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L. Yin C. M. Chung R. Huo H. Liu C. Zhou W. Xu H. Zhu J. Zhang Q. Shi H. Y. C. Wong J. Chen Y. Lu Y. Bi C. Zhao Y. Du M. Ma Y. Cai W. Y. Chen K. L. Fok L. L. Tsang K. Li Y. Ni Y. W. Chung Z. Zhou J. Sha H. C. Chan 《Cellular and molecular life sciences : CMLS》2009,66(5):900-908
The acrosome reaction has long been thought to be induced by the zona pellucida. Here we report the identification and function
of a novel human sperm glycosylphosphatidylinositol (GPI)-anchored membrane protein, NYD-SP8. The release of the protein during
sperm-egg interaction and its binding to the cumulus, the first layer of egg investment, elicits cross-talk between the gametes
and produces calcium dependant release of progesterone, which lead to the acrosome reaction. An in vivo mouse model of NYD-SP8 immunization is also established showing a reduced fertility rate. Thus, contrary to accepted dogma,
our study demonstrates for the first time that, prior to reaching the zona pellucida, sperm may release a surface protein
that acts on the cumulus cells leading to the acrosome reaction, which may be important for determining the outcome of fertilization.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users.
Received 11 August 2008; received after revision 18 December 2008; accepted 22 December 2008 相似文献
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Wang Y Guan X Fok KL Li S Zhang X Miao S Zong S Koide SS Chan HC Wang L 《Cellular and molecular life sciences : CMLS》2008,65(23):3822-3829
Rhomboid family members are widely conserved and found in all three kingdoms of life. They are serine proteases and serve
important regulatory functions. In the present study, a novel gene highly expressed in the testis, RHBDD1, is shown to be
a new member of the Rhomboid family, participating in the cleavage of BIK, a proapoptotic member of the Bcl-2 family. The
RHBDD1-involved proteolytic modification is upstream of the BIK protein degradation pathway. Mutagenesis studies show that
the amino acid residues glycine142 and serine144 of RHBDD1 are crucial for its activity in cleaving BIK at a site located
in the transmembrane region. Overexpression or knock-down of RHBDD1 in HEK 293T cells can reduce or enhance BIK-mediated apoptosis,
respectively. The present findings suggest that, by acting as a serine protease, RHBDD1 modulates BIK-mediated apoptotic activity.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users.
Received 31 July 2008; received after revision 16 September 2008; accepted 19 September 2008 相似文献
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