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• W2029586473 abstract "The macaque sperm surface protein PH-20 is a hyaluronidase, but it also interacts with hyaluronic acid (HA) to increase internal calcium ( [Ca2+]i ) in the sperm cell. A region of the PH-20 molecule, termed Peptide 2 (aa 205–235), has amino acid charge homology with other HA binding proteins. The Peptide 2 sequence was synthesized and two recombinant PH-20 proteins were developed, one containing the Peptide 2 region (G3, aa 143–510) and one without it (E12, aa 291–510). On Western blots, affinity-purified anti-Peptide 2 IgG recognized the 64 kDa band corresponding to PH-20 in acrosome intact sperm and, under reducing conditions, recognized the whole 67 kDa PH-20 and the endoproteolyzed N-terminal fragment of PH-20. HA conjugated to a photoaffinity substrate specifically bound to sperm surface PH-20. Indirect immunofluorescence demonstrated that Fab fragments of anti-Peptide 2 IgG bound to the head of live sperm. Biotinylated HA was bound by Peptide 2 and by sperm extracts in a microplate binding assay, and this binding was inhibited by Fab fragments of anti-Peptide 2 IgG. Biotinylated HA bound to the G3 protein and this binding was inhibited by anti-Peptide 2 Fab, but HA did not bind to the E12 protein. Fab fragments of anti-Peptide 2 IgG inhibited the increase in [Ca2+]i induced in macaque sperm by HA. Our results suggest that the Peptide 2 region of PH-20 is involved in binding HA, which results in the cell signaling events related to the elevation of [Ca2+]i during sperm penetration of the cumulus. Mol. Reprod. Dev. 60: 542–552, 2001. © 2001 Wiley-Liss, Inc." @default.
• W2029586473 created "2016-06-24" @default.
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• W2029586473 date "2001-01-01" @default.
• W2029586473 modified "2023-10-13" @default.
• W2029586473 title "Identification of a hyaluronic acid (HA) binding domain in the PH-20 protein that may function in cell signaling" @default.
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• W2029586473 doi "https://doi.org/10.1002/mrd.1119" @default.
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