Phospholipases A2 in the reproductive system of the bull

Rönkkö, Seppo; Lahtinen, Risto; Vanha‐Perttula, T.

doi:10.1016/0020-711x(87)90054-1

Cited by 22 publications

(7 citation statements)

References 16 publications

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“…These results differ significantly from those reported previously concerning bovine (30) or human (28,29,31,47,52) seminal plasma PLA 2 . The major human seminal plasma PLA 2 has been found to be identical to the synovial enzyme (31,32).…”

Section: Fig 5 Sensitivity Of the Seminal Enzyme To Pla 2 Inhibitorscontrasting

confidence: 99%

“…Although several studies have been undertaken to characterize the PLA 2 present in the spermatozoa and seminal plasma of various species (25)(26)(27)(28)(29)(30), only the enzyme from human seminal plasma has been purified to homogeneity and sequenced (31) so as to conclusively assign it to a particular PLA 2 group. The enzyme was found to be a 14-kDa protein, identical to the synovial enzyme (32), suggesting the same might be true of other mammalian species.…”

mentioning

confidence: 99%

“…In bovine seminal secretions, the enzyme was partially purified, but was not characterized enough to assign it to a particular PLA 2 group (30). To determine the exact type(s) of PLA 2 present in bovine seminal plasma and to assess the generality of the occurrence of sPLA 2 in mammalian seminal plasma, we purified and characterized the major PLA 2 activity from bovine seminal plasma.…”

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confidence: 99%

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Purification of a Novel Phospholipase A2 from Bovine Seminal Plasma

Soubeyrand

Khadir

Brindle

et al. 1997

Journal of Biological Chemistry

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Phospholipases A2 are enzymes believed to play important roles in numerous physiological systems including sperm cell maturation. Relatively little work has, however, been devoted to study these enzymes in seminal plasma. We therefore undertook the purification and characterization of this enzyme from bovine seminal plasma. After a 330-fold purification, an activity corresponding to a protein of 100 kDa was identified by gel filtration. SDS-polyacrylamide gel electrophoresis analysis of the purified fraction revealed the presence of a 60-kDa band that comigrated with the activity during ion-exchange and gel filtration chromatography as well as polyacrylamide gel electrophoresis. The enzyme possessed a pH optimum around pH 6.5 and was calcium-dependent. Using isoelectric focusing, its isoelectric point was determined to be 5.6 +/- 0.07. The enzymatic activity was resistant to p-bromophenacyl bromide, but was sensitive to gossypol and dithiothreitol. The enzyme was 2 orders of magnitude more active toward micelles formed with deoxycholate than with Triton X-100. Slight differences in the specificity toward head groups and/or sn-2-side chains were found in both assay systems. The enzyme was acid-labile and did not display affinity for heparin. It would therefore appear that the phospholipase A2 form isolated from bovine seminal plasma is of a novel type.

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Section: Fig 5 Sensitivity Of the Seminal Enzyme To Pla 2 Inhibitorscontrasting

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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Purification of a Novel Phospholipase A2 from Bovine Seminal Plasma

Soubeyrand

Khadir

Brindle

et al. 1997

Journal of Biological Chemistry

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“…In this direction, the acrosomal membrane is protected by the egg yolk against the occurrence of spontaneous activation (Iguer-Ouada and Verstegen 2001). Canine sperm could metabolise egg yolk through lipases during cold storage, as was described in sperm from different animal species (Rönkkö and others 1987, Pellicer-Rubio and Combarnous 1998, Carver and Ball 2002) and humans (Kunze and Bohn 1978). Therefore, the protective effect of extenders against freezing injury could be progressively reduced during the cooling process, explaining the low values of VS obtained in frozen semen after cold storage.…”

Section: Discussionmentioning

confidence: 86%

Cryopreservation of canine semen after cold storage in a Neopor box: effect of extender, centrifugation and storage time

et al. 2014

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The aim of this work was to assess the combined effect of sperm centrifugation, semen extender and storage time before freezing on post-thaw sperm quality and freezability on chilled stored canine semen in a Neopor box. Sperm parameters evaluated were total and progressive sperm motility by Computer-Assisted Sperm Analysis (CASA) and sperm viability and acrosome integrity using a triple fluorescent stain. Sperm quality and freezability indexes were also studied. First, the effect of centrifugation and two commercial extenders from Minitübe (Biladyl A and CaniPRO Freeze A) was evaluated in chilled semen after 24 and 45 hours of cold storage. No significant differences were observed between treatments in almost all the sperm parameters assessed. Secondly, chilled semen was frozen after 24 and 45 hours of cold storage in a Neopor box. The best results were obtained when semen was centrifuged, chilled with CaniPRO Freeze A and then frozen after 24 hours of cold storage, showing no differences in both post-thaw sperm quality and freezability in comparison with semen immediately frozen after collection. In conclusion, dog semen centrifuged after collection and extended with CaniPRO Freeze can be frozen after 24 hours of cold storage in a Neopor box, obtaining similar results to semen immediately frozen after collection.

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“…Osteopontin is a protein found in the postacrosomal region of cauda epididymal and ejaculates spermatozoa with a role suggested in fertilization and the blocking of the polyspermy [152], and PLA2 is present in the bull sperm plasma membrane [153], and it is related to acrosome reaction events [154], sperm-egg fusion [155, 156], and probable implications in sperm motility [157]. On the other hand, a lower amount of spermadhesin Z13 was found the protein extracts from those bulls, with a variable association of BSP5 expression.…”

Section: Molecular Markers Of Bull Fertilitymentioning

confidence: 99%

Post Testicular Sperm Maturational Changes in the Bull: Important Role of the Epididymosomes and Prostasomes

Caballero

Frenette

Sullivan

2011

Veterinary Medicine International

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After spermatogenesis, testicular spermatozoa are not able to fertilize an oocyte, they must undergo sequential maturational processes. Part of these essential processes occurs during the transit of the spermatozoa through the male reproductive tract. Since the sperm become silent in terms of translation and transcription at the testicular level, all the maturational changes that take place on them are dependent on the interaction of spermatozoa with epididymal and accessory gland fluids. During the last decades, reproductive biotechnologies applied to bovine species have advanced significantly. The knowledge of the bull reproductive physiology is really important for the improvement of these techniques and the development of new ones. This paper focuses on the importance of the sperm interaction with the male reproductive fluids to acquire the fertilizing ability, with special attention to the role of the membranous vesicles present in those fluids and the recent mechanisms of protein acquisition during sperm maturation.

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Phospholipases A2 in the reproductive system of the bull

Cited by 22 publications

References 16 publications

Purification of a Novel Phospholipase A2 from Bovine Seminal Plasma

Purification of a Novel Phospholipase A2 from Bovine Seminal Plasma

Cryopreservation of canine semen after cold storage in a Neopor box: effect of extender, centrifugation and storage time

Post Testicular Sperm Maturational Changes in the Bull: Important Role of the Epididymosomes and Prostasomes

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