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Post-translational modifications of seminal proteins and their importance in male fertility potential

ABSTRACT Introduction: The seminal proteome has been shown to directly influence the male fertile potential. Post-translational modifications (PTMs) are significant changes that play a role in the biological regulation of… Click to show full abstract

ABSTRACT Introduction: The seminal proteome has been shown to directly influence the male fertile potential. Post-translational modifications (PTMs) are significant changes that play a role in the biological regulation of proteins. Sperm cells are transcriptionally and translationally inactive and these modifications are essential to control protein function. Areas covered: Here we reviewed seven PTMs which importance for male reproductive function investigated in the past decade, namely S-nitrosylation and tyrosine nitration (both occurring by the action of NO), glycosylation, ubiquitination, acetylation, methylation, and SUMOylation. Since they were previously identified in human semen, we focus on their role in sperm function, as well as in physiological and pathophysiological processes which could contribute to the fertility potential. The following keywords were applied: ‘post-translational modification’, ‘sperm’, ‘semen’, ‘seminal plasma’, ‘male infertility’, ‘nitrosylation’, ‘nitration’, ‘histone methylation’, ‘SUMOylation’, ‘ubiquitination’, ‘ubiquitilation’, ‘glycosylation’, and ‘acetylation’. Expert opinion: Most biological processes orchestrated by proteins require PTMs for their activation or inhibition. Most of them are dynamic and occur in mature sperm, modulating protein function, thus exerting a significant role in sperm function and fertility. Finally, the study of PTMs should be also addressed in pathophysiological processes, as different clinical conditions are known to alter the proteome.

Keywords: post translational; fertility potential; function; translational modifications; importance male

Journal Title: Expert Review of Proteomics
Year Published: 2019

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