Low temperature‐induced dimerization of the bovine sperm serine protease, BSp66

Cesari, Andreína; Cacciato, Claudio Santiago; Castro, Rosana Esther de; Sánchez, Jorge

doi:10.1002/jcb.10430

Cited by 6 publications

(15 citation statements)

References 20 publications

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“…BSp66 is a trypsin-like serine protease located at the sperm head of bovine spermatozoa which showed no-crossreactivity with anti-acrosin/pro-acrosin antibodies (Cesari et al 2004a,b). BSp66 dimmerizes by disulfide bonds into a higher form named BSp120 (120 kDa) when bovine spermatozoa is cryopreseved (Cesari et al 2003). As reported for the widespread acrosin system, BSp66 is supposed to be present in other mammalian spermatozoa.…”

Section: Introductionmentioning

confidence: 82%

“…This BSp66 is conserved in molecular mass and location at the acrosomal region of hamster spermatozoa. In our previous work, two forms were identified as a monomer and a dimer of a unique protein that formed disulfide bonds after membrane modification induced by cryopreservation or cold storage (Cesari et al 2003). We reported that the dimeric form, named BSp120 was only found in cryopreserved bovine spermatozoa, while the monomeric form, BSp66, was present in fresh bovine sperm samples.…”

Section: Discussionmentioning

confidence: 99%

“…We have previously found a putative new serine protease in bovine sperm, named BSp66 for bovine sperm protease of 66 kDa (Cesari et al 2003), located at the sperm head surface. This protease was partially purified from bovine sperm and it was demonstrated that it showed no crossreactivity with anti-acrosin/pro-acrosin antibodies (Cesari et al 2004a).…”

Section: Discussionmentioning

confidence: 99%

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Serine protease activity, bovine sperm protease, 66 kDa (BSp66), is present in hamster sperm and is involved in sperm–zona interaction

Cesari

Katunar²,

Monclus³

et al. 2005

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Bovine sperm protease, 66 kDa (BSp66) is a serine protease previously characterized in bovine spermatozoa. Like other proteases, it may be present in sperm from other mammalian species different from bovine, playing a role in the fertilization process. In this study, we looked for BSp66 in hamster spermatozoa using heterologous antibodies against bovine BSp66. An immunoreactive protein was detected by Western blotting in mature and immature sperm. The detected protein had two isoforms similar to the ones reported in bovine sperm. Furthermore, indirect immune detection by fluorescence and electron microscopy assays, showed BSp66 signal at the acrosomal region similar to bovine sperm. As it was determined in bovine sperm, the acrosomal reaction displays the antigen within the acrosomal content. When live hamster sperm was incubated with polyclonal antibody against bovine BSp66 a decrease in the number of sperm bound to zona pellucida in homologous IVF and an impairment of head–head agglutination, were observed. These results suggest that a protease homologous to bovine BSp66 is present in golden hamster spermatozoa, with a conserved molecular mass and cellular location. Moreover, hamster BSp66 is probably involved in zona pellucida recognition.

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Section: Introductionmentioning

confidence: 82%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Serine protease activity, bovine sperm protease, 66 kDa (BSp66), is present in hamster sperm and is involved in sperm–zona interaction

Cesari

Katunar²,

Monclus³

et al. 2005

Reproduction

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“…, 2003). We found proteolytic activity in bovine spermatozoa that we named BSp66 for bovine sperm protease of 66 kDa, with a different molecular mass compared with other sperm proteases reported (Cesari et al. , 2003).…”

Section: Introductionmentioning

confidence: 66%

Partial purification and characterization of a trypsin‐like serine protease from bovine sperm

et al. 2004

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Sperm proteolytic activities are relevant in the enzymatic mechanism of fertilization. Several authors have suggested the presence of serine proteases other than acrosin in mice and human spermatozoa. In this work we describe the characterization of a partially purified bovine sperm serine protease BSp66 and its dimmer, BSp120. Partial purification of the monomer was performed from fresh spermatozoa, while the dimer form of the protease was obtained from cryopreserved spermatozoa. The Mr of BSp120 and BSp66 estimated by zymography and gel filtration chromatography were 120 and 66 kDa, respectively. They were positively stained by Schiff-PAS reagent for glycoproteins and they both digested synthetic peptides with basic amino acids in the P1 site. Polyclonal antibodies against acrosin or proacrosin did not cross-react neither with BSp120, nor BSp66. In addition, antibodies raised in our laboratory against BSp120 and BSp66 did not recognize acrosin or proacrosin suggesting that they are not antigenically related proteins. Also, no cross- reactivity was detected with proteins in the range of 120-66 kDa when antibodies against the proteasome were used. The cellular localization of this protease by optical immunocytochemistry using specific antibodies revealed a positive signal in the apical portion of the sperm head suggesting acrosomal or membrane localization. The evidences presented here characterize BSp66 as a trypsin-like serine protease, a putative new member of this highly redundant proteolytic system of the sperm acrosome.

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“…It dimerises when cryopreserved and forms BSp120 (Cesari et al, 2003). There are evidences of aspartate aminotransferase (AAT), hyaluronidase aminotransferase (HAT) and lactic dehydrogenase (Bhosrekar et al, 1994) in spermatozoa of bovine and GOT GTP, AKP, ACP and LDH in buffaloes (Dhami andKodagali, 1990 andDhami andSahni, 1994).…”

Section: Ne Usmentioning

confidence: 99%

Proteases and Proteases Inhibitors of Semen - A Review

Gurupriya¹

2014

Adv. Anim. Vet. Sci.

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| The ejaculate composition is extremely complicated and variable among livestock species. The seminal proteins and enzymes are vital for ejaculate metabolism, spermatozoa performance, survival, and transport within the feminine reproductive tract. Proteases and proteinase inhibitors are secreted by the accessory sex glands of the male reproductive tract and find mixed with the spermatozoa throughout ejaculation. But an entire understanding of those enzymes and their performance in numerous class species is not obtainable. The performance of the assorted proteinases and protease inhibitors of ejaculate stay a mystery, and only a few studies are conducted concerning the characterization of those enzymes. Throughout this review, we tend to target the current understanding of the key proteases and their inhibitors of ejaculate from various mammalian species.

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Low temperature‐induced dimerization of the bovine sperm serine protease, BSp66

Cited by 6 publications

References 20 publications

Serine protease activity, bovine sperm protease, 66 kDa (BSp66), is present in hamster sperm and is involved in sperm–zona interaction

Serine protease activity, bovine sperm protease, 66 kDa (BSp66), is present in hamster sperm and is involved in sperm–zona interaction

Partial purification and characterization of a trypsin‐like serine protease from bovine sperm

Proteases and Proteases Inhibitors of Semen - A Review

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