Labeled substance P as a neuropeptide reporter substance for enzyme activity.
Angiotensin-converting enzyme
Chloride
Complex regional pain syndrome
Dabsyl
Substance P
Thin-layer chromatography
Journal
Journal of pharmaceutical and biomedical analysis
ISSN: 1873-264X
Titre abrégé: J Pharm Biomed Anal
Pays: England
ID NLM: 8309336
Informations de publication
Date de publication:
30 Jan 2020
30 Jan 2020
Historique:
received:
08
08
2019
revised:
18
10
2019
accepted:
22
10
2019
pubmed:
14
11
2019
medline:
5
6
2020
entrez:
14
11
2019
Statut:
ppublish
Résumé
Recently, we developed a bradykinin reporter assay and demonstrated the differing protease activity in Complex Regional Pain Syndrome patients vs. controls. In order to further characterize CRPS pathophysiology, the neuropeptide substance P was evaluated as possible reporter substance, here. It was labeled with a chromophore at the lysine residue and generated two major fragments following incubation with serum (amino acid residues 3-8 and 3-11) which were reproducibly separated by thin-layer chromatography. Dabsylated substance P was shown to be a substrate of angiotensin-converting enzyme. The combination of both bradykinin and substance P reporter substances with specific enzyme inhibitors will shed more light on biochemical pathways in inflammatory processes and pain. Comparative clinical studies are now needed to define the application range of both assays in more detail.
Identifiants
pubmed: 31718985
pii: S0731-7085(19)31950-8
doi: 10.1016/j.jpba.2019.112953
pii:
doi:
Substances chimiques
Angiotensin-Converting Enzyme Inhibitors
0
Neuropeptides
0
Substance P
33507-63-0
Peptidyl-Dipeptidase A
EC 3.4.15.1
Bradykinin
S8TIM42R2W
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
112953Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.