imaging modalities, to detect and quantify enzyme activities has great potential to propel these areas of research. Here we describe the latest developments relating to the creation of substrates for imaging and quantifying the activities of glycoside hydrolases, focusing on mammalian systems. The limitations of current tools and the difficulties within the field are summarised, as are prospects for overcoming these challenges.

Identifiants

pubmed: 37856901
pii: S1367-5931(23)00141-2
doi: 10.1016/j.cbpa.2023.102403
pii:
doi:

Substances chimiques

Glycoside Hydrolases EC 3.2.1.-

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

102403

Informations de copyright

Copyright © 2023 Elsevier Ltd. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: David Vocadlo reports a relationship with Alectos Therapeutics that includes: board membership, consulting and advisory, and equity. David Vocadlo is an inventor of a pending patent on Substrates for imaging glucocerebrosidase activity assigned to Simon Fraser University. Matthew Deen is an inventor of a pending patent on Substrates for imaging glucocerebrosidase activity assigned to Simon Fraser University.

Auteurs

Matthew C Deen (MC)

Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.

Pierre-André Gilormini (PA)

Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.

David J Vocadlo (DJ)

Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada; Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada. Electronic address: dvocadlo@sfu.ca.

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Classifications MeSH