Copper‑containing amine oxidase purified from Lathyrus sativus as a modulator of human neutrophil functions.
Journal
International journal of molecular medicine
ISSN: 1791-244X
Titre abrégé: Int J Mol Med
Pays: Greece
ID NLM: 9810955
Informations de publication
Date de publication:
May 2020
May 2020
Historique:
received:
02
08
2019
accepted:
27
01
2020
pubmed:
24
4
2020
medline:
5
2
2021
entrez:
24
4
2020
Statut:
ppublish
Résumé
Over the last few decades, copper‑containing amine oxidase (Cu‑AO) from vegetal sources, and belonging to the class of diamine oxidase, has been documented to exhibit beneficial effects in both in vivo and ex vivo animal models of inflammatory or allergic conditions, including asthma‑like reaction and myocardial or intestinal ischemia‑reperfusion injuries. The aim of the present study was to assess the potential of vegetal Cu‑AO as an anti‑inflammatory and an antiallergic agent and to clarify its antioxidant properties. In cell‑free systems, the reactive oxygen species and reactive nitrogen species scavenging properties of Cu‑AO that is purified from Lathyrus sativus were investigated. Its effect on the formyl‑methionyl‑leucyl‑phenylalanine peptide (fMLP)‑activated cellular functions of human neutrophils were subsequently analyzed. The obtained results demonstrated that Cu‑AO is not a scavenger of superoxide or nitric oxide, and does not decompose hydrogen peroxide. However, it inhibits the fMLP‑dependent superoxide generation, elastase release and cell migration, and interferes with the process of calcium flux, supporting the idea that plant Cu‑AO can interact with human neutrophils to modulate their inflammatory function. Therefore, the importance of these properties on the possible use of vegetal Cu‑AO to control inflammatory conditions, particularly intestinal inflammation, is discussed in the current study.
Identifiants
pubmed: 32323757
doi: 10.3892/ijmm.2020.4535
doi:
Substances chimiques
Plant Proteins
0
Superoxides
11062-77-4
Nitric Oxide
31C4KY9ESH
Hydrogen Peroxide
BBX060AN9V
Amine Oxidase (Copper-Containing)
EC 1.4.3.21
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM