β-galactosidase in the seminal plasma and reproductive organs of the bull

Jauhiainen, Anneli; Vanha‐Perttula, T.

doi:10.1016/0020-711x(86)90395-2

Cited by 12 publications

(2 citation statements)

References 24 publications

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“…Beta-galactosidase (GLB1) was in the center of the next distinguished protein group, composed of proteins of presumably epididymal origin-aldose reductase (AKR1B1), β-glucuronidase, β-hexosaminidase (HEXB), and hexokinase 1, which is also involved in the glycolytic enzyme group described above. The GLB1 is a hydrolytic enzyme located mainly in the epididymis, which is probably involved in sperm maturation and can be an indicator for the function of the epididymal cauda (Jauhiainen and Vanha-Perttula, 1986;Dacheux et al, 2003). The AKR1B1 is associated with bull epididymosomes and epididymal spermatozoa (Frenette et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

Analysis of bull (Bos taurus) seminal vesicle fluid proteome in relation to seminal plasma proteome

Westfalewicz

Dietrich

Mostek

et al. 2017

Journal of Dairy Science

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The existing knowledge on the bull seminal vesicle proteome, a major seminal plasma constituent, and its relationship with seminal plasma is limited. This knowledge is prerequisite for a better understanding of seminal plasma variability, which is linked to semen quality. The objective of this study was to characterize the proteomes of seminal vesicle fluid and seminal plasma and to compare them to better understand the origin of seminal plasma proteins. We collected ejaculates and seminal vesicle fluid postmortem from 6 mature Holstein Friesian bulls. We performed the analysis and identification of proteins using 2-dimensional electrophoresis coupled with matrix-assisted laser desorption/ionization mass spectrometry. We identified 105 proteins in bull seminal vesicle fluid and 88 proteins in seminal plasma. For both seminal vesicles and seminal plasma proteins described in our study, top biological functions were cellular movement, cell death and survival, and cellular growth and proliferation. Additionally, seminal vesicle fluid proteins were involved in protein degradation and synthesis. Seminal plasma proteins were also involved in cellular assembly and organization and cell-to-cell signaling and interactions. Proteins of both fluids were involved in the following canonical pathways: glycolysis, gluconeogenesis, liver X receptor/farnesoid X receptor, and farnesoid X receptor/retinoid X receptor activation. Additionally, seminal vesicle fluid proteins appeared to be involved in oxidative stress response mediated by nuclear factor E2-related factor 2. Our results described the bull seminal vesicle fluid proteome for the first time and allowed for significant expansion of the current knowledge on the bull seminal plasma proteome. Moreover, analysis indicated that both bull seminal vesicle fluid and seminal plasma proteomes contained interconnected protein groups related to protective functions, glycolysis, and the morphology and physiology of the spermatozoa. These proteins and their interactions could be targeted in future research.

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Section: Discussionmentioning

confidence: 99%

Analysis of bull (Bos taurus) seminal vesicle fluid proteome in relation to seminal plasma proteome

Westfalewicz

Dietrich

Mostek

et al. 2017

Journal of Dairy Science

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“…/?-Galactosidase forms have been found in washed ejaculated and epididymal spermatozoa from bulls and rats (Jauhiainen and Vanha-Perttula, 1986;Majumder and Turkington, 1974). The latter authors also demonstrated their acrosomal localisation.…”

Section: Discussionmentioning

confidence: 86%

Properties of acidβ‐galactosidase from fowl spermatozoa

Droba

1988

British Poultry Science

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1. Two forms, I and II, of beta-galactosidase [EC 3.2.1.23] from fowl spermatozoa were separated by Blue-Sepharose CL-6B chromatography. 2. The two forms of the enzyme yielded different pI values (4.1 and 4.7 for form I and 5.3 for form II). 3. Their gel filtration patterns were also different: form I resolved into two peaks with Mr about 65,000 and 80,000, whereas form II resolved into a single peak with an Mr of about 65,000. 4. Both forms had similar optimum pH, pH stability, thermal stability and Km values. 5. Differences between the characteristics of beta-galactosidase forms from spermatozoa and from seminal plasma suggest that the beta-galactosidases investigated in this study are spermatozoa-specific.

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Characterization of bovine seminal plasma by proteomics

et al. 2006

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Previous investigations of bovine seminal plasma (BSP) have revealed the identities of the three major proteins, BSP-PDC109, BSP-A3 and BSP-30 kDa, which together constitute about half of the total protein, as well as about 30 of the minor proteins. Analyses of BSP by 2-DE have revealed about 250 protein spots, suggesting that much of the BSP proteome remains undescribed. In this study, BSP has been analyzed by 2-D LC-based and SDS-PAGE-based proteomic methods. Ninety-nine proteins were identified, including 49 minor proteins that have not previously been described in seminal plasma of any species.

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β-galactosidase in the seminal plasma and reproductive organs of the bull

Cited by 12 publications

References 24 publications

Analysis of bull (Bos taurus) seminal vesicle fluid proteome in relation to seminal plasma proteome

Analysis of bull (Bos taurus) seminal vesicle fluid proteome in relation to seminal plasma proteome

Properties of acidβ‐galactosidase from fowl spermatozoa

Characterization of bovine seminal plasma by proteomics

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