Relationship between Seminal Plasma Lactoferrin and Gonadal Function in Horses

Kikuchi, Motohiro; Takao, Yukihiro; Tokuda, Nanako; Ohnami, Yohji; Orino, Koichi; Watanabe, Kiyotaka

doi:10.1292/jvms.65.1273

Cited by 14 publications

(10 citation statements)

References 17 publications

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“…Lactotransferrin, also known as lactoferrin, is a glycosylated 75–82 kDa iron-binding protein that is a member of the transferrin family of proteins [66]. Lactotransferrin has been detected in various mammalian biological fluids [66], including milk, amniotic fluid, tears, and seminal plasma from several species (man [67], dog [68], boar [69], mouse [70], and stallion [68]). Although it is yet to be determined in elephants, lactotransferrin has previously been reported to be synthesized in the epididymis (mice [70], boar [69], and stallion [71]) or prostate and seminal vesicles (man [72]).…”

Section: Discussionmentioning

confidence: 99%

Lactotransferrin in Asian Elephant (Elephas maximus) Seminal Plasma Correlates with Semen Quality

et al. 2013

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Asian elephants (Elephas maximus) have highly variable ejaculate quality within individuals, greatly reducing the efficacy of artificial insemination and making it difficult to devise a sperm cryopreservation protocol for this endangered species. Because seminal plasma influences sperm function and physiology, including sperm motility, the objectives of this study were to characterize the chemistry and protein profiles of Asian elephant seminal plasma and to determine the relationships between seminal plasma components and semen quality. Ejaculates exhibiting good sperm motility (≥65%) expressed higher percentages of spermatozoa with normal morphology (80.3±13.0 vs. 44.9±30.8%) and positive Spermac staining (51.9±14.5 vs. 7.5±14.4%), in addition to higher total volume (135.1±89.6 vs. 88.8±73.1 ml) and lower sperm concentration (473.0±511.2 vs. 1313.8±764.7×106 cells ml−1) compared to ejaculates exhibiting poor sperm motility (≤10%; P<0.05). Comparison of seminal plasma from ejaculates with good versus poor sperm motility revealed significant differences in concentrations of creatine phosphokinase, alanine aminotransferase, phosphorus, sodium, chloride, magnesium, and glucose. These observations suggest seminal plasma influences semen quality in elephants. One- and two-dimensional (2D) gel electrophoresis revealed largely similar compositional profiles of seminal plasma proteins between good and poor motility ejaculates. However, a protein of ∼80 kDa was abundant in 85% of ejaculates with good motility, and was absent in 90% of poor motility ejaculates (P<0.05). We used mass spectrometry to identify this protein as lactotransferrin, and immunoblot analysis to confirm this identification. Together, these findings lay a functional foundation for understanding the contributions of seminal plasma in the regulation of Asian elephant sperm motility, and for improving semen collection and storage in this endangered species.

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Section: Discussionmentioning

confidence: 99%

Lactotransferrin in Asian Elephant (Elephas maximus) Seminal Plasma Correlates with Semen Quality

et al. 2013

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“…Furthermore, although Lf is also a milk protein, its addition to the 0.6% caseinate extender neither improved the sperm characteristics nor impaired them, in addition to not influencing the nitrite and H 2 O 2 concentrations after 24 h of cooling at 5 °C. Lactoferrin has been found in stallion's seminal plasma, and its presence was correlated with sperm concentration ml −1 and total sperm number reflecting a possible role in gonadal health (Inagaki et al ., ; Kikuchi et al ., ). It is known that Lf is synthesised in the stallion epididymis and can be involved in sperm maturation (Kikuchi et al ., ).…”

Section: Discussionmentioning

confidence: 97%

“…Lactoferrin has been found in stallion's seminal plasma, and its presence was correlated with sperm concentration ml −1 and total sperm number reflecting a possible role in gonadal health (Inagaki et al ., ; Kikuchi et al ., ). It is known that Lf is synthesised in the stallion epididymis and can be involved in sperm maturation (Kikuchi et al ., ). In a study of Lf supplementation in different concentrations in bovine semen extenders, Lf improved sperm motility after freezing and thawing.…”

Section: Discussionmentioning

confidence: 97%

Milk, caseinate and lactoferrin addition to equine semen cooling extenders

et al. 2016

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Cooled semen has been used routinely to prolong sperm viability until artificial insemination time. However, spermatozoa are subjected to oxidative stress. The aim of the present work was to investigate the protective and antioxidant effect of the milk proteins lactoferrin (Lf) and caseinate added to equine semen cooling extenders. Semen from six stallions was cooled at 5 °C after resuspension with C1) milk- and glucose-based, C2) 0.6% caseinate, C3) C2 + Lf 200 μg ml , C4) C2 + Lf 500 μg ml and C5) C2 + Lf 1000 μg ml extenders, and kept at 5 °C for 24 h. Sperm motility characteristics and intact membrane rates were not different among the treatments (P > 0.05). As a result of the cooling process, the nitrite concentration increased significantly in the cooled semen (69.6 ± 78.9 μm per ×10 spermatozoa) compared with the fresh semen (8.6 ± 1.9 μm per ×10 spermatozoa). In contrast, the H O concentrations were lower in the 0.6% caseinate extender (265.9 ± 221.3 μm per ×10 spermatozoa) than in the milk extender (430.9 ± 199.8 μm per ×10 spermatozoa, P < 0.05), showing an antioxidative effect of the caseinate compared with the milk. However, in all groups, hydrogen peroxide concentrations were similar to the undiluted fresh semen (332.8 ± 151.3 μm per ×10 spermatozoa). Caseinate showed to be as efficient as milk to protect equine-cooled spermatozoon.

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“…It was identified as a sperm-binding protein, with expression in the cells of the corpus and cauda of the epididymis, which could play a biological role in the protection and regulation of sperm activity (Inagaki et al, 2002;Pearl & Roser, 2014). Through its binding to iron, presents bacteriostatic and antioxidant activities (Kikuchi, Takao, et al, 2003), as iron promotes the production of the ROS by the Fenton and Haber-Weiss reactions, producing hydroxyl radicals and hydrogen peroxide (Baker & Baker, 2005). Due to these properties, Lf was used to modulate cytokines in the endometrium of susceptible mares with artificial insemination with fresh semen (Fedorka et al, 2017).…”

Section: O R I G I N a L A R T I C L Ementioning

confidence: 99%

“…Lactoferrin is one of the most abundant proteins secreted by the stallion epididymis representing approximately 41% of the total protein secretion (Fouchecourt, Metayer, Locatelli, Dacheux, & Dacheux, ). High concentrations of lactoferrin were found in the seminal plasma of horses (Kikuchi, Takao, et al., ) and dogs (Kikuchi, Mizoroki, et al.,). In those studies, seminal lactoferrin was positively correlated with sperm concentration and total sperm number.…”

Section: Introductionmentioning

confidence: 99%

Lactoferrin increases sperm membrane functionality of frozen equine semen

Martins

Silva²,

Côrtes³

et al. 2018

Reprod Domestic Animals

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During cryopreservation, sperm was submitted to an increase in reactive oxygen species generation. This work aimed to improve the quality of frozen equine sperm after the addition of antioxidants lactoferrin (Lf) and catalase (Cat) to a freezing extender. Semen from six stallions was frozen with the extenders: F1) control, INRA 82 freezing extender, F2) F1 + 500 μg/ml Lf and F3) F1 + 200 IU/ml Cat. After thawing, sperm motility parameters, membrane functionality and integrity, and acrosome integrity and spontaneous acrosome-reacted sperm were evaluated with a computer-assisted sperm analysis, a hypoosmotic swelling test and epifluorescent microscopy, respectively. Nitrite, hydroperoxide and iron concentrations of frozen semen were measured with spectrophotometry. The percentage of functional membrane sperm treated with Lf was higher (50.7% ± 11.6%) compared to that of the control (37.6% ± 15.6%), while the iron (61.4 ± 11.6 vs 73.3 ± 13.8 mg/dl) and nitrite concentrations (16.3 ± 7.1 vs 25.9 ± 4.2 μM/μg protein) were lower, respectively (p < .05). Thus, it can be suggested that Lf protect stallion spermatozoon during freezing as it has increased the percentage of sperm with functional membrane and decreased the lipid oxidant agents.

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Relationship between Seminal Plasma Lactoferrin and Gonadal Function in Horses

Cited by 14 publications

References 17 publications

Lactotransferrin in Asian Elephant (Elephas maximus) Seminal Plasma Correlates with Semen Quality

Lactotransferrin in Asian Elephant (Elephas maximus) Seminal Plasma Correlates with Semen Quality

Milk, caseinate and lactoferrin addition to equine semen cooling extenders

Lactoferrin increases sperm membrane functionality of frozen equine semen

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