Direct evidence for the secretion of lactoferrin and its binding to sperm in the porcine epididymis

Jin, Yin‐Zhe; Bannai, Shiro; Dacheux, Françoise; Dacheux, Jean‐Louis; Okamura, Naomichi

doi:10.1002/(sici)1098-2795(199708)47:4<490::aid-mrd16>3.3.co;2-a

Cited by 27 publications

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“…Although lactoferrin identified in boar seminal plasma has not been biochemically characterized [15], it was recently found that lactoferrin is first secreted as a 75-kDa glycoprotein and its carbohydrate moieties are gradually digested to form a 70-kDa protein in the porcine cauda epididymis [10]. Lactoferrin purified in the present study was highly iron-saturated.…”

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confidence: 57%

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Purification and Quantification of Lactoferrin in Equine Seminal Plasma.

et al. 2002

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ABSTRACT. Lactoferrin with a molecular mass of 80 kDa was purified from equine seminal plasma by heparin-Agarose affinity chromatography and Sephacryl S-200 gel filtration. Purified lactoferrin was found to be highly homogeneous on the bases of its migration as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and of the monospecificity of rabbit antibodies to the purified protein in immunoblotting of seminal plasma proteins. A sandwich enzyme-linked immunosorbent assay was developed for quantifying lactoferrin in equine seminal plasma. Seminal plasma lactoferrin concentrations in 23 normal stallions ranged from 42 to 453 µg/ml, with a mean value of 157 ± 118 µg/ml (S.D.).

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confidence: 57%

“…Lactoferrin is present in the seminal plasma of humans and boars at a level ranging from 0.1 to 1.0 mg/ ml [5,13,15], and is identified as a sperm-binding protein [8,10]. The physiological role of seminal lactoferrin remains unclear.…”

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confidence: 99%

Purification and Quantification of Lactoferrin in Equine Seminal Plasma.

et al. 2002

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“…GPX5, thioredoxin peroxidase, glutathione S-transferase P, thioredoxin peroxidase and superoxide dismutase), to the presence of powerful protease inhibitors (e.g. macroglobulin, α-1-antitrypsin, eppin, cystatin; review in Dacheux et al, 2009) and also to the presence of several antimicrobially active compounds, such as lactoferrin (Jin et al, 1997) and several β-defensins (Hall et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Fertility of undiluted ram epididymal spermatozoa stored for several days at 4°C

Abella

Costa

Guérin

et al. 2015

Animal

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In vitro preservation of the male gamete is a challenge in the development of artificial insemination techniques for domestic animals. Specific strategies and diluents have been developed for the preservation of the fertilizing ability of the semen for each species. However, the epididymal medium has been demonstrated to be the best sperm environment to maintain sperm viability over several days and weeks for mammals. The aims of this study were to evaluate the motility and in vivo fertility of ram epididymal spermatozoa when the semen was stored for up to 4 days at 4°C undiluted in epididymal plasma. The study was undertaken with two ovine breeds (Ile de France and Corriedale). The motility of epididymal spermatozoa was better preserved in the undiluted epididymal fluid than when epididymal spermatozoa were diluted in classic ovine extender such as skim milk. During storage, the decrease in the percentage of motile sperm was lower if the epididymal spermatozoa were collected immediately after epididymal sampling than 24 h after castration or animal death. The fertility obtained after cryopreservation of the stored sperm and subsequent intrauterine insemination ranged from 55% to 24% following 24 to 96-h sperm storage. There was a linear regression relationship between fertility and the number of motile sperm inseminated for both breeds. These results show that it is possible to keep epididymal sperm motile and fertile for several days without dilution. Such a method of sperm preservation could be a final possibility for animals of high genetic value or for endangered species when the collection of semen before death of the animal is not possible.

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“…Lactoferrin sequesters ionic iron (Nozaki et al, 2003) and adsorbs sperm during epididymal transit (Jin et al, 1997) and ejaculation (Thaler et al, 1990), when it also has antimicrobial effect. Seminal albumin, in turn, binds to lipid peroxides, contributing to sperm protection (Alvarez and Storey, 1983), and presents a positive correlation with the percentage of normal sperm in bovine semen (Elzanaty et al, 2007).…”

Section: Proteins Involved In Sperm Protectionmentioning

confidence: 99%

Functional aspects of seminal plasma and sperm proteins and their potential as molecularmarkers of fertility

Moura

Memili

2016

Anim Reprod

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Molecular components of sperm and in the media surrounding them influence bull fertility. Given this concept, proteins of the seminal plasma modulate crucial functions and events of reproduction, such as sperm motility and capacitation, cell protection, acrosome reaction, fertilization and embryonic development. Sperm proteins are also important for successful fertilization, egg activation and embryo development. Empirical associations between seminal and sperm proteins and fertility in the bovine indicate that these proteins are potential molecular markers of the male reproductive status.

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Direct evidence for the secretion of lactoferrin and its binding to sperm in the porcine epididymis

Cited by 27 publications

References 0 publications

Purification and Quantification of Lactoferrin in Equine Seminal Plasma.

Purification and Quantification of Lactoferrin in Equine Seminal Plasma.

Fertility of undiluted ram epididymal spermatozoa stored for several days at 4°C

Functional aspects of seminal plasma and sperm proteins and their potential as molecularmarkers of fertility

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