Calcium Influx and Male Fertility in the Context of the Sperm Proteome: An Update

Freshly ejaculated spermatozoa are incapable or poorly capable of fertilizing an oocyte. The fertilization aptness of spermatozoa depends on the appropriate and time-dependent acquisition of hyperactivation, chemotaxis, capacitation, and the acrosome reaction, where calcium (Ca2+) is extensively involved in almost every step. A literature review showed that several ion channel proteins are likely responsible for regulation of the Ca2+uptake in spermatozoa. Therefore, manipulation of the functions of channel proteins is closely related to Ca2+influx, ultimately affecting male fertility. Recently, it has been shown that, together with different physiological stimuli, protein-protein interaction also modifies the Ca2+influx mechanism in spermatozoa. Modern proteomic analyses have identified several sperm proteins, and, therefore, these findings might provide further insight into understanding the Ca2+influx, protein functions, and regulation of fertility. The objective of this review was to synthesize the published findings on the Ca2+influx mechanism in mammalian spermatozoa and its implications for the regulation of male fertility in the context of sperm proteins. Finally, Pathway Studio (9.0) was used to catalog the sperm proteins that regulate the Ca2+influx signaling by using the information available from the PubMed database following a MedScan Reader (5.0) search.

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Sperm Proteomics: Road to Male Fertility and Contraception

International Journal of Endocrinology ◽

10.1155/2013/360986 ◽

2013 ◽

Vol 2013 ◽

pp. 1-11 ◽

Cited By ~ 47

Author(s):

Md Saidur Rahman ◽

June-Sub Lee ◽

Woo-Sung Kwon ◽

Myung-Geol Pang

Keyword(s):

Posttranslational Modifications ◽

Gel Electrophoresis ◽

Male Fertility ◽

Large Scale ◽

Polyacrylamide Gel Electrophoresis ◽

Protein Biomarkers ◽

Scientific Publications ◽

Pubmed Database ◽

Protein Functions ◽

Specific Proteins

Spermatozoa are highly specialized cells that can be easily obtained and purified. Mature spermatozoa are transcriptionally and translationally inactive and incapable of protein synthesis. In addition, spermatozoa contain relatively higher amounts of membrane proteins compared to other cells; therefore, they are very suitable for proteomic studies. Recently, the application of proteomic approaches such as the two-dimensional polyacrylamide gel electrophoresis, mass spectrometry, and differential in-gel electrophoresis has identified several sperm-specific proteins. These findings have provided a further understanding of protein functions involved in different sperm processes as well as of the differentiation of normal state from an abnormal one. In addition, studies on the sperm proteome have demonstrated the importance of spermatozoal posttranslational modifications and their ability to induce physiological changes responsible for fertilization. Large-scale proteomic studies to identify hundreds to thousands of sperm proteins will ultimately result in the development of novel biomarkers that may help to detect fertility, the state of complete contraception, and beyond. Eventually, these protein biomarkers will allow for a better diagnosis of sperm dysfunctions and aid in drug development. This paper reviews the recent scientific publications available from the PubMed database to address sperm proteomics and its potential application to characterize male fertility and contraception.

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All four CatSper ion channel proteins are required for male fertility and sperm cell hyperactivated motility

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.0610286104 ◽

2007 ◽

Vol 104 (4) ◽

pp. 1219-1223 ◽

Cited By ~ 300

Author(s):

H. Qi ◽

M. M. Moran ◽

B. Navarro ◽

J. A. Chong ◽

G. Krapivinsky ◽

...

Keyword(s):

Ion Channel ◽

Male Fertility ◽

Sperm Cell ◽

Channel Proteins ◽

Ion Channel Proteins

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Insight into DEG/ENaC Channel Gating from Genetics and Structure

Physiology ◽

10.1152/physiol.00006.2012 ◽

2012 ◽

Vol 27 (5) ◽

pp. 282-290 ◽

Cited By ~ 35

Author(s):

Amy L. Eastwood ◽

Miriam B. Goodman

Keyword(s):

Ion Channel ◽

Research Community ◽

Mechanosensitive Channels ◽

C Elegans ◽

Channel Proteins ◽

New Models ◽

Ion Channel Proteins ◽

Pain Receptors ◽

Insight Into

The founding members of the superfamily of DEG/ENaC ion channel proteins are C. elegans proteins that form mechanosensitive channels in touch and pain receptors. For more than a decade, the research community has used mutagenesis to identify motifs that regulate gating. This review integrates insight derived from unbiased in vivo mutagenesis screens with recent crystal structures to develop new models for activation of mechanically gated DEGs.

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