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At least 19 recordsLinked to original sources
PubMed1989

Apolipoprotein A-I binds to a family of bovine seminal plasma proteins.

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). However, when calf or horse serum was included in the culture medium the secretion of gonadotropins was completely prevented. This effect was seen at levels up to 200 micrograms of BSP protein/ml while the presence of more than 200 micrograms of BSP protein/ml in the serum medium continued to release gonadotropins. This could be explained by the presence in the sera of a binding factor to the BSP proteins which prevents their action. This binding factor has been detected in all the sera tested, including human serum, in dot-blot experiments using 125I-labeled BSP-A1, -A2, -A3, or -30-kDa protein. Thus, it was of interest to isolate this binding factor from human serum by affinity chromatography on a column of BSP-A1/-A2-agarose. The purified binding factor was then identified as apolipoprotein A-I (apoA-I) by the following criteria: (a) it has a molecular mass of 27,000 daltons, (b) the amino acid composition is similar to apoA-I, (c) the first 25 residues at the amino-terminal end of this binding factor are identical to apoA-I, and (d) the binding factor cross-reacts in the radioimmunoassay of apoA-I. Furthermore, BSP proteins also bind to purified plasma apoA-I and apoA-I associated with high density lipoprotein. ApoA-I is the major protein of plasma high density lipoprotein and plays an important role in lipid transport and metabolism. Thus, the binding of bovine seminal plasma proteins to apoA-I suggests some physiological significance in lipoprotein function or vice versa.

Amino Acid Sequence↗
PubMed2003

Proteinase inhibitors in aggregated forms of boar seminal plasma proteins.

Boar seminal plasma proteins were separated by gel chromatography on Sephadex G-75 into five fractions (I-V). Serine proteinase inhibitors were found mainly in the protein fraction with relative molecular weight 5-25kDa. Small amounts of these inhibitors were also found in the high molecular weight protein fraction (M(r)>100kDa). The protein fraction containing most of the proteinase inhibitory activity was further separated by RP HPLC. Isolated proteins were characterized by SDS electrophoresis and immunoblotting, N-terminal amino acid sequencing and by determination of the proteinase inhibitory activity. In the fraction containing proteinase inhibitors, also beta-microseminoprotein (beta-MSP), AQN 1 and lactoferrin were identified. The possible existence of complexes of protein components in the fraction with relative molecular weight 5-25kDa was studied in detail using gel chromatographic separation on Sephadex G-50. A part of proteinase inhibitors with M(r) 8kDa was eluted together with AQN 1 spermadhesin. An interaction of isolated spermadhesin AQN 1 and proteinase inhibitor was shown.

Amino Acid Sequence↗
PubMed1990

Adsorption of seminal plasma proteins by boar spermatozoa.

Seminal plasma protein adsorption by boar spermatozoa was examined using ejaculated sperm from vesiculectomized boars and seminal plasma from vasectomized boars. Sperm adsorbed 14 pg protein/sperm in 10 min. When seminal plasma proteins were radiolabeled, most of the adsorbed radiolabel was present in low M(r) proteins, particularly a 12700 M(r) protein. A 349300 M(r) seminal plasma protein was also readily adsorbed. Three radiolabeled seminal plasma proteins (307600, 165400 and 7400 M(r)) were not detected on the sperm; either they are not adsorbed by the sperm or the sperm were previously exposed to these proteins in other accessory sex gland fluids and had already adsorbed them. A 29100 M(r) sperm protein was also radiolabeled (4.9% of the adsorbed radiolabel), although there was no corresponding seminal plasma protein. Large quantities of seminal plasma protein (particularly low M(r) proteins) are adsorbed by sperm not previously exposed to seminal vesicle secretion. The functions of these proteins are yet to be determined.

Journal Article↗
PubMedDate not supplied

Localized seminal plasma protein hypersensitivity.

Human seminal plasma protein hypersensitivity is a rare disorder. Since the first case report in 1958, allergic reactions to semen have gone relatively unnoticed or improperly diagnosed. Dozens of medical case reports and research prove that allergy to seminal fluid is a legitimate health concern.

Adult↗
PubMed2004

Interaction of fibronectin type II proteins with membranes: the stallion seminal plasma protein SP-1/2.

Seminal plasma of mammalians contains, among others, proteins that are characterized by the fibronectin (Fn) type II module. Our knowledge about the structure and the physiological function of seminal Fn type II proteins mainly originates from studies on PDC-109, the bovine representative of this protein family. The present work focuses on the equine protein SP-1/2 (also named HSP-1/2) with particular emphasis on its interaction with lipid membranes by employing the intrinsic protein fluorescence and a number of spin-labeled and fluorescent lipid analogues. The results indicate that the interaction of SP-1/2 with (lipid) membranes is similar to that of PDC-109 which can be explained by homologous amino acid sequences of both proteins. Like PDC-109, SP-1/2 has a specificity for phospholipids with the phosphocholine headgroup. Upon binding to lipid vesicles, the protein intercalates into the hydrophobic membrane core, resulting in a rigidification of the lipid phase and, at higher concentration, in a perturbation of membrane structure. However, compared with PDC-109, the impact of SP-1/2 on membranes is less intense in that the degree of protein-mediated immobilization of lipids was lower. Furthermore, different to PDC-109, SP-1/2 was not able to extract lipids from human red blood cells. The data are discussed with regard to similarities and species-specific differences of the function of seminal Fn type II proteins in the genesis of sperm cells.

Amino Acid Motifs↗
PubMedDate not supplied

[Formation of interpolymer complexes with human seminal plasma proteins].

Formation of interpolymeric complexes was studied involving human lactoferrin, prostate beta-globulin, specific acid phosphatase and polymers of various nature: polysaccharides--heparin, dextran sulfate; polylysine-16; proteins--human albumin, equine hemoglobin, gelatin, protamine. Immunoelectrophoresis proved to be a sensitive procedure to register the interpolymeric complexes formed. Electrophoretic mobility of lactoferrin and prostatic beta-globulin was most distinctly altered. Mechanisms of the complexes formation, including ionic and hydrophobic interactions, are discussed.

Humans↗
PubMed2006

Affinity liquid chromatography and capillary electrophoresis of seminal plasma proteins.

Interactions of boar, bull, and human seminal plasma proteins with heparin and phosphorylcholine were studied by affinity LC using heparin immobilized to a Toyopearl support. A step gradient elution from 0.15 to 1.50 M NaCl was employed to elute the seminal plasma proteins. Relative amounts of the heparin-binding fraction of seminal plasma proteins (H+) in seminal plasma of three species were determined. Further on, the fraction of seminal plasma proteins interacting with phosphorylcholine-binding proteins (P+) was evaluated. P+ proteins were not found in human seminal plasma and their highest amount was present in bull seminal plasma. A CE method was developed for separation of seminal plasma proteins. Various capillaries and separation conditions were tested; the best resolution was obtained in a bare-silica capillary, with a micellar system consisting of a 0.02 M borate buffer and 0.05 M SDS pH 10.0. The optimized conditions were applied to the identification of the components in boar plasma.

Animals↗
PubMedDate not supplied

Patterns of human seminal plasma proteins on polyacrylamide gel electrophoresis.

Seminal plasma proteins were separated by sodium dodecylsulphate polyacrylamide gel electrophoresis and the patterns for different conditions compared by densitometry. The changes in pattern with time after ejaculation because of proteolysis could be largely prevented by addition of bacitracin. Patterns were similar within the one man and little influenced by duration of abstinence from ejaculation. There were marked variations in pattern between individuals and no specific differences could be detected between samples from men with normal semen analyses, vasectomy, or azoospermia from seminiferous tubule failure. However, there were distinct patterns with congenital absence of the vasa and seminal vesicles and with androgen deficiency. Methods for identification of testicular and epididymal proteins in semen would expand the clinical usefulness of examination of seminal plasma proteins.

Bacitracin↗
PubMed2006

Genomic structure and tissue-specific expression of human and mouse genes encoding homologues of the major bovine seminal plasma proteins.

Sperm capacitation is a maturation event that takes place in the female reproductive tract and is essential for fertilization. A family of phospholipid-binding proteins present in bovine seminal plasma (BSP proteins) binds the sperm membrane at ejaculation and promotes bovine sperm capacitation. Homologues of these proteins have also been isolated from boar, ram, goat, bison and stallion seminal fluid, suggesting that BSP proteins and their homologues are conserved among mammals. However, there have been no reports on BSP-homologous proteins in mice and humans to date. A search of the mouse and human genomes, using the nucleic acid sequences of BSP proteins, revealed the presence of three BSP-like sequences in the mouse genome, named mouse BSP Homologue 1 (mBSPH1), mBSPH2 and mBSPH3, and one sequence in the human genome (hBSPH1). Mouse epididymal expressed sequence tags corresponding to partial sequences of mBSPH1 and mBSPH2 were identified. The entire complementary DNA (cDNA) sequences of mBSPH1 and mBSPH2 from mouse epididymis and hBSPH1 from human epididymis were obtained by 5'-/3'-rapid amplification of cDNA ends (RACE) and encode predicted proteins containing two tandemly repeated fibronectin type II domains, which is the signature of the BSP family of proteins. Using RT-PCR, it was revealed that mBSPH1, mBSPH2 and hBSPH1 mRNA are expressed only in the epididymis. Expression of mBSPH3 was not detected in any tissue and probably represents a pseudogene. This work shows, for the first time, that BSP homologues are expressed in mouse and human and may be involved in sperm capacitation in these species.

Adult↗
PubMed2001

Membrane insertion and lipid-protein interactions of bovine seminal plasma protein PDC-109 investigated by spin-label electron spin resonance spectroscopy.

The interaction of the major acidic bovine seminal plasma protein, PDC-109, with dimyristoylphosphatidylcholine (DMPC) membranes has been investigated by spin-label electron spin resonance spectroscopy. Studies employing phosphatidylcholine spin labels, bearing the spin labels at different positions along the sn-2 acyl chain indicate that the protein penetrates into the hydrophobic interior of the membrane and interacts with the lipid acyl chains up to the 14th C atom. Binding of PDC-109 at high protein/lipid ratios (PDC-109:DMPC = 1:2, w/w) results in a considerable decrease in the chain segmental mobility of the lipid as seen by spin-label electron spin resonance spectroscopy. A further interesting new observation is that, at high concentrations, PDC-109 is capable of (partially) solubilizing DMPC bilayers. The selectivity of PDC-109 in its interaction with membrane lipids was investigated by using different spin-labeled phospholipid and steroid probes in the DMPC host membrane. These studies indicate that the protein exhibits highest selectivity for the choline phospholipids phosphatidylcholine and sphingomyelin under physiological conditions of pH and ionic strength. The selectivity for different lipids is in the following order: phosphatidylcholine approximately sphingomyelin > or = phosphatidic acid (pH 6.0) > phosphatidylglycerol approximately phosphatidylserine approximately and rostanol > phosphatidylethanolamine > or = N-acyl phosphatidylethanolamine >> cholestane. Thus, the lipids bearing the phosphocholine moiety in the headgroup are clearly the lipids most strongly recognized by PDC-109. However, these studies demonstrate that this protein also recognizes other lipids such as phosphatidylglycerol and the sterol androstanol, albeit with somewhat reduced affinity.

Animals↗
PubMed1998

Interaction of bull, stallion and boar seminal plasma proteins and sperms with acidic polysaccharides.

The interaction of seminal plasma proteins, sperms and detergent-released sperm proteins of three species with different types of acidic polysaccharides was studied. Heparin-binding activity of boar, bull and stallion seminal plasma proteins, sperms and sperm proteins was compared with their ability to interact with polysaccharides differing in the presence of the sulfate groups or in their saccharide moiety (chondroitin sulfate, dextran sulfate, fucoidan, hyaluronic acid). Bull seminal plasma proteins were characterized by higher affinity to heparin, fucoidan and dextran sulfate, while significant differences between different types of polysaccharides were detected in the case of boar proteins. Sperm protein interactions with acidic polysaccharides in bull and stallion were analogous to the binding of seminal plasma proteins. Bull and stallion seminal plasma proteins inhibited the interaction of corresponding sperm proteins with acidic polysaccharides.

Animals↗
PubMed1995

Effect of glycosylation on the heparin-binding capability of boar and stallion seminal plasma proteins.

Boar and stallion seminal plasmas were fractionated using affinity chromatography on heparin-Sepharose. In both species, among other proteins, the heparin-binding (H+) and non-heparin-binding (H-) fractions each contained glycoforms of either porcine PSP-I or equine HSP-1 and HSP-2. However, porcine H+/PSP-I eluted as a monomeric protein, whereas H-/PSP-I formed a heterodimer with PSP-II, another major seminal plasma protein. On the other hand, the stallion proteins H+/HSP-1 and H+/HSP-2 eluted together as an aggregate of relative molecular mass (M(r)) 90,000, whereas H-/HSP-1 and H-/HSP-2 eluted as monomers (15,000). Remarkably, when PSP-I and PSP-II from the H- fraction were separated, both proteins bound to heparin. Altogether these data show that glycosylation has an indirect effect on the heparin-binding ability of PSP-I, HSP-1 and HSP-2 through modulation of their aggregation state.

Amino Acid Sequence↗
PubMed1985

Immunological studies on seminal plasma proteins of the Indian buffalo and cattle.

Seminal plasma proteins of the Indian buffalo and cattle were immunologically investigated using rabbit antibuffalo seminal plasma serum, rabbit anticattle seminal plasma serum (unabsorbed and absorbed), gel diffusion, and immunoelectrophoretic analysis. At least 9-12 and 7-10 different proteins, respectively, were present in the seminal plasma of the buffalo and cattle. Albumin and IgG were identified in both the species. At least 4-6 seminal plasma proteins of the buffalo and cattle were antigenically similar to their blood serum proteins. Using absorbed rabbit antibuffalo seminal plasma serum and rabbit anticattle seminal plasma serum, at least 6-7 and 5-6 seminal plasma specific proteins, respectively, were observed in the buffalo and cattle seminal plasma. Antigenically these proteins were different from the blood serum proteins of these two species. The origin and biological significance of seminal plasma proteins are discussed.

Albumins↗
PubMed2004

The approach to conception for women with seminal plasma protein hypersensitivity.

PROBLEM: Allergic reactions to human seminal plasma protein has become increasingly recognized in the medical community. Treatment for most allergic conditions usually begins with avoidance of the offending allergen. For women with seminal plasma protein hypersensitivity (SPH) who desire to conceive, this approach is unacceptable. We describe a case report of a woman with an SPH who desired to have unprotected intercourse in order to conceive. METHODS: The patient underwent skin prick testing to her fiancé's fresh undiluted semen. Serum-specific IgG and IgE was performed by ELISA to the fiancé's whole seminal plasma and seminal plasma proteins (SPP). The patient underwent an intravaginal graded challenge to whole seminal fluid. Intrauterine insemination with washed spermatozoa was attempted but in vitro fertilization was subsequently required. RESULTS: The patient had a positive prick test to whole seminal plasma but negative specific IgG and IgE ELISA to SPPs. An intravaginal graded challenge to whole seminal plasma was well tolerated. However, she experienced a subsequent severe local reaction after unprotected intercourse. She deferred treatment with systemic desensitization to relevant SPPs. She failed intrauterine insemination but successfully conceived with in vitro fertilization. CONCLUSION: This case report emphasizes that SPH is not associated with sterility. It also indicates that whole seminal plasma graded challenge is not uniformly successful for the treatment of SPH.

Adult↗
PubMed1998

Biophysical characterization of the interaction of bovine seminal plasma protein PDC-109 with phospholipid vesicles.

PDC-109 is the major protein of bovine seminal plasma. It binds to the bovine sperm surface at ejaculation and modulates sperm capacitation. PDC-109 displays phosphorylcholine- and heparin-binding activities which are thought to account for its sperm surface coating and glycosaminoglycan-induced sperm capacitating activities, respectively. We have characterized the interaction of isolated PDC-109 with membranes of phospholipid vesicles using a biophysical approach. Our results show that PDC-109 interacts not only with the solvent-exposed phosphorylcholine head group but also with the hydrophobic core of liposomes. Binding of PDC-109 to membranes is a very rapid, biphasic process with half times of less than one second. Maximal binding of PDC-109 to small unilamellar vesicles was achieved with a stoichiometric ratio of 10-11 phosphatidylcholine molecules/PDC-109 molecule. Incorporation of phosphatidylethanolamine or phosphatidylserine into phosphatidylcholine vesicles reduced the binding of PDC-109, suggesting that both the density of phosphorylcholine groups and the surface charge determine the interaction of the seminal plasma protein with the surface of the membrane. Electron spin resonance measurements showed that binding of PDC-109 to phosphatidylcholine vesicles caused a rigidification of the membrane. The relevance of the data for describing the role of PDC-109 in the modulation of sperm capacitation is discussed.

Animals↗