Novel Solution Structure of Porcine β-Microseminoprotein

Wang, Iren; Lou, Yuan‐Chao; Wu, Kuen‐Phon; Wu, Shih Hsiung; Chang, Wen Chang; Chen, Chinpan

doi:10.1016/j.jmb.2004.12.029

Cited by 11 publications

(17 citation statements)

References 43 publications

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“…From the sitespecific MSMB localization on the sperm membrane observed by immunofluorescence and electron microscopy in our study, and in accordance with the suggestion of a previous publication (Wang et al 2005), we speculate that an integral protein on the sperm plasma membrane may act as MSMB receptor.…”

Section: Discussionsupporting

confidence: 93%

“…Previous studies on pig MSMB that shares 51% identity sequence with the human protein has shown a compact structure and rapid evolution. These results led the authors to conclude that direct hydrophobic interaction with the membrane is unlikely to occur suggesting that MSMB might be a peripheral protein that binds to membrane integral proteins (Wang et al 2005).…”

Section: Discussionmentioning

confidence: 99%

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β-Microseminoprotein in human spermatozoa and its potential role in male fertility

Franchi

Avendaño²,

Molina³

et al. 2008

Reproduction

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Abstractb-Microseminoprotein (MSMB) is one of the most abundant proteins in human seminal plasma. The objectives of this study were: (1) to purify MSMB from seminal plasma (SP) and generate antibodies against the pure protein; (2) to investigate the interaction of MSMB with ejaculated spermatozoa and its possible effect on the spontaneous acrosome reaction (AR); and (3) to quantify MSMB content in SP and examine its relationship with the clinical sperm parameters. MSMB was purified from SP and its presence on the sperm surface was examined by indirect immunofluorescence using a specific polyclonal antibody. The effect of MSMB on the AR was evaluated using guinea pig epididymal spermatozoa as a model. MSMB quantification assay was performed with a two-site binding ELISA using two polyclonal antibodies against MSMB. MSMB was assessed in semen samples from fertile donors (controls) and subfertile patients according to World Health Organization criteria. MSMB was detected on the sperm surface and mainly localized to the acrosomal region of the head and neck. A significant spontaneous AR inhibition was observed when guinea pig epididymal spermatozoa were preincubated with MSMB. Finally, MSMB was significantly increased in subfertile patients when compared with fertile controls (P!0.02). The association of MSMB to the sperm surface, the inhibitor effect on the spontaneous AR and the increased MSMB levels found in SP in subfertile men suggests a relationship between this protein and semen quality and a possible role in the process of fertilization. Reproduction (2008) 136 157-166

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Section: Discussionsupporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

β-Microseminoprotein in human spermatozoa and its potential role in male fertility

Franchi

Avendaño²,

Molina³

et al. 2008

Reproduction

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“…The three-dimensional structure of porcine MSP was resolved by Wang et al (2005). On the basis of the suggested structure and physical features, the interaction of porcine MSP with the plasma membrane is likely because of the electrostatic interactions between the MSP and the integral proteins (Wang et al 2005;Franchi et al 2008).…”

Section: Discussionmentioning

confidence: 99%

“…On the basis of the suggested structure and physical features, the interaction of porcine MSP with the plasma membrane is likely because of the electrostatic interactions between the MSP and the integral proteins (Wang et al 2005;Franchi et al 2008). During ejaculation, boar spermatozoa receive a protective protein layer formed by seminal plasma components Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Human prostate MSP has been found to be identical with one component of the immunoglobulin-binding fraction (IgBF) of seminal plasma (Kamada et al 1998). The protein structure of MSP in humans and pigs has been completely resolved (Akiyama et al 1985;Fernlund et al 1994;Wang et al 2005;Ghasriani et al 2006). Additionally, MSP from the prostate of rhesus monkey (Nolet et al 1991) and rat (Kwong et al 2000) has been characterized.…”

Section: Introductionmentioning

confidence: 99%

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Reproductive tissue expression and sperm localization of porcine beta-microseminoprotein

et al. 2011

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Beta-microseminoprotein (MSP) is a predominant protein of human seminal plasma and originates from prostate secretions. MSP from boar seminal plasma has been sequenced and shows only 50%-52% homology with that of human. Porcine MSP is synthesized by the post-natal prostate gland and is identical with the sperm motility inhibitor. Although MSP is a protein characteristic of the prostate gland, we have established the presence of its mRNA transcript not only in boar prostate but also in other reproductive organ tissues. In extracts of all these organs, specific polyclonal antiMSP antibody recognizes a 12-kDa protein band identified by mass spectrometry as MSP. Immunofluorescence (IMF) has revealed the occurrence of MSP in the epithelial tissue of the prostate, epididymis, seminal vesicles and Cowper's glands. MSP has been localized on epididymal spermatozoa in the acrosomal region and on the flagellum of ejaculated spermatozoa. The absence of MSP on the surface of capacitated spermatozoa together with the antibody detection of MSP in the sperm acidic extract after in vitro capacitation indicates its acrosomal origin. Additionally, MSP has been localized by IMF in the sperm acrosome in capacitated spermatozoa with a permeabilized plasma membrane and by electron microscopy in ejaculated spermatozoa. The function of MSP in seminal plasma and spermatozoa is not fully understood. Nevertheless, the secretion of porcine MSP by various reproductive organs indicates its multiple roles in the reproductive process. For the first time in mammalian species, MSP has been localized in various physiological stages of sperm.

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Disulphide bond reduction and S-carboxamidomethylation of PSP94 affects its conformation but not the ability to bind immunoglobulin

Jagtap

Akkaladevi

Swamy

et al. 2007

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Novel Solution Structure of Porcine β-Microseminoprotein

Cited by 11 publications

References 43 publications

β-Microseminoprotein in human spermatozoa and its potential role in male fertility

β-Microseminoprotein in human spermatozoa and its potential role in male fertility

Reproductive tissue expression and sperm localization of porcine beta-microseminoprotein

Disulphide bond reduction and S-carboxamidomethylation of PSP94 affects its conformation but not the ability to bind immunoglobulin

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