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Gene Review:

BSP3 - binder of sperm 3

Bos taurus

Manjunath, P. et al., Seidah, N.G. et al., Gwathmey, T.M. et al., Manjunath, P. et al., Manjunath, P. et al., et al.

Calvete, Raida, Gentzel, Urbanke, Sanz, Töpfer-Petersen,

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High impact information on SVS8

Bovine seminal plasma (BSP) contains a family of four closely related proteins previously designated as BSP-A1, BSP-A2, BSP-A3, and BSP-30-kDa (collectively called BSP proteins) [1].
This domain also occurs in the major bovine seminal plasma heparin-binding proteins PDC-109 (BSP-A1/A2) and BSP-A3 [2].
We have recently shown that the major proteins of bovine seminal plasma, namely BSP-A1, BSP-A2, BSP-A3 and BSP-30-kDa (collectively called BSP proteins) bind to spermatozoa and that the binding sites on the plasma membrane of spermatozoa are choline phospholipids [3].
The collagen-binding domain of bovine fibronectin (type II sequence) was also found to be highly homologous to both BSP-A3 and PDC-109 [4].
BSP-A1 and BSP-A2 are glycoproteins containing galactosamine, sialic acid and neutral sugars, but BSP-A3 did not contain any covalently attached sugars [5].

Biological context of SVS8

Complete amino acid sequence of BSP-A3 from bovine seminal plasma. Homology to PDC-109 and to the collagen-binding domain of fibronectin [4].
Genome mapping of the bovine seminal plasma A3 gene (BSPA3 ) [6].
In cattle, the major proteins of (bovine)seminal plasma (BSP proteins: BSP-A1/A2, BSP-A3, and BSP-30-kDa) potentiate sperm capacitation induced by high-density lipoprotein (HDL) [7].

Anatomical context of SVS8

Bovine seminal plasma was shown to contain three similar proteins, called BSP-A1, BSP-A2 and BSP-A3 [4].
Bovine seminal vesicles synthesize a family of closely related proteins, namely BSP-A1, BSP-A2, BSP-A3, and BSP-30-kDa (collectively called BSP proteins) [8].
BSP-A3 and BSP-30-kDa each increased binding of epididymal sperm to epithelium and were as effective as PDC-109 in competitively inhibiting binding of ejaculated sperm [9].
Bovine Seminal Plasma Proteins PDC-109, BSP-A3, and BSP-30-kDa Share Functional Roles in Storing Sperm in the Oviduct [9].
Alcohol precipitates of bovine seminal plasma (designated crude BSP, cBSP), purified BSP-A1/-A2, BSP-A3 and BSP-30-kDa proteins stimulated cellular cholesterol and choline phospholipid efflux from fibroblasts [10].

Associations of SVS8 with chemical compounds

Complementary deoxyribonucleic acid cloning and tissue expression of BSP-A3 and BSP-30-kDa: phosphatidylcholine and heparin-binding proteins of bovine seminal plasma [11].
Horse seminal plasma proteins HSP-1 and HSP-2, and boar protein pB1, belong to the same family as the bull heparin- and phosphorylcholine-binding proteins BSP-A1/2, BSP-A3, and BSP-30K [12].
Whereas BSP-A2 and BSP-A3 were eluted unadsorbed, BSP-A1 bound to wheat-germ lectin-Sepharose 6MB and could be eluted by the competing sugar N-acetyl-D-glucosamine [5].
The major proteins of bull seminal plasma (BSP proteins: BSP-A1/A2, BSP-A3, and BSP-30-kDa) bind to sperm surface at ejaculation and stimulate cholesterol and phospholipid efflux from the sperm membrane [13].

Other interactions of SVS8

The first is between PDC-109 and BSP-A3, which is so high that we can confidently predict that both proteins evolved from a single ancestral gene [4].

Analytical, diagnostic and therapeutic context of SVS8

Bovine seminal plasma contains four similar acidic proteins, previously designated as BSP (bovine seminal plasma)-A1, BSP-A2, BSP-A3, and BSP-30-kDa, that when added to pituitary cell cultures result in the immediate secretion of gonadotropins (follitropin and lutropin) [14].
Three major acidic proteins of bovine seminal plasma, BSP-A1, BSP-A2 and BSP-A3, were purified to homogeneity, by employing fast protein liquid chromatography, gel filtration and h.p.l.c. The proteins were purified on the basis of their stimulatory effect on the basal release of gonadotropins by rat anterior-pituitary cells in culture [5].
Immunoblotting revealed that BiSV-16kDa cross-reacted with BSP-A3 antibodies, BiSV-17kDa and BiSV-18kDa cross-reacted with BSP-A1/-A2 antibodies, and BiSV-28kDa cross-reacted with BSP-30kDa antibodies [15].
Radioimmunoassays for bull seminal plasma proteins (BSP-A1/-A2, BSP-A3, and BSP-30-Kilodaltons), and their quantification in seminal plasma and sperm [16].
N-Terminal sequence analysis of these proteins identified a boar counterpart of the bovine capacitation factors BSP-A1/2 (also called PDC-109) and BSP-A3 [17].

References

Major proteins of bovine seminal fluid bind to insulin-like growth factor-II. Desnoyers, L., Manjunath, P. J. Biol. Chem. (1994) [Pubmed]
Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: effect of glycosylation on its heparin- and gelatin-binding capabilities. Calvete, J.J., Mann, K., Schäfer, W., Sanz, L., Reinert, M., Nessau, S., Raida, M., Töpfer-Petersen, E. Biochem. J. (1995) [Pubmed]
Major proteins of bovine seminal plasma inhibit phospholipase A2. Manjunath, P., Soubeyrand, S., Chandonnet, L., Roberts, K.D. Biochem. J. (1994) [Pubmed]
Complete amino acid sequence of BSP-A3 from bovine seminal plasma. Homology to PDC-109 and to the collagen-binding domain of fibronectin. Seidah, N.G., Manjunath, P., Rochemont, J., Sairam, M.R., Chrétien, M. Biochem. J. (1987) [Pubmed]
Purification and biochemical characterization of three major acidic proteins (BSP-A1, BSP-A2 and BSP-A3) from bovine seminal plasma. Manjunath, P., Sairam, M.R. Biochem. J. (1987) [Pubmed]
Genome mapping of the bovine seminal plasma A3 gene (BSPA3 ). Roncoleta, M., Kata, S.R., Womack, J.E., Amaral, M.E. Anim. Genet. (2002) [Pubmed]
Bovine seminal plasma phospholipid-binding proteins stimulate phospholipid efflux from epididymal sperm. Thérien, I., Moreau, R., Manjunath, P. Biol. Reprod. (1999) [Pubmed]
Major proteins of bovine seminal vesicles bind to spermatozoa. Manjunath, P., Chandonnet, L., Leblond, E., Desnoyers, L. Biol. Reprod. (1994) [Pubmed]
Bovine Seminal Plasma Proteins PDC-109, BSP-A3, and BSP-30-kDa Share Functional Roles in Storing Sperm in the Oviduct. Gwathmey, T.M., Ignotz, G.G., Mueller, J.L., Manjunath, P., Suarez, S.S. Biol. Reprod. (2006) [Pubmed]
Seminal plasma choline phospholipid-binding proteins stimulate cellular cholesterol and phospholipid efflux. Moreau, R., Frank, P.G., Perreault, C., Marcel, Y.L., Manjunath, P. Biochim. Biophys. Acta (1999) [Pubmed]
Complementary deoxyribonucleic acid cloning and tissue expression of BSP-A3 and BSP-30-kDa: phosphatidylcholine and heparin-binding proteins of bovine seminal plasma. Salois, D., Ménard, M., Paquette, Y., Manjunath, P. Biol. Reprod. (1999) [Pubmed]
Isolation and characterization of heparin- and phosphorylcholine-binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1. Calvete, J.J., Raida, M., Gentzel, M., Urbanke, C., Sanz, L., Töpfer-Petersen, E. FEBS Lett. (1997) [Pubmed]
Low-density lipoprotein fraction from hen's egg yolk decreases the binding of the major proteins of bovine seminal plasma to sperm and prevents lipid efflux from the sperm membrane. Bergeron, A., Crête, M.H., Brindle, Y., Manjunath, P. Biol. Reprod. (2004) [Pubmed]
Apolipoprotein A-I binds to a family of bovine seminal plasma proteins. Manjunath, P., Marcel, Y.L., Uma, J., Seidah, N.G., Chrétien, M., Chapdelaine, A. J. Biol. Chem. (1989) [Pubmed]
Isolation and characterization of gelatin-binding bison seminal vesicle secretory proteins. Boisvert, M., Bergeron, A., Lazure, C., Manjunath, P. Biol. Reprod. (2004) [Pubmed]
Radioimmunoassays for bull seminal plasma proteins (BSP-A1/-A2, BSP-A3, and BSP-30-Kilodaltons), and their quantification in seminal plasma and sperm. Nauc, V., Manjunath, P. Biol. Reprod. (2000) [Pubmed]
Isolation and biochemical characterization of heparin-binding proteins from boar seminal plasma: a dual role for spermadhesins in fertilization. Sanz, L., Calvete, J.J., Mann, K., Gabius, H.J., Töpfer-Petersen, E. Mol. Reprod. Dev. (1993) [Pubmed]

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