PXD050748 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Identifying a novel hydroxysteroid dehydrogenase enzyme that is capable of testosterone biosynthesis in the mouse |
Description | Androgens, such as testosterone and dihydrotestosterone (DHT), are essential for male sexual development, masculinisation, spermatogenesis, and general lifelong health. Androgens are predominantly synthesised in the testes of mice (~95%) by highly specialised cells known as the Leydig cells. There are two known androgen production pathways in the testes of mice: (i) the canonical pathway which synthesises testosterone which can be used as a substrate for the more potent DHT, and (ii) the alternate pathway which can synthesise DHT without the need for testosterone. The HSD17B3 enzyme is a key enzyme in the canonical pathway which converts androstenedione into testosterone and the SRD5A1 enzyme is the predominant 5α-reductase in the testes that converts androgen precursors into the alternate pathway. HSD17B3 deficiency in humans results in a disorder of sexual development with 46,XY individuals appearing with female or ambiguous external genitalia whilst having Wolffian internal structures. However, in contrast to humans, Hsd17b3 knockout (KO) mice can be identified as male from birth and throughout adulthood, remain fertile and have normal intratesticular testosterone levels indicating that compensatory mechanisms are apparent in the mouse. What these compensatory mechanisms are, be other enzymes, or other androgen production pathways, remains unknown. We have generated a mouse model incorporating wild-type (WT), Hsd17b3 KO and Hsd17b3; Srd5a1 double (d)KO mice. Proteomic analysis has been performed on WT, Hsd17b3 KO and dKO whole testis tissue to identify potential androgen compensatory mechanisms in the mouse and pathways that are impacted by the removal of the HSD17B3 or both the HSD17B3 and SRD5A1 proteins. The total proteins detected across the three groups were 2,892, 3,041, and 2813 in WT, Hsd17b3 KO and dKO testes, respectively. |
HostingRepository | PRIDE |
AnnounceDate | 2025-05-12 |
AnnouncementXML | Submission_2025-05-12_06:02:10.313.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD050748 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | David Skerrett-Byrne |
SpeciesList | scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; |
ModificationList | acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Eclipse |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2024-03-18 17:49:22 | ID requested | |
⏵ 1 | 2025-05-12 06:02:11 | announced | |
Publication List
Keyword List
submitter keyword: Androgens, Alternate Pathway, HSD17B7, Canonical Pathway, testosterone, SRD5A1, Testosterone Biosynthesis, HSD17B3 |
Contact List
Professor Lee Smith |
contact affiliation | Office for Research, Griffith University, Southport, QLD 4222, Australia |
contact email | Lee.smith@griffith.edu.au |
lab head | |
David Skerrett-Byrne |
contact affiliation | Helmholtz Zentrum München |
contact email | David.Skerrett-Byrne@newcastle.edu.au |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD050748
- Label: PRIDE project
- Name: Identifying a novel hydroxysteroid dehydrogenase enzyme that is capable of testosterone biosynthesis in the mouse