Comparative proteomic study between human normal motility sperm and idiopathic asthenozoospermia

Shen, Shuai; Wang, Jinzi; Liang, Junlin; He, Dalin

doi:10.1007/s00345-013-1023-5

Cited by 82 publications

(59 citation statements)

References 29 publications

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“…The function and exact location of this protein in flagella has not yet been clarified. Shen et al (2013) showed lower amounts of this protein in idiopathic asthenoospermia [47]. Paasch et al (2011) demonstrated higher expression levels of SPANX C, a isomer form of protein, in the sperm of diabetic and obese individuals [48].…”

Section: Discussionmentioning

confidence: 94%

A proteomic analysis on human sperm tail: comparison between normozoospermia and asthenozoospermia

Hashemitabar

Sabbagh

Orazizadeh

et al. 2015

J Assist Reprod Genet

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Purpose Asthenozoospermia is a common cause of human male infertility characterized by reduced sperm motility. The molecular mechanism that impairs sperm motility is not fully understood. This study proposed to identify novel biomarkers by focusing on sperm tail proteomic analysis of asthenozoospermic patients. Methods Sperm were isolated from normozoospermic and asthenozoospermic semen samples. Tail fractions were obtained by sonication followed by Percoll gradient. The proteins were extracted by solubilization and subjected to two-dimensional gel electrophoresis (2-DE); then, the spots were analyzed using Image Master 2D Platinum software. The significantly increased/ decreased amounts of proteins in the two groups were exploited by matrix-assisted laser desorption-ionization time-of-flight/ time-of-flight (MALDI-TOF-TOF) mass spectrometry. Results Three hundred ninety protein spots were detected in both groups. Twenty-one protein spots that had significantly altered amounts (p<0.05) were excised and exploited using MALDI-TOF-TOF mass spectrometry. They led to the identification of the following 14 unique proteins: Tubulin beta 2B; glutathione S-transferase Mu 3; keratin, type II cytoskeletal 1; outer dense fiber protein 2; voltage-dependent anionselective channel protein 2; A-kinase anchor protein 4; cytochrome c oxidase subunit 6B; sperm protein associated with the nucleus on the X chromosome B; phospholipid hydroperoxide glutathione peroxidase-mitochondrial; isoaspartyl peptidase/L-asparaginase; heat shock-related 70 kDa protein 2; stress-70 protein, mitochondrial; glyceraldehyde-3-phosphate dehydrogenase, testis-specific and clusterin. Conclusion Fourteen proteins present in different amounts in asthenozoospermic sperm tail samples were identified, four of which are reported here for the first time. These proteins might be used as markers for the better diagnosis of sperm dysfunctions, targets for male contraceptive development, and to predict embryo quality.

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Section: Discussionmentioning

confidence: 94%

A proteomic analysis on human sperm tail: comparison between normozoospermia and asthenozoospermia

Hashemitabar

Sabbagh

Orazizadeh

et al. 2015

J Assist Reprod Genet

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“…In the algorithm, we initialize the map with a size of (26,5) and the training is done in two phases: (a) rough training with large (initial) neighborhood radius and large (initial) learning rate; (b) fine-tuning with small radius and learning rate. The batch training algorithm is iterative, but instead of using a single data vector at a time, the whole data set is presented to the map before any adjustments are made.…”

Section: Validation Of Pathways By Clustering Proteins By Self Organimentioning

confidence: 99%

Human Spermatozoa Quantitative Proteomic Signature Classifies Normo- and Asthenozoospermia

Saraswat

Joenväära

Jain

et al. 2017

Molecular & Cellular Proteomics

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Scarcely understood defects lead to asthenozoospermia, which results in poor fertility outcomes. Incomplete knowledge of these defects hinders the development of new therapies and reliance on interventional therapies, such as in vitro fertilization, increases. Sperm cells, being transcriptionally and translationally silent, necessitate the proteomic approach to study the sperm function. We have performed a differential proteomics analysis of human sperm and seminal plasma and identified and quantified 667 proteins in sperm and 429 proteins in seminal plasma data set, which were used for further analysis. Statistical and mathematical analysis combined with pathway analysis and self-organizing maps clustering and correlation was performed on the data set.It was found that sperm proteomic signature combined with statistical analysis as opposed to the seminal plasma proteomic signature can differentiate the normozoospermic versus the asthenozoospermic sperm samples. This is despite the results that some of the seminal plasma proteins have big fold changes among classes but they fall short of statistical significance. S-Plot of the sperm proteomic data set generated some high confidence targets, which might be implicated in sperm motility pathways. These proteins also had the area under the curve value of 0.9 or 1 in ROC curve analysis.Various pathways were either enriched in these proteomic data sets by pathway analysis or they were searched by their constituent proteins. Some of these pathways were axoneme activation and focal adhesion assembly, glycolysis, gluconeogenesis, cellular response to stress and nucleosome assembly among others. The mass spectrometric data is available via ProteomeXchange with identifier PXD004098. Molecular & Cellular

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“…Similarly, a study in which obesity-induced asthenozoospermic sperm was analyzed reported alterations in the expression of proteins involved in cytoskeletal regulation, vesicle biogenesis, metabolism and protein degradation involved in spermiogenesis and sperm motility [95]. Interestingly, another comparative study of sperm proteome of asthenozoospermic phenotype with its transcriptome revealed that the effect on sperm motility is not entirely consistent at different molecular levels and evidenced that PTMs, such as N-glycosylation, may play an important role in sperm motility [96]. Phosphorylation is another important PTM that regulates sperm motility that has also been subject for differential proteomic studies.…”

Section: Studymentioning

confidence: 94%

Advances in sperm proteomics: best-practise methodology and clinical potential

Codina

Estanyol

Fidalgo

et al. 2015

Expert Review of Proteomics

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The recent application of mass spectrometry to the study of the sperm cell has led to an unprecedented capacity for identification of sperm proteins in a variety of species. Knowledge of the proteins that make up the sperm cell represents the first step towards understanding its normal function and the molecular anomalies associated with male infertility. The present review starts with an introduction of the sperm cell biology and is followed by the consideration of the methodological key aspects to be aware of during sample sourcing and preparation, including data interpretation. It then overviews the initiatives developed so far towards the completion of the sperm proteome, with a particular focus in human but with the inclusion of some comments on different model species. Finally, all studies performing differential proteomics in infertile patients are reviewed, pointing to future potential applications.

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Comparative proteomic study between human normal motility sperm and idiopathic asthenozoospermia

Abstract: These experimental results expand the scope of the protein database, generating targets for further investigation of the pathogenic mechanism of idiopathic asthenozoospermia.

Cited by 82 publications

References 29 publications

A proteomic analysis on human sperm tail: comparison between normozoospermia and asthenozoospermia

A proteomic analysis on human sperm tail: comparison between normozoospermia and asthenozoospermia

Human Spermatozoa Quantitative Proteomic Signature Classifies Normo- and Asthenozoospermia

Advances in sperm proteomics: best-practise methodology and clinical potential

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