PXD052170-1

PXD052170 is an original dataset announced via ProteomeXchange.

Title	Loss of fertilizing ability of sturgeon spermatozoa cryopreserved with the use of DMSO is not related to impairment of sperm motility but alteration of proteins involved in acrosome reaction, egg recognition and early stages of embryo development
Description	Background: The cryopreservation of semen is crucial for conserving genetic diversity and reproductive success in endangered species like the Siberian sturgeon. However, this process can cause cryodamage, affecting quality and protein profile of spermatozoa. While cryoprotectants like dimethyl sulfoxide (DMSO) and methanol (MeOH) facilitate post-thaw motility recovery, DMSO-preserved spermatozoa exhibit reduced fertilizing ability. This study investigates how DMSO and MeOH impact the proteome of Siberian sturgeon spermatozoa and examines semen quality parameters. Two complementary approaches of quantitative proteomics, liquid chromatography-mass spectrometry (LC-MS) and two-dimensional difference in gel electrophoresis (2D-DIGE), were used to analyze the proteomic profiles of fresh and cryopreserved spermatozoa, as well as the extracellular medium (EM; n=7 for each group). Results: Cryopreservation led to a decline in motility parameters (MOT, VCL, PROG) and viability, along with an increase in ROS levels, membrane fluidity, and acrosome damage. Despite similar quality parameters between DMSO and MeOH-preserved sperm, DMSO-preserved sperm showed dramatically lower fertilization success (6.2% vs 51.2%). A total of 224 and 118 differentially abundant proteins in spermatozoa cryopreserved with MeOH and DMSO, respectively, were identified compared to fresh samples, with 342 and 363 proteins released into the EM. The most affected proteins by cryopreservation included H2A, CABYR, PYGM, ENO3, DBI and LTA4H. Additionally, 36 and 39 uniquely altered sperm-leakage proteins were identified for MeOH and DMSO cryopreserved samples, respectively. Bioinformatic analysis showed that MeOH-specific proteins were related to chromosomal structure and mitochondrial functionality, while DMSO-specific proteins were mainly involved in acrosome reaction, zona pellucida binding, flagella structure, and nuclear pore organization. These proteins are potentially involved in sturgeon sperm fertilizing ability. The expression of six proteins was verified by western blot analysis. Conclusions: This study provides the first comprehensive proteomic characterization of Siberian sturgeon spermatozoa after cryopreservation with DMSO and MeOH, revealing insights into proteomic changes that affect fertilizing ability and aiding conservation efforts for this endangered species.
HostingRepository	PRIDE
AnnounceDate	2024-08-11
AnnouncementXML	Submission_2024-08-10_16:20:40.714.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD052170
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Agata Malinowska
SpeciesList	scientific name: Acipenser baerii; NCBI TaxID: 27689;
ModificationList	methylthiolated residue; phosphorylated residue; monohydroxylated residue
Instrument	Orbitrap Exploris 480

Revision	Datetime	Status	ChangeLog Entry
0	2024-05-10 05:38:57	ID requested
⏵ 1	2024-08-10 16:20:41	announced
2	2024-10-22 06:54:43	announced	2024-10-22: Updated project metadata.

10.6019/PXD052170;

10.1038/s41598-024-68395-7;

submitter keyword: extracellular medium, mass spectrometry, cryopreservation,Acipenser baerii, semen, proteome

Mariola A. Dietrich
contact affiliation	Department of Gamete and Embryo Biology, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Poland
contact email	m.dietrich@pan.olsztyn.pl
lab head
Agata Malinowska
contact affiliation	IBB PAS
contact email	esme@ibb.waw.pl
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD052170
     1. Label: PRIDE project
     2. Name: Loss of fertilizing ability of sturgeon spermatozoa cryopreserved with the use of DMSO is not related to impairment of sperm motility but alteration of proteins involved in acrosome reaction, egg recognition and early stages of embryo development