Motility of carp spermatozoa is associated with profound changes in the sperm proteome

Dietrich, Mariola A.; Dietrich, G.J.; Mostek, Agnieszka; Ciereszko, Andrzej

doi:10.1016/j.jprot.2016.02.029

Cited by 29 publications

(23 citation statements)

References 52 publications

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“…In the current study, motility was blocked in the presence of the PKC inhibitor (chelerythrine) both in C. carpio and A. ruthenus spermatozoa, and results of Western blotting and immunolabeling indicated the presence of PKC and phosphorylated PKC substrates in spermatozoa of both species. Though we were not able to identify PKC substrates in carp spermatozoa due to low signal from antibodies on immunoblots of 2D gels, the involvement of protein kinase C and casein kinase substrate protein in carp sperm motility has been recently reported (Dietrich et al 2016). Thus, our results indicate that this protein is temporarily phosphorylated during motility period.…”

Section: Involvement Of Pka and Pkc In Sperm Motilitycontrasting

confidence: 62%

Protein phosphorylation in spermatozoa motility of Acipenser ruthenus and Cyprinus carpio

et al. 2017

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Spermatozoa of externally fertilizing freshwater fish possess several different modes of motility activation. Spermatozoa of common carp ( L.) are activated by hypoosmolality, whereas spermatozoa of sterlet () require Ca2+ and low concentration of K+ for motility activation. Intracellular signaling differs between these two species as well, particularly in terms of utilization of secondary messengers (cAMP and Ca2+), and kinase activities. The current study was performed in order to determine the importance of protein phosphorylation and protein kinases for activation of sperm motility in carp and sterlet. Treatment with kinase inhibitors indicates that protein kinases A and C (PKA and PKC) participate in spermatozoa motility of both species. Immunodetection of phospho-(Ser/Thr) PKA substrates shows that phosphorylated proteins are localized differently in spermatozoa of carp and sterlet. Strong phosphorylation of PKC substrate was observed in flagella of sterlet spermatozoa, whereas in carp sperm, PKC substrates were lightly phosphorylated in the midpiece and flagella. Motility activation induced either phosphorylation or dephosphorylation on serine, threonine and tyrosine residues of numerous proteins in carp and sterlet spermatozoa. Proteomic methods were used to identify proteins whose phosphorylation state changes upon the initiation of sperm motility. Numerous mitochondrial and glycolytic enzymes were identified in spermatozoa of both species, as well as axonemal proteins, heat shock proteins, septins and calcium-binding proteins. Our results contribute to an understanding of the roles of signaling molecules, protein kinases and protein phosphorylation in motility activation and regulation of two valuable fish species, and.

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Section: Involvement Of Pka and Pkc In Sperm Motilitycontrasting

confidence: 62%

Protein phosphorylation in spermatozoa motility of Acipenser ruthenus and Cyprinus carpio

et al. 2017

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“…Previous studies showed that that ubiquitin–proteasome pathways exhibit significantly higher activity levels in germline tissues than in somatic tissues of Ascaris suum [86]. In carp spermatozoa, ubiquitin–proteasome pathways have also been shown to be related to sperm energy metabolism and motility [87]. In addition, in human semen, asthenozoospermic samples showed lower levels of proteasome alpha complex than those from normozoospermic patients [88].…”

Section: Discussionmentioning

confidence: 99%

Different expression patterns of sperm motility-related genes in testis of diploid and tetraploid cyprinid fish†

Zhou

et al. 2017

Biology of Reproduction

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Sperm motility is an important standard to measure the fertility of male. In our previous study, we found that the diploid spermatozoa from allotetraploid hybrid (4nAT) had longer durations of rapid and slow progressive motility than haploid spermatozoa from common carp (COC). In this study, to explore sperm motility-related molecular mechanisms, we compared the testis tissues transcriptomes from 2-year-old male COC and 4nAT. The RNA-seq data revealed that 2985 genes were differentially expressed between COC and 4nAT, including 2216 upregulated and 769 downregulated genes in 4nAT. Some differentially expressed genes, such as tubulin genes, dynein, axonemal, heavy chain(dnah) genes, mitogen-activated protein kinase(mapk) genes, tektin 4, FOX transcription factors, proteasome genes, and ubiquitin carboxyl-terminal hydrolase(uchl) genes, are involved in the regulation of cell division, flagellar and ciliary motility, gene transcription, cytoskeleton, energy metabolism, and the ubiquitin–proteasome system, suggesting that these genes were related to sperm motility of the 4nAT. We confirmed the differential expression of 12 such genes in 4nAT by quantitative PCR. By western blotting, we also confirmed increased expression of Uchl3 in 4nAT testis. In addition, we identified 1915 and 2551 predicted long noncoding RNA (lncRNA) transcripts from testis tissue transcriptomes of COC and 4nAT, respectively. Of these, 1575 lncRNAs were specifically expressed in 4nAT and 939 were specifically expressed in COC. This study provides insights into the transcriptome profile of testis tissues from diploid and tetraploid, which are useful for research on regulatory mechanisms behind sperm motility in male polyploidy.

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“…IDH3 catalyses the reversible oxidative decarboxylation of isocitrate to yield α‐ketoglutarate (α‐KG) and CO 2 as part of the TCA cycle in glucose metabolism (Huh et al, ). Its presence is previously reported in human spermatozoa (Schumacher et al, ) and higher levels of IDH3A expression is observed in activated spermatozoa compared to immobilized spermatozoa of fishes (Dietrich, Dietrich, Mostek, & Ciereszko, ). Tubulin is a key constituent of the microtubules arranged in the tail of spermatozoa, but the association between the expression levels of Tubulin and fertility parameters is not well explained yet (Peknicova et al, ).…”

Section: Discussionmentioning

confidence: 56%

“…IDH3 catalyses the reversible oxidative decarboxylation of isocitrate to yield α-ketoglutarate (α-KG) and CO 2 as part of the TCA cycle in glucose metabolism (Huh et al, 1997). Its presence is previously reported in human spermatozoa (Schumacher et al, 2013) and higher levels of IDH3A expression is observed in activated spermatozoa compared to immobilized spermatozoa of fishes (Dietrich, Dietrich, Mostek, & Ciereszko, 2016).…”

Section: Discussionmentioning

confidence: 56%

Comparative proteomic analysis of high‐ and low‐fertile buffalo bull spermatozoa for identification of fertility‐associated proteins

Aslam

Kumaresan

Yadav

et al. 2019

Reprod Domestic Animals

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Contents The present study identified few potential proteins in the spermatozoa of buffalo bulls that can be used as an aid in fertility determination through comparative proteomics. The sperm proteome of high‐fertile buffalo bulls was compared with that of low‐fertile buffalo bulls using two‐dimensional difference gel electrophoresis (2D‐DIGE), and the differentially expressed proteins were identified through mass spectrometric method. The protein interaction network and the functional bioinformatics analysis of differentially expressed proteins were also carried out. In the spermatozoa of high‐fertile bulls, 10 proteins were found overexpressed and 15 proteins were underexpressed at the level of twofold or more (p ≤ 0.05). The proteins overexpressed in high‐fertile spermatozoa were PDZD8, GTF2F2, ZNF397, KIZ, LOH12CR1, ACRBP, PRSS37, CYP11B2, F13A1 and SPO11, whereas those overexpressed in low‐fertile spermatozoa were MT1A, ATP5F1, CS, TCRB, PRODH2, HARS, IDH3A, SRPK3, Uncharacterized protein C9orf9 homolog isoform X4, TUBB2B, GPR4, PMP2, CTSL1, TPPP2 and EGFL6. The differential expression ranged from 2.0‐ to 6.1‐fold between the two groups, where CYP11B2 was high abundant in high‐fertile spermatozoa and MT1A was highly abundant in low‐fertile spermatozoa. Most of the proteins overexpressed in low‐fertile spermatozoa were related to energy metabolism and capacitation factors, pointing out the possible role of pre‐mature capacitation and cryo‐damages in reducing the fertility of cryopreserved buffalo spermatozoa.

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Motility of carp spermatozoa is associated with profound changes in the sperm proteome

Cited by 29 publications

References 52 publications

Protein phosphorylation in spermatozoa motility of Acipenser ruthenus and Cyprinus carpio

Protein phosphorylation in spermatozoa motility of Acipenser ruthenus and Cyprinus carpio

Different expression patterns of sperm motility-related genes in testis of diploid and tetraploid cyprinid fish†

Comparative proteomic analysis of high‐ and low‐fertile buffalo bull spermatozoa for identification of fertility‐associated proteins

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