β-Microseminoprotein/prostatic secretory protein is a member of immunoglobulin binding factor family

Kamada, Masao; Mori, Hidetoshi; Maeda, Naomi; Yamamoto, Shozo; Kunimi, Kotaro; Takikawa, Masaya; Murakami, Masahiko; Aono, Toshihiro; Futaki, Shiroh; Koide, S. S.

doi:10.1016/s0167-4838(98)00164-2

Cited by 33 publications

(29 citation statements)

References 29 publications

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“…These findings suggest that the gene may be regulated by hormones (Nolet et al 1991, Ochiai et al 1995 as also reported in rat lateral prostate (Kwong et al 2000). Although putative biological/clinical roles have been suggested, i.e., acting as an immunoglobulin binding factor (Kamada et al 1998) and/or tumor marker for prostate cancer (Sakai et al 1999), the biological function of MSMB in the male or female reproductive tract is still unknown.…”

supporting

confidence: 62%

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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supporting

confidence: 62%

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

Franchi

Avendaño²,

Molina³

et al. 2008

Reproduction

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“…The apparent pI 5.6 and M r 13 000 determined are comparable to the theoretical values of 5.4 and 11 000. The functional role of IgBF is unclear, but because it binds to immunoglobulins and suppresses B-cell activation it may act as a modulator of local immune responses [25]. The protein has mostly been studied from seminal plasma but has also been demonstrated in human BALF [26].…”

Section: Immunoglobulin Binding Factor (Igbf)mentioning

confidence: 99%

Newly identified proteins in human nasal and bronchoalveolar lavage fluids: Potential biomedical and clinical applications

1999

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Protein patterns of nasal lavage fluid (NLF) and bronchoalveolar lavage fluid (BALF) were analyzed with two-dimensional gel electrophoresis (2-DE) and a number of previously unidentified proteins (lipocalin-1, cystatin S, transthyretin, immunoglobulin binding factor and an 11 kDa fragment of albumin) were identified by N-terminal amino acid sequencing. Lipocalin-1 was shown to be a dominant protein in NLF from healthy subjects but was almost undetectable in NLF from a patient with asthma. It further appeared that lipocalin-1 in NLF consists of eight forms with pIs between 5.2 and 5.5: three with the expected M r of 17 500, two with increased M r (18 000), and three truncated variants with M r of 17 000. Two forms of cystatin S were identified both in NLF and BALF: one with pI 5.1 and M r 13 000, and the other with pI 4.9 and M r 13 500. The distribution of the two forms was clearly different in NLF and BALF from healthy subjects with the 4.9/13 500 form constituting only about 13% in NLF but 69% in BALF. In NLF from subjects with upper airway irritation a twofold increased proportion of the 4.9/ 13 500 form was detected. Amino acid sequence data and the spot position indicate that the 4.9/13 500 form might be a phosphorylated variant of cystatin S. Lower levels of both forms of cystatin S were found in BALF from smokers than nonsmokers. The levels of transthyretin in NLF were decreased in subjects exposed to irritating chemicals. Finally, higher levels of IgBF were found in BALF from smokers than nonsmokers. Taken together, these results illustrate the potential biomedical and clinical applications of identifying proteins in 2-DE patterns of human BALF and NLF. The possibility to describe and monitor airway disorders at the molecular level is inferred.

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“…This ¢nding suggests that MSPs have undergone a rapid and unusual evolution. Although the putative biological roles, such as immunoglobulin binding factor [9] and tumor marker for gastric carcinoid disease [10], have been suggested for some MSPs, the biological functions that MSPs possess are still poorly understood. In addition, their sequences bear no signi¢cant resemblance to proteins of known function, making it di⁄cult to speculate about their biological functions.…”

Section: Introductionmentioning

confidence: 99%

Disulfide pairings and secondary structure of porcine β‐microseminoprotein

Wang

et al. 2003

FEBS Letters

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A sperm motility inhibitor isolated from porcine seminal plasma is identical to porcine L L-microseminoprotein (MSP). Circular dichroism (CD) and nuclear magnetic resonance (NMR) data showed that the native and recombinant porcine MSPs exhibit very similar structure. The ¢ve disul¢de pairings on porcine MSP were unambiguously assigned based on NMR data and further con¢rmed using structural calculations. Surprisingly, our derived pairings di¡er from those recently reported for ostrich MSP based on matrix-assisted laser desorption ionization-time of £ight (MALDI-TOF) analysis. Furthermore, the secondary structure was determined to comprise one four-stranded and two double-stranded antiparallel L L-sheets. As we know, this is the ¢rst detailed secondary structure reported among several types of MSPs. ß

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β-Microseminoprotein/prostatic secretory protein is a member of immunoglobulin binding factor family

Cited by 33 publications

References 29 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

Newly identified proteins in human nasal and bronchoalveolar lavage fluids: Potential biomedical and clinical applications

Disulfide pairings and secondary structure of porcine β‐microseminoprotein

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