Sources of all-trans retinal oxidation independent of the aldehyde dehydrogenase 1A isozymes exist in the postnatal testis†.
Aldh1A
Aldh1a2
WIN 18,446
retinoic acid
spermatogenesis
spermatogonia
testis
Journal
Biology of reproduction
ISSN: 1529-7268
Titre abrégé: Biol Reprod
Pays: United States
ID NLM: 0207224
Informations de publication
Date de publication:
01 02 2019
01 02 2019
Historique:
received:
23
05
2018
revised:
01
08
2018
accepted:
11
09
2018
pubmed:
25
9
2018
medline:
31
3
2020
entrez:
25
9
2018
Statut:
ppublish
Résumé
Despite the essential role of the active metabolite of vitamin A, all-trans retinoic acid (atRA) in spermatogenesis, the enzymes, and cellular populations responsible for its synthesis in the postnatal testis remain largely unknown. The aldehyde dehydrogenase 1A (ALDH1A) family of enzymes residing within Sertoli cells is responsible for the synthesis of atRA, driving the first round of spermatogenesis. Those studies also revealed that the atRA required to drive subsequent rounds of spermatogenesis is possibly derived from the ALDH1A enzymes residing within the meiotic and post-meiotic germ cells. Three ALDH1A isozymes (ALDH1A1, ALDH1A2, and ALDH1A3) are present in the testis. Although, ALDH1A1 is expressed in adult Sertoli cells and is suggested to contribute to the atRA required for the pre-meiotic transitions, ALDH1A2 is proposed to be the essential isomer involved in testicular atRA biosynthesis. In this report, we first examine the requirement for ALDH1A2 via the generation and analysis of a conditional Aldh1a2 germ cell knockout and a tamoxifen-induced Aldh1a2 knockout model. We then utilized the pan-ALDH1A inhibitor (WIN 18446) to test the collective contribution of the ALDH1A enzymes to atRA biosynthesis following the first round of spermatogenesis. Collectively, our data provide the first in vivo evidence demonstrating that animals severely deficient in ALDH1A2 postnatally proceed normally through spermatogenesis. Our studies with a pan-ALDH1A inhibitor (WIN 18446) also suggest that an alternative source of atRA biosynthesis independent of the ALDH1A enzymes becomes available to maintain atRA levels for several spermatogenic cycles following an initial atRA injection.
Identifiants
pubmed: 30247516
pii: 5105748
doi: 10.1093/biolre/ioy200
pmc: PMC6378859
doi:
Substances chimiques
Isoenzymes
0
Tamoxifen
094ZI81Y45
Tretinoin
5688UTC01R
Aldehyde Dehydrogenase 1 Family
EC 1.2.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
547-560Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM111772
Pays : United States
Organisme : NICHD NIH HHS
ID : R01 HD010808
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007750
Pays : United States
Organisme : NICHD NIH HHS
ID : U54 HD042454
Pays : United States
Informations de copyright
© The Author(s) 2018. Published by Oxford University Press on behalf of Society for the Study of Reproduction.
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