cDNA sequence and deduced amino acid sequence of bovine oviductal fluid catalase

Lapointe, Serge; Légaré, Christine; Gaudreault, Christian; Sullivan, Robert; Sirard, Marc‐André

doi:10.1002/(sici)1098-2795(199811)51:3<265::aid-mrd5>3.0.co;2-n

Cited by 11 publications

(10 citation statements)

References 54 publications

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“…The oviductal environment is a complex, regionalized and hormonally regulated milieu that is fine-tuned during the oestrous cycle to accomplish its different functions on gametes and embryos. In the bovine species, HEP-like glycoconjugates (Parrish et al 1989a), as well as antioxidants, such as catalase and GSH (Lapointe et al 1998, Lapointe & Bilodeau 2003 in oviduct luminal fluid, are under cyclic ovarian control. It is worth noting that they reach a peak during the period of oestrus, i.e.…”

Section: Discussionmentioning

confidence: 99%

Redox control of surface protein sulphhydryls in bovine spermatozoa reversibly modulates sperm adhesion to the oviductal epithelium and capacitation

Gualtieri¹,

Mollo²,

Duma³

et al. 2009

Reproduction

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Oviductal fluid molecules, such as sulphated glycosaminoglycans and disulphide-reductants, may represent periovulatory signals for the release of spermatozoa from the oviductal reservoir in the bovine species. Disulphide-reductants release spermatozoa through the reduction of sperm-surface disulphides to sulphhydryls (SH). Herein, we studied sperm-surface protein SH through labelling with maleimidylpropionyl biocytin in the initial sperm suspension, in the subpopulations able and unable to adhere to the in vitro cultured oviductal epithelium, and in spermatozoa released either through the disulphide-reductant penicillamine (PEN) or the sulphated glycosaminoglycan heparin (HEP). Adhesion assays were performed to study the ability of released spermatozoa to readhere to the oviductal epithelium. Results showed that the level of SH in sperm-surface proteins was: 1) low in adhering spermatozoa; 2) high in spermatozoa unable to adhere; and 3) markedly increased in released spermatozoa. Adhesion assays showed that: 1) PEN-released spermatozoa promptly recovered adhesion after removal of the disulphide-reductant and could be released again in response to PEN; 2) conversely, a limited number of HEP-released spermatozoa was able to readhere to the oviductal epithelium and this ability was not affected by HEP removal. Recovery of adhesion was associated to reoxidation of sperm-surface protein SH and to the reversal of capacitation. In conclusion, redox modulation of sperm-surface protein SH is involved in the release of spermatozoa adhering to the oviduct in vitro; the reversible action of disulphide-reductants might be responsible for intermittent phases of adhesions and releases; and the irreversible action of HEP indicates that it may represent a terminal releasing signal.

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Section: Discussionmentioning

confidence: 99%

Redox control of surface protein sulphhydryls in bovine spermatozoa reversibly modulates sperm adhesion to the oviductal epithelium and capacitation

Gualtieri¹,

Mollo²,

Duma³

et al. 2009

Reproduction

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“…Recent evidence indicating that post-thaw semen characteristics of Murrah buffalo are improved when oviductal secretions are included in the cryopreservation extender (Imam et al, 2008) indicates that the secretions impart a protective effect on the sperm membranes subjected to freeze-thaw. The bovine oviduct is believed to maintain the optimal balance between reactive oxygen species and antioxidants through the activity of glutathione peroxidase, Superoxide dismutase, and catalase (Lapointe and Bilodeau, 2003), and catalase from OF has been shown to bind to sperm (Lapointe et al, 1998). Maintaining an ideal balance between reactive oxygen species and antioxidants is likely important for several aspects of sperm function in the oviduct, including viability and motility.…”

Section: Proteins In Ofmentioning

confidence: 99%

PHYSIOLOGY AND ENDOCRINOLOGY SYMPOSIUM: Evidence that oviduct secretions influence sperm function: A retrospective view for livestock1

Killian¹

2011

Journal of Animal Science

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The mammalian oviduct has long been recognized as an organ essential for successful reproduction. Bovine, ovine, porcine, and equine animal models have offered clear advantages for oviduct study related to gamete physiology, fertilization, and early embryonic development. Livestock species are amenable to surgical alteration of the reproductive tract, estrous cycle manipulation, gamete cryopreservation, and AI, as well as in vitro fertilization and embryo production. Although most reproductive technology developed for livestock was intended to benefit production animal agriculture, these techniques are a treasure trove of tools for researchers to better understand how the oviduct influences gamete function. Oviduct secretions obtained from in vitro tissue cultures or via indwelling oviduct catheters have been used for analyses to define the protein, lipid, carbohydrate, enzyme, and electrolyte compositions of the secretions during the estrous cycle or in response to hormone treatment. Oviduct secretions or components purified from them have also been used in in vitro assays to assess their ability to bind to sperm, influence sperm viability, motility, sperm capacitation, the acrosome reaction, sperm-egg binding, and egg penetration, as well as subsequent embryonic development. Compelling data have emerged which show that the composition of secretions differs during the estrous cycle and that their composition differs whether they originate from the ampullary or isthmic regions of the oviduct. These differences in composition are functionally relevant and associated with different responses by sperm. Evidence indicatess that oviduct-specific glycoproteins, glycosaminoglycans, carbohydrates, norepinepherine, catecholamines, heat-shock protein, and osteopontin are components of the oviductal milieu that have the capacity to modulate sperm function. Future research on the livestock oviduct will likely define the role that oviduct secretions have in modulating sperm function and how these modifications ultimately affect fertilization and embryo development.

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“…In cattle, the major antioxidants found in the oviductal fluid are catalase, superoxide dismutase, glutathione peroxidase, and reduced glutathione (GSH) [24][25][26]. Antioxidants such as catalase and GSH reach their maximal concentration in the bovine oviduct toward the end of the estrous cycle [26] (i.e., when spermatozoa selected and stored through the process of oviductal adhesion are released to migrate toward the fertilization site).…”

Section: Introductionmentioning

confidence: 97%

Redox Regulation of Sperm Surface Thiols Modulates Adhesion to the Fallopian Tube Epithelium1

Talevi¹,

Zagami²,

Castaldo³

et al. 2007

Biology of Reproduction

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Sperm that adhere to the fallopian tube epithelium are of superior quality and adhesion extends their fertile life. It has been postulated that periovulatory signals, as yet undefined, promote sperm release. In the in vitro studies described here, we examined the effects of several antioxidants, reportedly present within oviductal fluid, on the modulation of sperm-oviduct adhesion in bovine species. Results showed that 1) the cell-permeant thiols (penicillamine, beta mercaptoethanol, cysteine, and dithiotreitol), as well as the nonpermeant thiol, reduced glutathione, cause adhering spermatozoa to release from the epithelium; 2) thiol action is exerted on spermatozoa; and 3) oxidized glutathione, as well as the non-thiol antioxidants (dimethylthiourea, trolox, superoxide dismutase, and catalase) have no effect. Sperm surface sulfhydryls labeled with iodoacetamide fluorescein showed that spermatozoa devoid of sulfhydryls on the head surface adhered to the fallopian epithelium in vitro, whereas thiol-induced release increased the exposure of sulfhydryls on the sperm head surface. Finally, analysis of capacitation status demonstrated that uncapacitated spermatozoa adhered to the oviduct, and that thiol-induced release of spermatozoa was accompanied by capacitation. In conclusion, thiol-reducing agents in the oviductal fluid may modulate the redox status of sperm surface proteins, leading to the release of spermatozoa selected and stored through adhesion to the fallopian tube epithelium in the bovine species.

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cDNA sequence and deduced amino acid sequence of bovine oviductal fluid catalase

Cited by 11 publications

References 54 publications

Redox control of surface protein sulphhydryls in bovine spermatozoa reversibly modulates sperm adhesion to the oviductal epithelium and capacitation

Redox control of surface protein sulphhydryls in bovine spermatozoa reversibly modulates sperm adhesion to the oviductal epithelium and capacitation

PHYSIOLOGY AND ENDOCRINOLOGY SYMPOSIUM: Evidence that oviduct secretions influence sperm function: A retrospective view for livestock1

Redox Regulation of Sperm Surface Thiols Modulates Adhesion to the Fallopian Tube Epithelium1

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