Requirement of protein tyrosine kinase and phosphatase activities for human sperm exocytosis

Tomes, Claudia N.; Roggero, Carlos M.; Blas, Gerardo De; Saling, Patricia M.; Mayorga, Luis S.

doi:10.1016/j.ydbio.2003.09.032

Cited by 57 publications

(55 citation statements)

References 84 publications

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“…Following that, a study further described the presence and activity of PTP1B at the protein level in human sperm. Their finding supported the idea that capacitation might modulate tyrosine phosphorylation through inhibition of some PTPs [49]. Similarly, Seligman et al suggested that diminished PTP activity promoted tyrosine phosphorylation of sperm proteins during rat sperm maturation [50].…”

Section: Discussionmentioning

confidence: 58%

Protein tyrosine phosphatase non-receptor type 14 is a novel sperm-motility biomarker

Chao

Chung

Pan

et al. 2011

J Assist Reprod Genet

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Purpose To understand the molecular basis of spermmotility and to identify related novel motility biomarkers. Methods Two-dimensional electrophoresis (2DE) followed by Reverse-phase-nano-high-performance liquid chromatography-electrospray ionization tandem mass spectrometry (RP-nano-HPLC-ESI-MS/MS) were applied to establish the human sperm proteome. Then the sperm proteome of moderate-motile human sperm fraction and that of good-motile human sperm fraction from pooled spermatozoa of forty normozoospermic donors (Group 1 subjects) were compared to identify the dysregulated proteins. Among these down-regulated proteins, Protein tyrosine phosphatase non-receptor type 14 (PTPN14) was chosen to reconfirm by Western blotting and semiquantitative reverse transcription polymerase chain reaction. For clinical application, Western blotting and real-time reverse transcription polymerase chain reaction was performed to compare the expression level of PTPN14 in (Group 2 subjects) nine normozoospermic controls and thirty-three asthenozoospermic patients (including 21 mild asthenozoospermic cases and 12 severe cases). Finally, bioinformatic tools prediction and immunofluorescence assay were performed to elucidate the potential localization of PTPN14. Results The expression levels of three proteins were observed to be lower in the moderate-motile sperm fraction than in good-motile sperm of group 1 subjects. Among three proteins with persistent down-regulation in the moderate-motile sperm, we reconfirmed that the expression level of PTPN14 was significantly lower in both mRNA and protein levels from the moderate-motile sperm fraction. Further, down-regulation of PTPN14 was found at the translational and transcriptional level in the asthenozoospermic men. Finally, Bioinformatic tools prediction and immunofluorescence assay showed that PTPN14 maybe predominantly localized at the mitochondria in the midpiece of human ejaculated sperm. Conclusions Proteomics tools were applied to identify three possible sperm motility-related proteins. Among these proteins, PTPN14 was highly likely a novel spermmotility biomarker and a potential mitochondrial protein.Capsule Protein tyrosine phosphatase non-receptor type 14 is a novel sperm-motility biomarker proven by proteomic tools.Electronic supplementary material The online version of this article

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Section: Discussionmentioning

confidence: 58%

Protein tyrosine phosphatase non-receptor type 14 is a novel sperm-motility biomarker

Chao

Chung

Pan

et al. 2011

J Assist Reprod Genet

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“…The role of genistein in capacitation is not well defined; Fraser et al [49] reported that genistein at low concentrations (1, 10 and 100 nmol L -1 ) accelerated the capacitation and acrosome loss in human spermatozoa measured by CTC staining. On the other hand, several studies have shown the capacity of genistein taken at a higher concentration to inhibit the progesterone-induced acrosome reaction [50][51][52]. Besides these differences related to concentration, another question to take into consideration is related to the possible different mechanisms for induced npg capacitation of fresh spermatozoa and cryocapacitation, as previously described in bull spermatozoa [53].…”

Section: Resultsmentioning

confidence: 93%

Effect of genistein supplementation of thawing medium on characteristics of frozen human spermatozoa

Martínez-Soto¹,

DiosHourcade²,

Gutiérrez‐Adán³

et al. 2010

Asian J Androl

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In this study, we evaluated the effects of genistein supplementation of the thawing extender on frozen-thawed human semen parameters. We analyzed the effect of supplementation on sperm motility, capacitation (membrane lipid disorder), reactive oxygen species (ROS) generation, chromatin condensation and DNA damage. Using this preliminary information, it maybe possible to improve the cryopreservation process and reduce the cellular damage. We have confirmed that the isoflavone genistein (10 mmol L -1 ) has antioxidant properties on the frozen-thawed spermatozoa. This results in a decreased ROS production that shows a slight improvement in the sperm motility, and decreases the membrane lipid disorder and DNA damage caused by cryopreservation. These results suggest an effect of genistein on sperm functionality that could be of interest for assisted reproduction treatments using frozenthawed human spermatozoa, but further studies will be necessary to confirm our findings and to evaluate the possible clinical applications.

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“…Another phosphatase family is protein tyrosine phosphatase (PTPs), which removes phosphate groups from phosphorylated tyrosine residues of proteins (for a review, see Montalibet et al 2005). Both mouse and human spermatozoa contain highly active tyrosine phosphatases and inhibition of tyrosine phosphatases with sodium pervanadate, bis(N,N-dimethylhydroxoamido) hydroxovanadate, ethyl-3,4-dephostatin and phenylarsine oxide prevents the acrosome reaction, suggesting that PTPs play a role in mammalian sperm exocytosis (Tomes et al 2004). With regard to fowl spermatozoa, it is suggested that PP2B appears to be involved in the regulation of the acrosome reaction, since the addition of specific inhibitors of PP2B, such as Figure 5 Effect of SC-9 on (a) the motility and (b) acrosome reaction of fowl spermatozoa incubated with or without IPVL in the presence of 2 mmol CaCl 2 /l at 40 8C.…”

Section: Discussionmentioning

confidence: 99%

Regulation of acrosome reaction of fowl spermatozoa: evidence for the involvement of protein kinase C and protein phosphatase-type 1 and/or -type 2A

Ashizawa¹,

Wishart²,

Katayama³

et al. 2006

Reproduction

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The signal transduction pathways involved in the regulation of the acrosome reaction and motility of fowl spermatozoa were investigated. The motility and acrosomal integrity of fowl spermatozoa in TES/NaCl buffer, with or without homogenised inner perivitelline layers (IPVL), prepared from laid fowl eggs, was almost negligible at 40 8C. In the presence of 2 mmol CaCl 2 /l at 40 8C, motility became vigorous and the acrosome reaction was stimulated when IPVL was added. In the absence of Ca 2C , motility was stimulated by the addition of calyculin A and okadaic acid, both specific inhibitors of protein phosphatase-type 1 (PP1) and -type 2A (PP2A), but Okadaic acid, which is a weaker inhibitor of PP1, did not completely restore motility at 40 8C. However, the acrosome reaction was significantly and equally stimulated in a dose-dependent manner by both inhibitors in the range of 10-1000 nmol/l, when spermatozoa were incubated with IPVL but without Ca 2C . These inhibitors did not stimulate the acrosome reaction in the absence of IPVL. The vigorous motility of spermatozoa, stimulated by the addition of Ca 2C, was reduced gradually as the concentrations of SC-9, a selective activator of protein kinase C (PKC), were increased and a similar SC-9-induced inhibition was observed in the acrosome reaction in the presence of Ca 2C and IPVL. These results confirm that IPVL is necessary for the activation of the acrosome reaction in fowl spermatozoa and that Ca 2C plays an important role in the stimulation of motility and acrosomal exocytosis. Furthermore, it appears that the intracellular molecular mechanisms for the regulation of acrosome reaction of fowl spermatozoa are different from those for the restoration of motility, i.e., protein dephosporylation involving PP1 and/or PP2A in the former, and PP1 alone in the latter case. In addition, the activation of PKC may contribute to a decrease in the flagellar movement and acrosome reaction of fowl spermatozoa.

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Requirement of protein tyrosine kinase and phosphatase activities for human sperm exocytosis

Cited by 57 publications

References 84 publications

Protein tyrosine phosphatase non-receptor type 14 is a novel sperm-motility biomarker

Protein tyrosine phosphatase non-receptor type 14 is a novel sperm-motility biomarker

Effect of genistein supplementation of thawing medium on characteristics of frozen human spermatozoa

Regulation of acrosome reaction of fowl spermatozoa: evidence for the involvement of protein kinase C and protein phosphatase-type 1 and/or -type 2A

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