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Published-Ahead-of-Print August 23, 2006, DOI:10.2164/jandrol.106.000356

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Hyalp1 in Murine Sperm function: Evidence for unique and overlapping functions with other Reproductive Hyaluronidases

Kimberly A. Miller , Minghai Shao , and Patricia A. Martin-DeLeon *

* To whom correspondence should be addressed. E-mail: pdeleon{at}udel.edu.

While Sperm adhesion molecule1 (SPAM1) is the highly conserved mammalian sperm hyaluronidase (hyase), multiple hyases are present in the mouse testis. In this study we show that one of the murine hyases, Hyalp1, which is predominantly expressed in the testis in a 24 kDa isoform has neutral enzymatic activity. On sperm it is localized on the plasma membrane of the anterior head and exists predominantly in two isoforms ,~40 and ~66 kDa which has neutral hyase activity at a low level, compared to Spam1 and Hyal5. This activity is associated with in vitro cumulus penetration, since antibody inhibition of Hyalp1 significantly (P= 0.034) retarded the rate of penetration of wild-type (WT) sperm. Antibody-inhibited Spam1 null sperm were more severely retarded (P= 4.2 x 10 -19 ) suggesting an upregulation of Hyalp1 in these mice. A functionality test of the hyaluronic acid (HA) receptor domain identified in the N-terminus by in silico analysis revealed that sperm Hyalp1 is significantly (P=0.006) involved in the progesterone-induced HAenhanced acrosome reaction. Finally, developmental RT-PCR shows that testicular transcripts of Hyalp1 are detected as early as 6 days post-parturition, similar to transcripts for Spam1, suggesting that the gene might also play a role in the developing testes, prior to spermiogenesis. Taken together, the findings reveal that Hyalp1 likely has a unique function in the adult testis, and redundant overlapping ones with Spam1 and may compensate for it in Spam1 null mice.


Key words: Fertilization • Reproductive Genetics • Sperm • Spermatogenesis • Testis




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