Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Although sperm hyaluronidase is thought to play an important role in mammalian fertilization, the molecular function underlying these steps remains largely unknown. In mouse models, sperm-specific SPAM1 and HYAL5 hyaluronidase are believed to function in both sperm penetration of the cumulus matrix and sperm-ZP binding. However, gene-targeting studies for SPAM1 or HYAL5 show that hyaluronidases are not essential for fertilization, despite the fact that exogenous hyaluronidase can disrupt the cumulus matrix. Therefore, to evaluate whether sperm hyaluronidase is essential for mammalian fertilization, it is necessary to generate HYAL5/SPAM1 double-knockout mice. However, generating double-knockout mice is very difficult because these two genes exist on the same chromosome. Recently, investigators have begun to employ the pig model system to study human disease due to its similarities to human anatomy and physiology. In this study, we confirmed that pig SPAM1 exists as a single copy gene on chromosome 18 and is specifically expressed in the testis. In addition, we expressed recombinant pig SPAM1 in human embryonic kidney 293 cells and showed that these enzymes possess hyaluronidase activity. We also demonstrated that a polyclonal antibody against pig sperm hyaluronidase inhibits sperm-egg interactions in an in vitro fertilization (IVF) assay. Our results suggest that pig SPAM1 may play a critical role in pig fertilization and that recombinant SPAM1 can disperse the oocyte-cumulus complex in an IVF assay.
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PMID:Characterization of pig sperm hyaluronidase and improvement of the digestibility of cumulus cell mass by recombinant pSPAM1 hyaluronidase in an in vitro fertilization assay. 2526 Oct 76

Sperm adhesion molecule 1 (SPAM1) is a sperm protein possessing a hyaluronidase domain in its N-terminus and a zona pellucida-binding domain in its C-terminus. Our previous studies showed that bovine spermatozoa potentially have 2 SPAM1 isoforms that present different C-terminal domains, different origins (testis and epididymis) and different locations in spermatozoa. In this study, two approaches were taken to characterize the different SPAM1 isoforms. First, 3'-RACE experiments were done to determine the sequence of the 3' regions of the potential transcripts. Second, by in silico analyses, we aimed to determine whether our antibody that recognizes the N-terminal domain of SPAM1 detects two SPAM1 isoforms or two highly similar, although different, proteins. We found that the 3' regions of SPAM1 transcripts from bovine testis and caput epididymis were identical. Nevertheless, two transcript variants that differ by 90 nucleotides, encoded by an entire exon, are expressed in both tissues. Only the protein encoded by the longest SPAM1 transcript variant was confirmed in ejaculated bull spermatozoa by mass spectrometry. In silico analyses revealed a highly similar protein to SPAM1, PH-20, that could potentially be recognized by our N-terminal antibody. The presence of PH-20 transcripts was confirmed in bovine testis and the protein is present in ejaculated spermatozoa. Our N-terminal antibody possibly recognizes both SPAM1 and the highly homologous protein PH-20 instead of two SPAM1 isoforms. Identifying the proteins implicated in the fertilization process is crucial in order to elucidate their roles and to better understand the complex process of fertilization.
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PMID:SPAM1 and PH-20 are two gene products expressed in bovine testis and present in sperm. 3032 44


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