Stimulation of protein tyrosine phosphorylation by a progesterone receptor on the cell surface of human sperm.

@article{Tesarik1993StimulationOP,
  title={Stimulation of protein tyrosine phosphorylation by a progesterone receptor on the cell surface of human sperm.},
  author={Jan Tesarik and Jiř{\'i} Moos and Carmen Mendoza},
  journal={Endocrinology},
  year={1993},
  volume={133 1},
  pages={
          328-35
        }
}
Mature human sperm initiate a rapid Ca2+ influx and the acrosomal exocytosis in response to progesterone. Recent evidence indicates that both events can be induced by antibody-mediated cross-linking of a sperm surface progesterone receptor. In many other systems in which signal is generated by receptor cross-linking, protein phosphorylation on tyrosine residues is involved in the signal transduction across the plasma membrane. In this study we examined whether tyrosine phosphorylation is… 

Figures and Tables from this paper

Progesterone-stimulated intracellular calcium increase in human spermatozoa is protein kinase C-independent.
TLDR
It is found that progesterone stimulates sperm PKC activity and that PKC inhibition with staurosporine and bisindolylmaleimide partially reversed the effect of progester one on acrosome reaction, indicating an involvement of the enzyme in the effectof the steroid.
Progesterone stimulates p42 extracellular signal-regulated kinase (p42erk) in human spermatozoa.
TLDR
It is demonstrated that short-term incubation of spermatozoa with progesterone induces phosphorylation and activation of ERKs, resulting in redistribution of the proteins from the post-acrosomal region to the equatorial segment within the sperm head.
Regulation of the Human Sperm Tyrosine Kinase c-yes. Activation by Cyclic Adenosine 3′,5′-Monophosphate and Inhibition by Ca2+ 1
TLDR
Results suggest that cAMP activates while Ca2+ inhibits human sperm c-yes kinase activity, which is a tyrosine kinase putatively responsible for the increases in sperm protein phosphotyrosine content.
Human sperm plasma membrane progesterone receptor(s) and the acrosome reaction.
TLDR
The results strongly support the involvement of sperm plasma membrane receptors in the progesterone-initiated AR and provide a candidate for one such receptor.
Extracellular signal-regulated kinases modulate capacitation of human spermatozoa.
TLDR
The data demonstrate the presence of functional ERKs in human spermatozoa and indicate that these enzymes are involved in activation of these cells during capacitation, providing new insight in clarifying the molecular mechanisms and the signal transduction pathways of this process.
Regulation of protein tyrosine phosphorylation in boar sperm through a cAMP‐dependent pathway
TLDR
The results suggest that a cAMP‐dependent event is required for tyrosine phosphorylation of triton‐insoluble proteins such as p93 and p175, and that sensitivity to calcium and distinct basal levels of cyclic nucleotide PDE might correspond to species‐specific reproduction strategies in mammals.
EFFECT OF TYROSINE KINASE INHIBITORS ON TYROSINE PHOSPHORYLATION AND MOTILITY PARAMETERS IN HUMAN SPERM
TLDR
Genistein was the most active and consistent, inhibiting sperm tyrosine kinase activity, PY proteins, incidence of PY sperm, and sperm motility and motion parameters, such as VEL, ALH, and hyperactivation.
...
...

References

SHOWING 1-10 OF 39 REFERENCES
Progesterone acts at the plasma membrane of human sperm
Progesterone inhibits membrane-bound adenylate cyclase in Xenopus laevis oocytes
Recent experimental evidence indicates that progesterone acts at the cell surface to trigger protein synthesis and to reinitiate the first meiotic division in Xenopus laevis oocytes1,2. The steroid
Phosphatidylinositol 4,5-bisphosphate hydrolysis in human sperm stimulated with follicular fluid or progesterone is dependent upon Ca2+ influx.
TLDR
It is reported here that both a Sephadex G-75 column fraction, derived from follicular fluid, and progesterone stimulate rapid hydrolysis of PtdIns(4,5)P2 and PTDIns4P in human sperm and that progester one stimulates a rapid influx of Ca2+ inhuman sperm.
Receptor tyrosine kinases
  • D. Cadena, G. Gill
  • Biology
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1992
TLDR
The tyrosine kinase receptors are essential for normal growth, development, and reparative processes and mutations that remove normal regulatory constraints on the ~ 290 amino acid kinase core of these large proteins result in constitutive function and cell transformation.
Genistein, a specific inhibitor of tyrosine-specific protein kinases.
Evidence that aggregation of mouse sperm receptors by ZP3 triggers the acrosome reaction
TLDR
It is suggested that the aggregation of sperm molecules recognized by ZP3 glycopeptides or by TPA-treated ZP is sufficient to trigger the events that occur during acrosomal exocytosis.
Acrosin activation follows its surface exposure and precedes membrane fusion in human sperm acrosome reaction.
TLDR
This study characterized further this antibody with regard to its reactivity with different forms of acrosin and found that it recognizes specifically an active form of this enzyme and does not react with its proenzyme form.
...
...