Isolation and characterization of the major proteins of ram seminal plasma

Bergeron, Annick; Villemure, Michèle; Lazure, Claude; Manjunath, Puttaswamy

doi:10.1002/mrd.20310

Cited by 114 publications

(98 citation statements)

References 48 publications

(47 reference statements)

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“…More recently (Barrios et al, 2005), we have proven that 2 proteins of approximately 14 (P14) and 20 (P20) kDa are responsible for this protective and restoring effect. By cytochemical analysis, we showed that both proteins have several binding sites on the sperm surface, and the NH 2 -terminal sequencing showed that the P14 fragment has a high homology with the bovine PDC-109 (Esch et al, 1983), GSP-14/15 kDa (goat seminal plasma protein, related to the BSP family) (Villemure et al, 2003), and the recently reported RSP15 of ram (Bergeron et al, 2005). The homology was found from amino acid 19-34 (CVFPFTYYDDRHFDCT) with 49-64 of PDC-109 (CVFPFVYRNRKHFDCT), which is the FN2 domain (Greube et al, 2001).…”

Section: Discussionmentioning

confidence: 85%

Immunohistochemical Localization of Sperm‐Preserving Proteins in the Ram Reproductive Tract

Fernández‐Juan

Gallego

Barrios

et al. 2006

Journal of Andrology

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Previously, we reported that the addition of seminal plasma proteins before cold-shock treatment prevents sperm membrane injury, and that 2 proteins of approximately 14 (P14) and 20 (P20) kDa, the main components of fraction 6 isolated by exclusion chromatography, are responsible for this protective effect. The objective of the present study was to localize P14 and P20 in tissues of the ram reproductive tract to determine their origin. Antiserum generated against purified P14 and P20 reacted with proteins in seminal vesicles and vas deferens by Western blot analyses of protein tissue extracts. However, these antisera failed to detect P14 and P20 in testis, prostate, efferent ductules, bulbourethral glands, and epididymis (caput, corpus, and cauda). Immunohistochemical analyses by both indirect immunofluorescence and the avidin-biotin complex technique confirmed that only seminal vesicles showed reactivity, restricted to the secretory cells, with both antibodies. Obtained results indicate that P14 and P20 are secreted specifically in the seminal vesicles. To further confirm that P14 and P20 are specifically expressed in seminal vesicles, we used Northern blot analyses to investigate the expression of both proteins in seminal vesicles and vas deferens. These assays corroborated again that P14 and P20 were specifically expressed in seminal vesicles. Consequently, we suggest referring to these 2 proteins as RSVP14 and RSVP20, respectively, according to their origin and molecular weight.

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Section: Discussionmentioning

confidence: 85%

Immunohistochemical Localization of Sperm‐Preserving Proteins in the Ram Reproductive Tract

Fernández‐Juan

Gallego

Barrios

et al. 2006

Journal of Andrology

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“…In addition to main immunoreactive fragments, low but detectable and distinct FN immunoreactivity of 8-15 kDa protein bands was observed. This pattern of low molecular mass species resembles that of the acidic gelatin-binding proteins as the main proteins present in the seminal plasma of different animals [21,[35][36][37]. As already mentioned, they contain an FN-type II domain, but there are no data on their possible antigenic relatedness with FN.…”

Section: Discussionmentioning

confidence: 79%

Molecular heterogeneity of gelatin-binding proteins from human seminal plasma

Kosanović¹,

Janković²

2010

Asian J Androl

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Defining the molecular characteristics of seminal plasma proteins is essential for understanding their function in physiological and pathological conditions. Starting from the predicted importance of human seminal plasma gelatin-binding proteins, comprising fibronectin (FN) and FN-related molecules, for male fertility, this study aims at gaining insight into their immuno-glycobiochemical properties. Human seminal plasma from subjects with normal semen parameters were separated on a gelatin-Sepharose column and analyzed by sodium dodecyl sulfatepolyacrylamide gel electrophoresis and immunoblotting using antibodies against distinct FN forms. Heterogeneity of the isolated molecular species was examined by protein chip arrays combined with surface-enhanced laser desorption/ionization time of flight mass spectrometry, on normal, metal and hydrophobic surfaces. Carbohydrate composition was investigated using mannose-, fucose-and sialic acid-specific plant lectins and galectin-1. The results obtained indicated a pattern of isolated proteins corresponding to that of known FN fragments, as confirmed by immunoreactivity. Among them heparin-binding ability was preferentially associated with low molecular mass species. As for posttranslational modifications, phosphorylation and glycosylation of distinct fragments were revealed. Lectin binding to fragments containing the gelatin-binding domain, particularly with Ricinus communis agglutinin I, was stronger than to fragments containing the cell-binding site of FN. A low level of sialylation and distinctive concanavalin A-and Lens culinaris agglutinin-reactive species were also observed. Galectin-1 did not interact with the isolated preparation. Resolving the molecular heterogeneity of normal human seminal plasma FN and gaining initial insight into possible similarities/differences with known FN molecular species may be considered a prerequisite step preceding challenging the clinical usefulness of these molecular properties.

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“…Our results mainly focusing on the 8 bands that are associated with fertility in south Indian Jersey and hybrid bulls. SDS-PAGE analysis of alcohol-precipitated ram seminal proteins indicated the presence of about 25 proteins with molecular masses from 14-120 kDa, a group of proteins with a molecular mass of 15-16 kDa and 22-24 kDa was more predominant (Bergeron et al, 2005). The relative content of protein for low fertility group and high fertility group of Jersey were found to be with significant different in that fertility associated proteins.…”

Section: Resultsmentioning

confidence: 90%

Analysis of Seminal Plasma Proteins of South Indian Jersey and Hybrid Bulls and their Correlation with Semen Quality

Vickram¹,

Rajeswari²,

Pathy³

et al. 2015

Asian J. of Animal Sciences

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This is a preliminary study of the protein profiles of the semen in Jersey breed bulls. Jersey bulls were mainly used for fertility purposes; they were grouped based on the fertility, such as highly fertile group (95% fertility), medium fertile group (65-70%), low fertile group (45-50%) and hybrid bulls. Semen of 20 Jersey and hybrid bulls was collected through artificial vagina. The semen characteristics includes volume, pH value, viscosity, viability, sperm concentration, agglutination, total motility and their group, sperm morphology and Hypo-Osmotic Swelling test (HOS) were carried out immediately after collection. Total antioxidant capacity test by using catalase and cholesterol analysis were also carried out. Quantification of the amino acids and proteins were carried out by Ninhydrin and Lowry method, protein analysis by Sodium Dodecyl Sulphate (SDS) was carried out for the following categories. (1) Highly fertile group (Jersey), (2) Medium fertile group (Jersey), (3) Low fertile group (Jersey) and (4) Hybrid group. Analysis of semen protein reveals about seventeen protein bands of sizes ranging between 14 and 205 kDa were identified. Among those proteins bands, the relative protein content of nine bands shows significantly different from each group. The rest of the proteins bands seem to have some positive and/or negative correlation on the semen characterizes or fertility. The antioxidant capacity of highly fertile and hybrid group was very high compare to low fertile group of Jersey. This study clearly indicates the bull seminal plasma proteins are associated with fertility and as well as determination of semen quality and ultimately decides the fertility.Key words: Semen, seminal plasma, jersey bulls, catalase, antioxidants, ninhydrin test INTRODUCTIONSemen consists of mature spermatozoon and swims in a highly complex features seminal fluid. Seminal fluid contains a complex mixture of organic compounds secreted from epididymis, testes and other accessory sex glands, influences sperm morphology, motility, sperm concentration acrosome reaction and fertility (Mann and Lutwak-Mann, 1981). Biochemical analysis of seminal fluid reveals that it is composed of amino acids, proteins and polypeptides. These molecules of seminal plasma determines semen quality and fertility were different in different species, some are reported to be associated with the fertility. Good quality semen is the most important factor to implement breeding programs (Stradaioli et al., 2004).The presence of proteins, lipids and hormones in seminal plasma suggests that a large part of the physiological functions of this fluid are not yet ascertained. It is a fact that components especially, high levels of fructose and zinc are not present in other body fluids. Effective semen

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Isolation and characterization of the major proteins of ram seminal plasma

Cited by 114 publications

References 48 publications

Immunohistochemical Localization of Sperm‐Preserving Proteins in the Ram Reproductive Tract

Immunohistochemical Localization of Sperm‐Preserving Proteins in the Ram Reproductive Tract

Molecular heterogeneity of gelatin-binding proteins from human seminal plasma

Analysis of Seminal Plasma Proteins of South Indian Jersey and Hybrid Bulls and their Correlation with Semen Quality

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