Tyrosine phosphoproteome of hamster spermatozoa: Role of glycerol‐3‐phosphate dehydrogenase 2 in sperm capacitation

@article{Kota2009TyrosinePO,
  title={Tyrosine phosphoproteome of hamster spermatozoa: Role of glycerol‐3‐phosphate dehydrogenase 2 in sperm capacitation},
  author={Venkatesh Kota and Vishnu Mukund Dhople and Sisinthy Shivaji},
  journal={PROTEOMICS},
  year={2009},
  volume={9}
}
Capacitation confers on the spermatozoa the competence to fertilize the oocyte. At the molecular level, a cyclic adenosine monophosphate (cAMP) dependent protein tyrosine phosphorylation pathway operates in capacitated spermatozoa, thus resulting in tyrosine phosphorylation of specific proteins. Identification of these tyrosine‐phosphorylated proteins and their function with respect to hyperactivation and acrosome reaction, would unravel the molecular basis of capacitation. With this in view… 
Role of glycerol‐3‐phosphate dehydrogenase 2 in mouse sperm capacitation
TLDR
It has been demonstrated that in the absence of GPD2, hyperactivation and acrosome reaction were significantly altered, and a few changes in protein tyrosine phosphorylation were also observed during capacitation, implying that G PD2 is involved in sperm capacitation.
Identification of NO induced and capacitation associated tyrosine phosphoproteins in buffalo (Bubalus bubalis) spermatozoa.
TLDR
This study identifies the proteins undergo tyrosine phosphorylation in response to NO induced signaling pathways during capacitation of buffalo sperm using 2-D immunoblotting and mass spectrometry.
The protein tyrosine phosphorylation during in vitro capacitation and cryopreservation of mammalian spermatozoa.
TLDR
Information is summarized about the proteins undergoing tyrosine phosphorylation during capacitation and the effect of cryopreservation on PTP as well as the possibilities to reduce the changes associated with cryo-capacitation process.
Functional Characterization of Candidate Tyrosine Phosphoproteins during in Vitro Capacitation of Fresh and Cryopreserved Buffalo Spermatoza.
Before fertilization, mammalian spermatozoa accomplish the capacitation, a wellcontrolled process crucial to fertilize mature oocyte. The protein tyrosine phosphorylation is a meaningful indicator of
Identification of capacitation associated tyrosine phosphoproteins in buffalo (Bubalus bubalis) and cattle spermatozoa.
TLDR
Among several proteins identified in the buffalo capacitated sperm, serine/threonine-protein phosphatase PP1-gamma catalytic subunit, MGC157332 protein, alpha-enolase, 3-oxoacid CoA transferase 2 and actin-like protein 7A were identified as new tyrosine phosphorylation substrates in mammalian spermatozoa.
SRC family kinases in hamster spermatozoa: evidence for the presence of LCK.
TLDR
This is the first report on the presence of LCK, an SFK of hematopoietic lineage in spermatozoa besides being the first study on the role of SFKs in the spermutozoa of Syrian hamsters.
Relationship of protein tyrosine phosphorylation state with tolerance to frozen storage and the potential to undergo cyclic AMP‐dependent hyperactivation in the spermatozoa of Japanese Black bulls
TLDR
Results are consistent with the suggestion that immunodetection levels of tyrosine‐phosphorylated proteins are valid markers that can predict the level of tolerance to frozen storage and the potential to undergo cAMP‐dependent hyperactivation for the spermatozoa of individual Japanese Black bulls.
(S)-α-Chlorohydrin Inhibits Protein Tyrosine Phosphorylation through Blocking Cyclic AMP - Protein Kinase A Pathway in Spermatozoa
TLDR
Results suggested SACH inhibited PTP through blocking cAMP/PKA pathway in sperm, and PTP inhibition may play a role in infertility associated with SACH.
A comprehensive proteomic approach to identifying capacitation related proteins in boar spermatozoa
TLDR
The results from this study elucidate the proteins involved in capacitation, which may aid in the design of biomarkers that can be used to predict boar sperm quality.
Detection, Localization and Tyrosine Phosphorylation Status of Ser/Thr Protein Phosphatase1γ in Freshly Ejaculated, In Vitro Capacitated and Cryopreserved Buffalo Spermatozoa.
TLDR
The results suggest that buffalo spermatozoa express different isoforms of PP1γ protein, which was localized to principle, mid-piece, post-acrosomal and equatorial regions of buffalo spermutozoa and the protein expression and tyrosine phosphorylation ofPP1γ were increased during capacitation.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 69 REFERENCES
Novel Tyrosine-Phosphorylated Post-Pyruvate Metabolic Enzyme, Dihydrolipoamide Dehydrogenase, Involved in Capacitation of Hamster Spermatozoa1
TLDR
This report identifies a candidate protein, dihydrolipoamide dehydrogenase, which is a post-pyruvate metabolic enzyme, exhibiting tyrosine phosphorylation during hamster spermatozoal capacitation, and delineates the temporal involvement of glucose and pyruVate-lactate, showing that the former is required in the earlier stages and the latter for the later stages of hamster infertility capacitation.
Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition
TLDR
A novel mechanism for mammalian gamete interaction is proposed whereby the activation of sperm-surface chaperones by tyrosine phosphorylation during capacitation may trigger conformational changes facilitating the formation of a functional zona pellucida receptor complex on the surface of mammalian spermatozoa.
Identification of proteins undergoing tyrosine phosphorylation during mouse sperm capacitation.
TLDR
It is hypothesized that tyrosine phosphorylation of these proteins can play a role in the regulation of glycolysis during capacitation, but neither the Km nor the Vmax of aldolase changed as a function of capacitation when its enzymatic activity was assayed in vitro, suggesting other levels of regulation for aldlase function.
Regulation of protein-tyrosine phosphorylation and human sperm capacitation by reactive oxygen derivatives.
TLDR
Investigation of the association between protein-tyrosine phosphorylation and ROS-induced human sperm capacitation found some discrepancies are observed in the regulation of these two processes according to the redox status of the spermatozoa.
Tyrosine Phosphorylation of HSP-90 During Mammalian Sperm Capacitation1
TLDR
These results represent the first report of a protein that undergoes tyrosine phosphorylation during mouse sperm capacitation and the first study implicating molecular chaperones in the processes by which mammalian spermatozoa gain the ability to fertilize the oocyte.
Phosphoproteome Analysis of Capacitated Human Sperm
TLDR
The phosphopeptide enrichment and quantification methodology coupled to MS/MS, described here for the first time, can be employed to map and compare phosphorylation sites involved in multiple cellular processes.
Activity of Pyruvate Dehydrogenase A (PDHA) in Hamster Spermatozoa Correlates Positively with Hyperactivation and Is Associated with Sperm Capacitation1
TLDR
Given the localization of PDHA and the evidence that its activity correlates positively with hyperactivation and that its PDHA2 subunit exhibits capacitation-associated protein tyrosine phosphorylation, it appears thatPDHA2 is associated with the process of capacitation.
Capacitation‐associated changes in protein tyrosine phosphorylation, hyperactivation and acrosome reaction in hamster spermatozoa
TLDR
This study is the first to provide evidence that capacitation‐associated protein tyrosine phosphorylation is linked to hyperactivation in hamster spermatozoa.
Novelty of the Pyruvate Metabolic Enzyme Dihydrolipoamide Dehydrogenase in Spermatozoa
TLDR
This is the first report of a direct correlation of the localization, tyrosine phosphorylation, and activity of the important metabolic enzyme, dihydrolipoamide dehydrogenase, implicating dual involvement and regulation of the enzyme during sperm capacitation.
Analysis of chaperone proteins associated with human spermatozoa during capacitation.
TLDR
It is concluded that strong species-specific differences exist in the molecular mechanisms that drive sperm-egg recognition and that alternative, chaperone-independent, mechanisms must underpin sperm-zona interaction in the human.
...
1
2
3
4
5
...