ArticleThe Biochemical journal2007
Mouse testicular hyaluronidase-like proteins SPAM1 and HYAL5 but not HYALP1 degrade hyaluronan.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 34 citations in OpenAlex.
- Molecular interplay between sperm and oocyte: a narrative review.Human reproduction update · 2026Review
- Functional Analysis ofInternational journal of molecular sciences · 2025Article
- Hyaluronidase: structure, mechanism of action, diseases and therapeutic targets.Molecular biomedicine · 2025Review
- Article
- A modified flavonoid accelerates oligodendrocyte maturation and functional remyelination.Glia · 2020Article
- Article
- Impact of glycosylation on the unimpaired functions of the sperm.Clinical and experimental reproductive medicine · 2015Review
- Biology of hyaluronan: Insights from genetic disorders of hyaluronan metabolism.World journal of biological chemistry · 2015Review
- Hyaluronan fragments as mediators of inflammation in allergic pulmonary disease.Immunobiology · 2015Review
- Hyaluronan as an immune regulator in human diseases.Physiological reviews · 2011Review
- Designed human serum hyaluronidase 1 variant, HYAL1DeltaL, exhibits activity up to pH 5.9.The Journal of biological chemistry · 2009Article
- Oocyte-specific deletion of complex and hybrid N-glycans leads to defects in preovulatory follicle and cumulus mass development.Reproduction (Cambridge, England) · 2009Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Besides SPAM1 (sperm adhesion molecule 1; formerly named PH-20), further hyaluronidase-like proteins, HYAL5 (hyaluronoglucosaminidase 5) and HYALP1 (hyaluronoglucosaminidase pseudogene 1) are also expressed in murine testicular tissue. As they share a high degree of sequence similarity with known hyaluronidases, all three polypeptides could potentially exhibit hyaluronidase activity, a function that is beneficial for spermatozoa in order to penetrate the hyaluronan-rich cumulus, which surrounds the oocyte. Recently, it was reported that SPAM1-deficient mice are fertile and spermatozoa derived from mutant mice still exhibit hyaluronidase activity [Baba, Kashiwabara, Honda, Yamagata, Wu, Ikawa, Okabe and Baba (2002) J. Biol. Chem. 277, 30310-30314]. We have now recombinantly expressed mouse SPAM1, HYAL5 and HYALP1 in Xenopus laevis oocytes and determined their respective expression pattern in testis. Transcripts of all three genes are expressed in seminiferous tubules in regions where maturing spermatogenic cells reside. SPAM1 and HYAL5 but not HYALP1 proteins exhibit hyaluronidase activity at neutral pH. The two active hyaluronidases are both bound to the cell surface via a glycosylphosphatidylinositol anchor. Furthermore, structural characteristics are discussed that are necessary for hyaluronidases in order to exhibit hyaluronan cleavage.
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