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- W1898525837 endingPage "1794" @default.
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- W1898525837 abstract "ABSTRACT Plasma membrane-anchored proteases have key roles in cell signaling, migration and refashioning the cell surface and its surroundings. We report the first example of a plasma membrane-anchored protease on mature sperm, testase 1 (ADAM 24). Unlike other studied sperm ADAMs (fertilin α and β, cyritestin) whose metalloprotease domains are removed during sperm development, we found testase 1 retains an active metalloprotease domain, suggesting it acts as a protease on mature sperm. Testase 1 is a glycoprotein (molecular mass 88 kDa), localized to the equatorial region of the plasma membrane of cauda epididymal sperm. Typically, proteolytic removal of the pro-domain is an initial activation step for ADAM proteases. The pro-domain of the testase 1 precursor (108 kDa) is proteolytically removed as sperm transit the caput epididymis to produce processed (mature) testase 1 (88 kDa). Testase 1 is unique among all studied ADAMs in that its proteolytic processing occurs on the sperm plasma membrane instead of at an intracellular site (the Golgi). Using GST-fusion proteins and a synthetic testase 1 C-terminal peptide, we found that the cytoplasmic tail of testase 1 could be phosphorylated in vitro by protein kinase C (PKC). Thus testase 1 apparently has a cytoplasmic PKC phosphorylation site(s). Protein kinase C is known to stimulate other ADAMs’ protease activity. Because events of the acrosome reaction include PKC activation, we speculate that testase 1 protease function could be important in sperm penetration of the zona pellucida after sperm PKC is activated during the acrosome reaction." @default.
- W1898525837 created "2016-06-24" @default.
- W1898525837 creator A5029839843 @default.
- W1898525837 creator A5070103960 @default.
- W1898525837 creator A5078892626 @default.
- W1898525837 date "2001-05-01" @default.
- W1898525837 modified "2023-09-27" @default.
- W1898525837 title "Testase 1 (<i>ADAM 24</i>) a plasma membrane-anchored sperm protease implicated in sperm function during epididymal maturation or fertilization" @default.
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- W1898525837 doi "https://doi.org/10.1242/jcs.114.9.1787" @default.
- W1898525837 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11309208" @default.
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