Novel sperm-binding proteins of epididymal origin contain four fibronectin type II-modules

Saalmann, A.; Münz, Sibylle; Ellerbrock, K.; Ivell, Richard; Kirchhoff, Christiane

doi:10.1002/1098-2795(200101)58:1<88::aid-mrd12>3.0.co;2-d

Cited by 47 publications

(49 citation statements)

References 30 publications

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“…BSP1 Fn2 domains are single binding sites for either choline phospholipids or heparin . Although of epididymal origin (Saalmann et al 2001), ELSPBP1 is a four-Fn2 domain-containing protein, which suggests biochemical properties similar to those of BSPs. Its affinity for choline phospholipids has been established, and sequence alignment reveals that the key amino acid residues involved in choline phospholipids binding are highly conserved (Ekhlasi-Hundrieser et al 2007).…”

Section: Proteomic Comparison Of Sperm Proteins From Bullsmentioning

confidence: 98%

“…Membranes were blocked for 1 h in PBS 0.1% Tween-20 (PBS-T) containing 5% (w/v) defatted milk. Membranes were incubated with 1/500 rabbit anti-CE12-3 (ELSPBP1; generously provided by C Kirchhoff from the Institute for Hormone and Fertility Research, Hamburg, Germany (Saalmann et al 2001)), 1/5000 anti-BSP-A1/A2 (BSP1; generously provided by Dr P Manjunath from Université de Montréal, Montréal, Canada (Sigma) was used as the housekeeping protein. Membranes were then incubated with HRP-conjugated goat anti-rabbit, rabbit anti-goat or goat anti-mouse IgG (dilution 1/5000) in 5% (w/v) defatted milk in PBS-T for 1 h at room temperature.…”

Section: One-dimensional Gel Electrophoresis and Western Blot Analysismentioning

confidence: 99%

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Proteomic comparison of detergent-extracted sperm proteins from bulls with different fertility indexes

D’Amours

Frenette²,

Fortier³

et al. 2010

Reproduction

147

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Intrinsic factors such as proteins modulate the fertilising ability of male gametes. We compared detergent-extracted sperm protein composition of bulls with different fertility indexes in order to highlight putative fertility markers of sperm. Frozen semen from 23 Holstein bulls with documented fertility was used. According to their 'fertility solution' (SOL), as calculated by the Canadian dairy network, bulls were divided into four groups: high fertility (HF) (SOLO3.0; nZ6), medium-HF (2.9OSOLO2.0; nZ5), medium-low fertility (K2.8OSOLOK4.9; nZ8) and low fertility (LF; SOL!K5.0; nZ4), with a SOLZ0 being the average. Triton X-100 protein extracts from ejaculated spermatozoa were subjected to two-dimensional difference gel electrophoresis, and polypeptide maps were quantitatively analysed by ImageMaster software. Nine protein spots showed significant differences between the HF and LF groups, and eight of these proteins were identified by liquid chromatography-tandem mass spectrometry. T-complex protein 1 subunits 3 and q (CCT5 and CCT8), two isoforms of epididymal sperm-binding protein E12 (ELSPBP1), proteasome subunit a type-6 and binder of sperm 1 (BSP1) were more expressed in the LF group than in the HF group. On the other hand, adenylate kinase isoenzyme 1 (AK1) and phosphatidylethanolamine-binding protein 1 (PEBP1) were more expressed in the HF group than in the LF group. The presence and expression level of ELSPBP1, BSP1, AK1 and PEBP1 were confirmed by western blot. A linear regression model established that CCT5 and AK1 explained 64% (P!0.001) of the fertility scores. The reported functions of these proteins are in agreement with a putative involvement in defective sperm physiology, where lower or higher levels can jeopardise sperm ability to reach and fertilise the oocyte.

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Section: Proteomic Comparison Of Sperm Proteins From Bullsmentioning

confidence: 98%

Section: One-dimensional Gel Electrophoresis and Western Blot Analysismentioning

confidence: 99%

Proteomic comparison of detergent-extracted sperm proteins from bulls with different fertility indexes

D’Amours

Frenette²,

Fortier³

et al. 2010

Reproduction

147

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“…Human epididymal studies mirror the rodent work and confirm functional changes in epididymal spermatozoa (16) and specific proteins at the RNA and protein levels. The construction of human epididymal cDNA libraries from prostatic cancer patients led to the discovery of up to 12 human epididymal genes (17) that encode sperm-binding proteins with different functions (18). Dacheux et al (19) performed two-dimensional gel analyses to characterize the human epididymal secretome and epididymosomes have been shown to transfer human epididymal proteins to spermatozoa (20).…”

mentioning

confidence: 99%

Systematic Mapping and Functional Analysis of a Family of Human Epididymal Secretory Sperm-Located Proteins

Liu

Wang

et al. 2010

Molecular & Cellular Proteomics

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The mammalian spermatozoon has many cellular compartments, such as head and tail, permitting it to interact with the female reproductive tract and fertilize the egg. It acquires this fertilizing potential during transit through the epididymis, which secretes proteins that coat different sperm domains. Optimal levels of these proteins provide the spermatozoon with its ability to move to, bind to, fuse with, and penetrate the egg; otherwise male infertility results. As few human epididymal proteins have been characterized, this work was performed to generate a database of human epididymal sperm-located proteins involved in maturation. Two-dimensional gel electrophoresis of epididymal tissue and luminal fluid proteins, followed by identification using MALDI-TOF/MS or MALDI-TOF/TOF, revealed over a thousand spots in gels comprising 745 abundant nonstructural proteins, 408 in luminal fluids, of which 207 were present on spermatozoa. Antibodies raised to 619 recombinant or synthetic peptides, used in Western blots, histological sections, and washed sperm preparations to confirm antibody quality and protein expression, indicated their regional location in the epididymal epithelium and highly specific locations on washed functional spermatozoa. Sperm function tests suggested the role of some proteins in motility and protection against oxidative attack. A large database of these proteins, characterized by size, pI, chromosomal location, and function, was given a unified terminology reflecting their sperm domain location. These novel, secreted human epididymal proteins are potential targets for a posttesticular contraceptive acting to provide rapid, reversible, functional sterility in men and they are also biomarkers that could be used in noninvasive assessments of male fertility. Molecular & Cellular Proteomics 9:2517-2528, 2010.There are two major challenges for population and reproductive health. First, rapid global population expansion, which will see the world population reach 9 billion by 2045 (http:// www.census.gov/ipc/www/idb/worldpopgraph.php). Second, infertility is suffered by around 180 million couples, comprising about 10%-15% worldwide and over 25% in some countries, of which 40%-50% is related to the male (http://www.who.int/ reproductivehealth/publications/infertility/progress_63/en/ index.html). Natural fertilization requires tightly coordinated and sequential sperm functions (1), from maturation in the epididymis (2) and survival in the female tract to fusion with the ovum (3). Fertility and infertility are both sides of the same reproductive coin so that understanding one can provide clues to the other. On the one hand, the widespread application to infertile couples of artificial reproductive technology, which bypasses natural fertilization mechanisms, has diverted attention from understanding the biological causes of the infertility for its cure, to that of overcoming the symptom of childlessness. On the other, controlling population growth by contraceptive means is currently only available to large ...

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“…NPC2 in the bovine seminal plasma acts as a membrane reorganization factor in a capacitation-independent process [22]. The epididymal sperm-binding protein 1 (ELSPBP1) is having highly regionalised expression in the epididymis [63]. Their distinct spatial expression patterns along the epididymal duct suggest that ELSPBP1 may have a role in sperm maturation [65].…”

Section: Some Others Seminal Plasma Proteinsmentioning

confidence: 99%

Seminal Plasma Proteome: Promising Biomarkers for Bull Fertility

Kumar

Singh

et al. 2012

Agric Res

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The seminal plasma is a mixture of secretions from the testis, epididymis and male accessory sex glands. A number of seminal plasma proteins are associated with male fertility but most of these have not been studied in detail till now. Recently, proteomics has been used to show the differences in proteins profile in seminal plasma from high and low fertility bulls. For example, osteopontin, phospholipase A2, P25b, acidic seminal fluid proteins, a-L-fucosidase and cathepsin D are positively correlated with fertility of bulls and may act as useful fertility marker (s), while lipocalin-type prostaglandin D synthase, spermadhesin Z13, clusterin and ubiquitin are negatively correlated with fertility in bulls. Bovine seminal plasma proteins in seminal plasma act like a double-edged sword and showed a quadratic association with bull fertility. The physiological roles of the metalloproteinase-2 (TIMP-2), ecto-ADP-ribosyltransferase 5, nuclobindin, Niemann-Pick C2 and epididymal sperm-binding protein 1 and their relationship to bull fertility need further studies. This review summarizes the physiological functions of proteins of seminal plasma and their relation to bull fertility.

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Novel sperm-binding proteins of epididymal origin contain four fibronectin type II-modules

Cited by 47 publications

References 30 publications

Proteomic comparison of detergent-extracted sperm proteins from bulls with different fertility indexes

Proteomic comparison of detergent-extracted sperm proteins from bulls with different fertility indexes

Systematic Mapping and Functional Analysis of a Family of Human Epididymal Secretory Sperm-Located Proteins

Seminal Plasma Proteome: Promising Biomarkers for Bull Fertility

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