1999
DOI: 10.1002/(sici)1098-2795(199901)52:1<57::aid-mrd8>3.0.co;2-u
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Bull subfertility is associated with low levels of a sperm membrane antigen

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Cited by 61 publications
(41 citation statements)
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“…Bull (Ollero et al 1998) and boar (Huang et al 2009) sperm surface proteins, collected before and after freeze-thawing, showed processing related differences using comparative SDS-PAGE analysis, but the effect of these protein alterations on sperm function remains unknown. The intensity of a fertility-associated protein (P25b; Parent et al 1999) has also been shown to remain stable if bull spermatozoa were stored in liquid nitrogen for !5 days but longer storage periods (O28 days) reduce its abundance compared with that of fresh spermatozoa (Lessard et al 2000). This result is interesting because it suggests that cryo-elution of the protein occurred in an environment where chemically and thermally driven reactions are minimised, and not during cooling or thawing where the majority of damage to the plasma membrane occurs.…”
Section: Sperm Surface Alterations During Sperm Handlingmentioning
confidence: 99%
“…Bull (Ollero et al 1998) and boar (Huang et al 2009) sperm surface proteins, collected before and after freeze-thawing, showed processing related differences using comparative SDS-PAGE analysis, but the effect of these protein alterations on sperm function remains unknown. The intensity of a fertility-associated protein (P25b; Parent et al 1999) has also been shown to remain stable if bull spermatozoa were stored in liquid nitrogen for !5 days but longer storage periods (O28 days) reduce its abundance compared with that of fresh spermatozoa (Lessard et al 2000). This result is interesting because it suggests that cryo-elution of the protein occurred in an environment where chemically and thermally driven reactions are minimised, and not during cooling or thawing where the majority of damage to the plasma membrane occurs.…”
Section: Sperm Surface Alterations During Sperm Handlingmentioning
confidence: 99%
“…Moreover, P26h is found in epididymosomes and becomes GPI-anchored to the sperm surface of the acrosomal region during epididymal transit, via an as yet unknown mechanism (Sullivan et al, 2007). While homologous proteins have subsequently been described in man (P34H; Boué et al, 1996), cattle (P25b; Parent et al, 1999) and monkeys (P31m; Lamontagne et al, 2001), it now appears that P26h mRNA and protein are present in relatively large amounts in the testes of sexually mature hamsters whereas the P26h mRNA in the epididymis is much less (Gaudreault et al, 1999). The cellular origin of the P26h on the acrosome of sperm in the cauda epididymis remains, therefore, to be confirmed.…”
Section: Epididymosomes and Their Proteinsmentioning
confidence: 99%
“…Based on their implication in particular steps of the fertilisation process, many sperm components such as lipids (Brinsko et al 2007), proteins (Bellin et al 1998, Parent et al 1999, ions (Collin et al 2000) and nucleic acids (Lalancette et al 2008) have been proposed to vary in quantity or quality according to the male fertility status in many mammalian species. Levels of P25b, a bovine sperm membrane antigen, are lower in semen from subfertile bulls than in the semen from bulls with high fertility (HF) rates (Parent et al 1999). P25b counterparts in human and hamster, P34H and P26h, are involved in zona pellucida (ZP) recognition , Boue et al 1994.…”
Section: Introductionmentioning
confidence: 99%