'OMICS' of Human Sperm: Profiling Protein Phosphatases
| Autor: | Odete A. B. da Cruz e Silva, Luís Korrodi-Gregório, Alberto Barros, Mónica Ferreira, Mário Sousa, Sandra Vieira, Edgar F. da Cruz e Silva, Sandra Rebelo, Margarida Fardilha, Steven L. Pelech, Vladimiro Silva |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Male
Proteomics endocrine system Proteome Biology Biochemistry chemistry.chemical_compound Capacitation Phosphoprotein Phosphatases Genetics Humans Protein phosphorylation Molecular Biology reproductive and urinary physiology Sperm motility Sperm Count urogenital system Kinase Reproducibility of Results Tyrosine phosphorylation Original Articles Okadaic acid Spermatozoa Sperm High-Throughput Screening Assays Protein Transport chemistry Sperm Motility Molecular Medicine Phosphorylation Biotechnology |
| Zdroj: | OMICS: A Journal of Integrative Biology. 17:460-472 |
| ISSN: | 1557-8100 1536-2310 |
| DOI: | 10.1089/omi.2012.0119 |
| Popis: | Phosphorylation is a major regulatory mechanism in eukaryotic cells performed by the concerted actions of kinases and phosphatases (PPs). Protein phosphorylation has long been relevant to sperm physiology, from acquisition of motility in the epididymis to capacitation in the female reproductive tract. While the precise kinases involved in the regulation of sperm phosphorylation have been studied for decades, the PPs have only recently received research interest. Tyrosine phosphorylation was first implicated in the regulation of several sperm-related functions, from capacitation to oocyte binding. Only afterwards, in 1996, the inhibition of the serine/threonine-PP phosphoprotein phosphatase 1 (PPP1) by okadaic acid and calyculin-A was shown to initiate motility in caput epididymal sperm. Today, the current mechanisms of sperm motility acquisition based on PPP1 and its regulators are still far from being fully understood. PPP1CC2, specifically expressed in mammalian sperm, has been considered to be the only sperm-specific serine/threonine-PP, while other PPP1 isoforms were thought to be absent from sperm. This article examines the “Omics” of human sperm, and reports, for the first time, the identification of three new serine/threonine-protein PPs, PPP1CB, PPP4C, and PPP6C, in human sperm, together with two tyrosine-PPs, MKP1 and PTP1C. We specifically localized in sperm PPP1CB and PPP1CC2 from the PPP1 subfamily, and PPP2CA, PPP4C, and PPP6C from the PPP2 subfamily of the serine/threonine-PPs. A semi-quantitative analysis was performed to determine the various PPs' differential expression in sperm head and tail. These findings contribute to a comprehensive understanding of human sperm PPs, and warrant further research for their clinical and therapeutic significance. |
| Databáze: | OpenAIRE |
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