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Review
. 2020 Feb 27;21(5):1621.
doi: 10.3390/ijms21051621.

Proteomic Analyses of Human Sperm Cells: Understanding the Role of Proteins and Molecular Pathways Affecting Male Reproductive Health

Affiliations
Review

Proteomic Analyses of Human Sperm Cells: Understanding the Role of Proteins and Molecular Pathways Affecting Male Reproductive Health

Ashok Agarwal et al. Int J Mol Sci. .

Abstract

Human sperm proteomics research has gained increasing attention lately, which provides complete information about the functional state of the spermatozoa. Changes in the sperm proteome are evident in several male infertility associated conditions. Global proteomic tools, such as liquid chromatography tandem mass spectrometry and matrix-assisted laser desorption/ionization time-of-flight, are used to profile the sperm proteins to identify the molecular pathways that are defective in infertile men. This review discusses the use of proteomic techniques to analyze the spermatozoa proteome. It also highlights the general steps involved in global proteomic approaches including bioinformatic analysis of the sperm proteomic data. Also, we have presented the findings of major proteomic studies and possible biomarkers in the diagnosis and therapeutics of male infertility. Extensive research on sperm proteome will help in understanding the role of fertility associated sperm proteins. Validation of the sperm proteins as biomarkers in different male infertility conditions may aid the physician in better clinical management.

Keywords: bioinformatics; male infertility; molecular pathways; proteomics; sperm.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Workflow involving the processing of semen samples for sperm proteomics.
Figure 2
Figure 2
Interaction between the differentially expressed proteins and transcriptional factors in varicocele patients with mitochondrial dysfunc­tion. TOMM22: mitochondrial import receptor subunit TOM22 homolog, COX5B: cytochrome c oxidase subunit 5B, mitochondrial, NDUFS1: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, IMMT: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, UQCRC2: cytochrome b-c1 complex subunit 2, mitochondrial, PGAM5: serine/threonine-protein phosphatase PGAM5, mitochondrial, TAL1: T-cell acute lymphocytic leukemia protein 1, ACAT1: acetyl-CoA acetyltransferase, mitochondrial, ECHS1: enoyl-CoA hydratase, mitochondrial, ECH1: delta(3,5)-delta(2,4)-dienoyl-CoA isomerase, mitochondrial, LETM1: mitochondrial proton/calcium exchanger protein, IDH3B: isocitrate dehydro­genase [NAD] subunit beta, mitochondrial, c-Src: proto-oncogene tyrosine-protein kinase Src, PRKAR1A: cAMP-dependent protein kinase type I-alpha regulatory subunit, PRKACA: cAMP-dependent protein kinase catalytic subunit alpha, CISY: citrate synthase, mitochondrial, ACO2: aconitate hydratase, mitochondrial, IDH3A: isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial, HADHA: trifunctional enzyme subunit alpha, mitochondrial, ISOC2: isochorismatase domain-containing protein 2, PKC: protein kinase C, NRF2: nuclear factor erythroid 2 (NFE2)-related factor 2, GCR: glucocorticoid receptor, PPAR-β (Δ): peroxisome proliferator-activated receptor beta or delta, YY1: Yin Yang 1, VDR: vitamin D receptor, ATF: activating transcription factor, CREB: cAMP response element binding, OCT-3/4: octamer-binding transcription factor 3/4, AP-1: activator protein 1, SP1: specificity protein 1, ESR1: estrogen receptor 1, ERR1: steroid hormone receptor ERR1, NF-κB: nuclear factor kappa-light-chain-enhancer of activated B cells.

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