Sperm Ecto-Protein Kinase and Its Protein Substrate: Novel Regulators of Membrane Fusion During Acrosome Reaction
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
Sperm Ecto-Protein Kinase
and Its Protein Substrate:
Novel Regulators of Membrane
Fusion During Acrosome Reaction
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| Creator |
Maiti, Arunima
Nath, Debjani Dungdung, Sandhya Rekha Majumder, Gopal Chandra |
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| Subject |
Cell Biology & Physiology
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| Description |
Previously we have purified and characterized a unique plasma membrane-specific cyclic AMP-independent ecto-protein kinase
(ecto-CIK) as well as its ecto-phosphoprotein substrate (MPS) using caprine sperm model. This study reports for the first time the role of
the sperm external surface protein phosphorylation system on sperm acrosome reaction, which is essential for fertilization. Calcium
ionophore A23187 has been used to trigger the sperm acrosome reaction in vitro. Treatment of sperm cells with CIK antibody (dil: 1:500)
causes a significant decrease (approx. 50%) in percentage of acrosome reacted sperm. Onset of the acrosome reaction causes a
remarkable increase in the rate of acrosin release from the cells in the medium. However, CIK antibody inhibits significantly (approx. 50%)
the acrosin release. The level of membrane-bound MPS as estimated by ELISA and the degree of its phosphorylation catalyzed by the
endogenous ecto-CIK, increase significantly with the progress of the acrosome reaction. Both the parameters increase by approximately
100% during the 20 min of the reaction. MPS antibody (1:100 dilution) markedly decreases (approx. 75%) percentage of acrosome-reacted
sperm. MPS antibody as well shows high efficacy to inhibit acrosin release from spermatozoa. The results demonstrate that the
cell–surface protein kinase and its protein substrate are essential for membrane fusion component of acrosome reaction. The data are
consistent with the view that MPS regulates acrosomal membrane fusion with the overlying plasma membrane by the mechanism of its
phosphorylation and dephosphorylation
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| Publisher |
John Wiley & Sons
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| Date |
2009
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/194/1/JOURNAL_OF_CELLULAR_PHYSIOLOGY%2C220(2)%2C__394%2D400%2C2009[43].pdf
Maiti, Arunima and Nath, Debjani and Dungdung, Sandhya Rekha and Majumder, Gopal Chandra (2009) Sperm Ecto-Protein Kinase and Its Protein Substrate: Novel Regulators of Membrane Fusion During Acrosome Reaction. Journal of Cellular Physiology, 220 (2). pp. 394-400. ISSN 0021-9541 |
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| Relation |
http://dx.doi.org/10.1002/jcp.21778
http://www.eprints.iicb.res.in/194/ |
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