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PDBsum entry 2ceb
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Fertilization
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PDB id
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2ceb
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References listed in PDB file
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Key reference
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Title
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Bovine seminal plasma proteins pdc-109, Bsp-A3, And bsp-30-Kda share functional roles in storing sperm in the oviduct.
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Authors
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T.M.Gwathmey,
G.G.Ignotz,
J.L.Mueller,
P.Manjunath,
S.S.Suarez.
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Ref.
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Biol Reprod, 2006,
75,
501-507.
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PubMed id
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Abstract
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On ejaculation, sperm become coated with proteins secreted by the male accessory
sex glands. In the bull, these proteins consist predominantly of the bovine
seminal plasma family of proteins (BSPs): PDC-109 (BSP-A1/-A2), BSP-A3, and
BSP-30-kDa. PDC-109 plays a role in forming an oviductal sperm reservoir by
enabling sperm to bind to oviductal epithelium. Because PDC-109 has high
sequence identity with the other BSPs, we tested BSP-A3 and BSP-30-kDa for the
capacity to bind sperm to oviductal epithelium. BSP-A3 and BSP-30-kDa each
increased binding of epididymal sperm to epithelium and were as effective as
PDC-109 in competitively inhibiting binding of ejaculated sperm. Because binding
extends the motile life of sperm, BSPs were tested for the ability to maintain
sperm motility. BSP-treated epididymal sperm incubated with plasma membrane
vesicles from bovine oviductal epithelium maintained progressive motility longer
than untreated sperm. To our knowledge, this is the first report of this
protective effect of BSPs. Similarities in function among the BSPs were
reflected in their three-dimensional structure, whereas surface maps of
electrostatic potential indicated differences in binding affinities and
kinetics. Such differences may provide sperm with greater adaptability to
variations among females. Altogether, these results indicate that BSPs play a
crucial role in fertilization by maintaining sperm motility during storage.
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