Proteomic analysis of the mouse sperm acrosome- towards an understanding of an organelle with diverse functionality

0571542 - BTÚ 2024 RIV NL eng J - Článek v odborném periodiku
Otčenášková, T. - Macickova, E. - Vondráková, Jana - Frolíková, Michaela - Komrsková, Kateřina - Stopková, R. - Stopka, P.
Proteomic analysis of the mouse sperm acrosome- towards an understanding of an organelle with diverse functionality.
European Journal of Cell Biology. Roč. 102, č. 2 (2023), č. článku 151296. ISSN 0171-9335. E-ISSN 1618-1298
Grant CEP: GA MŠMT(CZ) LM2018129; GA MŠMT(CZ) EF18_046/0016045; GA MŠMT(CZ) ED1.1.00/02.0109
Institucionální podpora: RVO:86652036
Klíčová slova: Sperm * Acrosome * Lipocalin * nLC-MS * MS proteomics
Obor OECD: Cell biology
Impakt faktor: 6.6, rok: 2022
Způsob publikování: Open access
https://www.sciencedirect.com/science/article/pii/S0171933523000110?via%3Dihub

The acrosome located within the mammalian sperm head is essential for successful fertilization, as it enables the sperm to penetrate the extracellular layers of the oocyte and fuse with oolemma. However, the mammalian acrosomal vesicle is no longer considered to contain only hydrolytic enzymes. Using label-free nano-scale liquid chromatography tandem mass spectrometry (nLC-MS/MS) proteomics, we identified a total of 885 proteins in the acrosome isolated from spermatozoa obtained from cauda epididymis of free-living house mice Mus musculus musculus contains a total of 885 proteins. Among these, 334 proteins were significantly enriched in the acrosome thus representing 27.3% of the whole proteome of the intact sperm. Importantly, we have detected a total of nine calycins while eight of them belong to the lipocalin protein family. In mice, lipocalins are involved in multi-level chemical communication between individuals including pheromone transport and odor perception. Using an indirect immunofluorescence assay, we demonstrated that lipocalin 5 (LCN5) is expressed in the mouse germ cells, and after completing spermatogenesis, it remains localized in the sperm acrosome until the last step of the extratesticular maturation, the acrosome reaction. The presence of lipocalins in the acrosome and acrosome-reacted sperm suggests their original role as chelators of organic and potentially toxic compounds resulting from ongoing spermiogenesis. Along with this evidence, detected mitochondrial (e.g., a subunit of the cyto-chrome c oxidase MTCO1) and proteasomal proteins (subunits of both 20 S core proteasome [PSMA2, PSMBs] and 19 S regulatory particle [PSMDs]) in acrosomes provide further evidence that acrosomes could also function as `waste baskets` after testicular sperm maturation.
Trvalý link: https://hdl.handle.net/11104/0347899