A New Proteinaceous Factor Participating in the Rat Ejaculate Coagulation—Identification, Isolation and Function1

Schön, E; Lukač, Josip; Milković, S.

doi:10.1095/biolreprod26.5.875

Cited by 4 publications

(3 citation statements)

References 13 publications

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“…Care was taken to avoid 890 contamination with either blood or coagulating gland secretions, as these rapidly catalyze the precipitation of proteins within the SV fluid [40]. The glands were removed individually and the fluid contents were allowed to drip out and/or were manually expressed into microcentrifuge tubes.…”

Section: Mouse Seminal Vesicle Fluid Collection and Incubationmentioning

confidence: 99%

Visualization of GM1 with Cholera Toxin B in Live Epididymal Versus Ejaculated Bull, Mouse, and Human Spermatozoa1

Buttke¹,

Nelson²,

Hunnicutt³

et al. 2006

Biology of Reproduction

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The organization of membrane subdomains in mammalian sperm has recently generated controversy, with several reports describing widely differing localization patterns for the ganglioside GM1. Using the pentameric B subunit of cholera toxin (CTB), we found GM1 to be restricted to the plasma membrane overlying the acrosome in the heads of live murine sperm. Interestingly, CTB had minimal binding to live bovine and human sperm. To investigate whether this difference in GM1 localization was because of species differences or differences between collection from the epididymis (mouse) or an ejaculate (bull, human), we examined epididymal bovine and human sperm. We found that GM1 localized to the plasma membrane overlying the acrosome in sperm from these species. To determine whether some component of seminal plasma was interfering with the ability of CTB to access GM1, we incubated epididymal mouse sperm with fluid from murine seminal vesicles and epididymal bull sperm with bovine seminal plasma. This treatment largely abolished the ability of the CTB to bind to GM1, producing a fluorescence pattern similar to that reported for the human. The most abundant seminal plasma protein, PDC-109, was not responsible for this loss. As demonstration that the seminal plasma was not removing GM1, sperm exposed to seminal plasma were fixed before CTB addition, and again displayed fluorescence over the acrosome. These observations reconcile inconsistencies reported for the localization of GM1 in sperm of different species, and provide evidence for the segregation of GM1 to a stable subdomain in the plasma membrane overlying the acrosome.

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Section: Mouse Seminal Vesicle Fluid Collection and Incubationmentioning

confidence: 99%

Visualization of GM1 with Cholera Toxin B in Live Epididymal Versus Ejaculated Bull, Mouse, and Human Spermatozoa1

Buttke¹,

Nelson²,

Hunnicutt³

et al. 2006

Biology of Reproduction

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“…Differential protein profiles expression was observed in dromedary seminal plasma [ 7 ]. The process of coagulation and liquefaction has been studied in the rat [ 8 , 9 ], guinea pig [ 10 ], and human [ 11 – 16 ]. Following ejaculation in the human, a soft clot is formed that then dissolves over 5–20 min [ 17 ].…”

Section: Introductionmentioning

confidence: 99%

Studies on Liquefaction Time and Proteins Involved in the Improvement of Seminal Characteristics in Dromedary Camels (Camelus dromedarius)

et al. 2016

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Semen was collected from six dromedary camels using artificial vagina during rutting season. Liquefaction of the viscous semen occurred in 23.89 ± 1.49 h. During liquefaction, proteins with molecular masses of 24.55 kDa and 22.07 kDa appeared in conjunction with the disappearance of intact 26.00 kDa protein after 18–24 h. These proteins were identified as β-nerve growth factors (β-NGFs) in liquefied camel semen. Guanidine-HCL improves the rheological characteristics of dromedary camel semen along with significant (P < 0.01) increase in sperm motility. No significant differences were found in viability of spermatozoa indicating no visible detrimental effects on spermatozoa. The cause of semen viscosity, as well as proteins that are present in liquefied dromedary camel seminal plasma, is described for the first time.

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“…Evidences have been presented that coagulum formation in these species is caused by the enzyme transglutaminase secreted from coagulating gland (anterior prostate) forming E(yglutamy1)lysine cross-bridges between basic vesicular secretion protein precursors (Williams-Ashman et al -1972;1977;1980). Schon et al (1982) presented the evidence for a protein of molecular weight estimated at 163K necessary for the in vitro coagulation of rat seminal vesicle proteins. Essentially nothing is known about the coagulation process in man except for a recent report on the role of fructose in the coagulation of human semen (Montagnon et al -1982).…”

Section: Introductionmentioning

confidence: 99%

Molecular Structure of Human Seminal Coagulum: The Role of Disulfide Bonds

Chaistitvanich

Boonsaeng

2009

Andrologia

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A New Proteinaceous Factor Participating in the Rat Ejaculate Coagulation—Identification, Isolation and Function1

Cited by 4 publications

References 13 publications

Visualization of GM1 with Cholera Toxin B in Live Epididymal Versus Ejaculated Bull, Mouse, and Human Spermatozoa1

Visualization of GM1 with Cholera Toxin B in Live Epididymal Versus Ejaculated Bull, Mouse, and Human Spermatozoa1

Studies on Liquefaction Time and Proteins Involved in the Improvement of Seminal Characteristics in Dromedary Camels (Camelus dromedarius)

Molecular Structure of Human Seminal Coagulum: The Role of Disulfide Bonds

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