Dataset Information

De novo protein synthesis occurs through cytoplasmic translation machinery in mammalian spermatozoa

ABSTRACT: For decades, it was widely accepted that mammalian spermatozoa were devoid of translational activity due to the functional and morphological changes that occurred during spermatogenesis. However, it was proved that capacitated spermatozoa possess translation activity, which appears to be ensured by mitochondrial ribosomes. Since mitochondrial translation has several particularities, the hypothesis that sperm translation occurs through mitochondrial ribosomes raises some questions. The main objectives of this work were to study the impact of translation inhibition in the bovine spermatozoa proteome and to identify the de novo synthesized proteins by capacitated bovine spermatozoa. To identify which proteins were de novo translated, capacitated bovine spermatozoa were treated with puromycin and puromycin-peptides were immunoprecipitated. To study the impact of translation inhibitors in capacitated sperm proteome, bovine spermatozoa were capacitated in the presence or absence of translation inhibitors - Cycloheximide (CHX, cytoplasmic translation inhibitor) and D-Chloramphenicol (D-CP, mitochondrial translation inhibitor). After capacitation, sperm lysates were analysed by mass spectrometry. We identify nine newly synthesised cytoplasmic proteins by capacitated bovine spermatozoa, which are related to sperm-specific processes. Both translation inhibitors impact differently the sperm proteome leading to the deregulation of cytoplasmic protein related to sperm physiology and function. These results support the existence of cytoplasmic translation in bovine spermatozoa during capacitation.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Bos Taurus (bovine)

TISSUE(S): Spermatozoid

SUBMITTER: Sara Dufour

LAB HEAD: Pedro O. Corda; Margarida Fardilha

PROVIDER: PXD050868 | Pride | 2025-06-13

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	5230_allSpectra.HCD.FTMS.iso_0.apl	Other
	5230_allSpectra.HCD.FTMS.iso_1.apl	Other
	5230_allSpectra.HCD.FTMS.iso_10.apl	Other
	5230_allSpectra.HCD.FTMS.iso_100.apl	Other
	5230_allSpectra.HCD.FTMS.iso_101.apl	Other

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De Novo Protein Synthesis Occurs Through the Cytoplasmic Translation Machinery in Mammalian Spermatozoa.

Corda Pedro O PO Silva Joana Vieira JV Almeida Catarina R CR Pierre Philippe P Fardilha Margarida M

Journal of cellular physiology 20250501 5

The current hypothesis suggests that translation occurs in capacitated spermatozoa through mitochondrial ribosomes. Mitochondrial translation has several particularities, which rise some questions about how mitochondrial ribosomes can ensure sperm translation activity. Here, we aimed to elucidate if cytoplasmic translation occurs in mammalian spermatozoa. A bioinformatic workflow was performed to identify translation-related proteins in human spermatozoa and their association with cytoplasmic tr ...[more]

PMID: 40373039

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Project description:Male factors account for approximately 40% of all infertility. Conventional semen analysis focus on seminal physicochemical property and spermatozoa morphology. They yield no information concerning the functional competence of the spermatozoa(Petrunkina et al., 2007). Owning to the essential role of proteins in the reproductive process, comprehensive and systematic identification of proteome is critical to gain new insights into spermatogenesis and infertility. Recent advances in mass spectrometry have allowed the identification of hundreds to thousands of protein in spermatozoa(Oliva et al., 2008; Amaral et al., 2014; Codina et al., 2015). In major domestic mammalian species, global spermatozoa proteomic profiles have been described in rodents(Baker et al., 2008a; Baker et al., 2008b) and bovine(Peddinti et al., 2008). Meanwhile, lacking of new protein synthesis in spermatozoa supports the current view that the regulation of sperm maturation is controlled by exogenous proteins(O'Rand et al., 2011) (e.g., during epididymal transit). Among the seminal plasma proteins, The human seminal plasma has been comprehensively described (Pilch and Mann, 2006; Batruch et al., 2011; Milardi et al., 2012; Milardi et al., 2013; Sharma et al., 2013). In domestic animal species, some studies performing a systematic analysis on using high throughput proteomics have been performed(Kelly et al., 2006; Moura et al., 2007; Souza et al., 2012; Druart et al., 2013; Soleilhavoup et al., 2014). Buffalos (Bubalus bubalis) are adapted to hot–humid tropical climatic conditions, but have low reproductive efficiency. The low sperm motility maybe contributed to protein components variation of spermatozoa and seminal plasma. The composition of buffalo spermatozoa and buffalo seminal plasma (BSP) remains unknown. Proteomic study would be beneficial to the elucidation of the roles of sperm and BSP proteins in regulation of maturation, motility and fertilization. As such, the aim of the current study was to extensively characterize the differentially expressed protein of buffalo spermatozoa and seminal plasma using a comparative proteomics.