L-amino acid oxidase 1 in sperm is associated with reproductive performance in male mice and bulls.
L-amino acid
acrosome reaction
hydrogen peroxide
male fertility
sperm viability
Journal
Biology of reproduction
ISSN: 1529-7268
Titre abrégé: Biol Reprod
Pays: United States
ID NLM: 0207224
Informations de publication
Date de publication:
07 05 2021
07 05 2021
Historique:
received:
29
09
2020
revised:
21
01
2021
accepted:
12
02
2021
pubmed:
17
2
2021
medline:
5
1
2022
entrez:
16
2
2021
Statut:
ppublish
Résumé
Sperm quality is an important indicator of male fertility, and a suitable biomarker enables the selection of high-quality spermatozoa. We previously found that L-amino acid oxidase encoded by the L-amino acid oxidase 1 (Lao1) gene exerts biological roles in the mammary gland and brain by converting specific L-amino acids into keto acids, ammonia, and hydrogen peroxide (H2O2). Here, we describe the role of Lao1 in male reproduction. Lao1-deficient (Lao1-/-) male mice generated fewer pregnant embryos and pups as well as lower ratios of fertilized oocytes and even ovulated number was not different, suggesting that male subfertility caused the smaller litters. We found that LAO1 expressed in acrosomes is associated with high malformation ratios and low viability of Lao1-/- sperm. Wild-type (WT) sperm produced more H2O2 than Lao1-/- sperm, and 10 μM H2O2 restored knockout (KO) sperm viability in vitro. In addition, the sperm ratio of induced acrosome reaction was higher in WT than in Lao1-/- sperm incubated with the calcium ionophore A23187. Moreover, LAO1 expression was abundant in bovine sperm with high fertilization ratios. We concluded that LAO1 localized in the sperm acrosome influences sperm viability and morphology as well as the acrosome reaction, and that LAO1-deficient sperm might cause male subfertility. Thus, LAO1 might serve as a novel marker for selecting high-quality spermatozoa, especially for livestock reproduction.
Identifiants
pubmed: 33590844
pii: 6137629
doi: 10.1093/biolre/ioab024
doi:
Substances chimiques
L-Amino Acid Oxidase
EC 1.4.3.2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1154-1161Informations de copyright
© The Author(s) 2021. Published by Oxford University Press on behalf of Society for the Study of Reproduction. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.