Proteomic Insights into Seminal Plasma and Spermatozoa Proteins of Small-Spotted Catsharks, Scyliorhinus canicula: Implications for Reproductive Conservation in Aquariums

Author:

Muñoz-Baquero Marta12ORCID,Lorenzo-Rebenaque Laura3ORCID,García-Domínguez Ximo3ORCID,Valdés-Hernández Jesús3ORCID,García-Párraga Daniel24ORCID,Marin Clara1ORCID,García-Vázquez Francisco Alberto5,Marco-Jiménez Francisco3ORCID

Affiliation:

1. Department of Animal Production and Health, Veterinary Public Health and Food Science and Technology, Biomedical Research Institute, Faculty of Veterinary Medicine, Cardenal Herrera-CEU University, CEU Universities, Calle Santiago Ramón y Cajal 20, 45115 Alfara del Patriarca, Spain

2. Fundación Oceanogràfic de la Comunidad Valenciana, 46005 Valencia, Spain

3. Institute for Animal Science and Technology, Universitat Politècnica de València, 46022 Valencia, Spain

4. Veterinary Services, Avanqua-Oceanogràfic S.L., Ciudad de las Artes y las Ciencias, 46013 Valencia, Spain

5. Departamento de Fisiología, Facultad de Veterinaria, Universidad de Murcia, Campus de Excelencia Internacional Mare Nostrum, 30100 Murcia, Spain

Abstract

In the ex situ conservation of chondrichthyan species, successful reproduction in aquaria is essential. However, these species often exhibit reduced reproductive success under human care. A key aspect is that conventional sperm analyses do not provide insights into the functional competence of sperm. However, proteomics analysis enables a better understanding of male physiology, gaining relevance as a powerful tool for discovering protein biomarkers related to fertility. The present work aims to build the first proteome database for shark semen and to investigate the proteomic profiles of seminal plasma and spermatozoa from small-spotted catsharks (Scyliorhinus canicula) related to the underlying adaptations to both natural and aquarium environments, thereby identifying the reproductive impact in aquarium specimens. A total of 305 seminal plasma and 535 spermatozoa proteins were identified. Among these, 89 proteins (29.2% of the seminal plasma set) were common to both spermatozoa and seminal plasma. In the seminal plasma, only adenosylhomocysteinase protein showed differential abundance (DAP) between wild and aquarium animals. With respect to the spermatozoa proteins, a total of 107 DAPs were found between groups. Gene Ontology enrichment analysis highlighted the primary functional roles of these DAPs involved in oxidoreductase activity. Additionally, KEGG analysis indicated that these DAPs were primarily associated with metabolic pathways and carbon metabolism. In conclusion, we have successfully generated an initial proteome database for S. canicula seminal plasma and spermatozoa. Furthermore, we have identified protein variations, predominantly within spermatozoa, between aquarium and wild populations of S. canicula. These findings provide a foundation for future biomarker discovery in shark reproduction studies. However, additional research is required to determine whether these protein variations correlate with reproductive declines in captive sharks.

Publisher

MDPI AG

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