Localization and concentration of a new bioactive acetic seminal fluid protein (aSFP) in bulls (Bos taurus)

Einspanier, Ralf; WAmselgruber, W; Sinowatz, Fred; Henle, T.; Röpke, R; Scham, D

doi:10.1530/jrf.0.0980241

Cited by 20 publications

(13 citation statements)

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“…Bovine acidic seminal fluid protein is a member of the spermadhesin family that essentially consists of a single CUB domain [32][33][34][35]. In itro, this protein functions as a mitogen, growth factor and it stimulates progesterone secretion in cultured ovarian cells [32].…”

Section: Discussionmentioning

confidence: 99%

A cDNA cloned from pregnant mouse uterus exhibits temporo-spatial expression and predicts a novel protein

Kasik

1998

Biochemical Journal

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A cDNA was cloned from a pregnant mouse uterus cDNA library. On conceptual translation, the cDNA has one long open reading frame that predicts a novel protein of 606 amino acids. This protein is principally composed of two CUB domains and a ZP domain; motifs found in proteins implicated in egg-sperm recognition. Probes derived from the cDNA were used to conduct Northern hybridizations. The expression of this mRNA is temporal; message first appears in the uterus 6 days prior to birth, it increases each subsequent day to attain maximal levels at 3 days prior to birth and then abruptly decreases during the last 3 days of pregnancy. The expression of this mRNA is restricted; message is abundant in the uterus during late pregnancy, but it is not found in non-pregnant uterus or in a variety of adult or fetal tissues. The temporo-spatial expression of this pregnant uterus specific mRNA and the consolidation in the predicted protein of two motifs implicated in early pregnancy events suggests that the product of the gene represented by this mRNA may play an important role in events that transpire during late pregnancy.

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Section: Discussionmentioning

confidence: 99%

A cDNA cloned from pregnant mouse uterus exhibits temporo-spatial expression and predicts a novel protein

Kasik

1998

Biochemical Journal

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“…It is encoded by a single gene locus [3]. This 13 kDa protein is mainly synthesized by the ampulla and seminal vesicle epithelium of the bull in high concentrations (l-7 mg/ml) and has not been detected in any other bovine tissues nor in other mammalian species, such as goat, sheep, pig, rat, dog, or human [4,5].…”

Section: Introductionmentioning

confidence: 99%

“…It comprises 114 residues and shows up to 50% similarity with boar spermadhesins [6-lo]. Unlike the porcine proteins, bovine aSFP does not tightly bind to the surface of spermatozoa [5], and therefore may not play a role in sperm-egg interaction. Interestingly, aSFP has been characterized as a new growth factor which stimulates the in vitro division of lymphocytes and progesterone secretion by ovarian granulosa cells [l 11.…”

Section: Introductionmentioning

confidence: 99%

Bovine seminal plasma ASFP: Localization of disulfide bridges and detection of three different isoelectric forms

Einspanier¹,

Krause

Calvete

et al. 1994

FEBS Letters

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Acidic seminal fluid protein (aSFP) is a major 13 kDa protein isolated from bull seminal plasma and characterized as a new growth factor which stimulates in vitro cell division and progesterone secretion by ovarian cells. Here, we establish that the four cysteines of oxidized aSFP form two disulfide bridges between nearest-neighbour residues. This pattern is conserved in boar spermadhesins, with which aSFP shares up to 50% amino acid sequence identity, and other proteins of the recently identified CUB domain family. Using isoelectric focusing in combination with sulfhydryl group-specific blotting, the three forms of aSFP were identified as completely oxidized (PI 4.7), partly reduced (PI 4.8) and fully reduced at pI 5.1. These results indicate that native aSFP possesses two pairs of cysteine residues of different reactivity. The observation that aSFP can protect sperm from oxidative damage might be explained by its reduction/oxidation behaviour.

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“…This contrasts with pig, where at least five different spermadhesin polypeptides (AQN-1, AQN-3, AWN, PSP-I and PSP-II), as well as several glycosylated isoforms coexist in the seminal plasma (Calvete et al, 1995c, and references therein) but is similar to the situation in the bull, where a single spermadhesin molecule (aSFP) is present (Einspanier et al, 1993;DostdovB et al, 1994b). However, bovine aSFP has an isoelectric point of 4.8 (Wempe et al, 1992) and binds neither heparin nor zona pellucida glycoproteins (Calvete et al, 1996b), whereas equine HSP-7 has a basic PI ("8) and displays both heparin-binding and zona-pellucidabinding activities.…”

Section: Discussionmentioning

confidence: 96%

Primary Structure of Stallion Seminal Plasma Protein HSP‐7, a Zona‐Pellucida‐Binding Protein of the Spermadhesin Family

Reinert

Calvete

Sanz

et al. 1996

European Journal of Biochemistry

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The primary structure of HSP-7, a 14-kDa protein isolated from stallion seminal plasma, has been determined. HSP-7 belongs to the spermadhesin protein family, shares 98 76 sequence identity with the boar seminal plasma protein AWN, and, like its boar homolog, displays zona-pellucida-binding activity. Despite these conserved structural and functional features, the equine and porcine spermadhesins differ in their topography on spermatozoa.Keywords: horse seminal plasma-7 ; anti-(boar seminal plasma protein) ; zona-pellucida-binding protein ; equine spermadhesi n ; seminal plasma protein.The interaction between complementary molecules situated on the surface of capacitated spermatozoa and the extracellular glycoprotein matrix encasing the oocyte, the zona pellucida, initiates the chain of events leading to the physiological agonistinduced acrosome reaction, a necessary step of the mammalian fertilization process (Yanagimachi, 1994). However, despite the importance of gamete recognition and binding for the survival and evolution of species and the fact that the complementarymolecules-hypothesis was already postulated at the beginning of this century (Lillie, 191 3), the molecular details of sperm-zonapellucida binding remain ill defined. Many sperm-associated proteins (both integral and peripheral proteins) have been proposed as candidates for primary zona pellucida-binding molecules Calvete, 1995, 1996). However, the actual participation of most of these proteins in the in wivo process, as well as the identity of zona pellucida carbohydrate structures acting as ligands for these proteins, are still a matter of debate (Cardullo and Wolf, 1995;Litscher et al., 1995;Thall et al., 1995;Yonezawa et a]., 1995;Bork, 1996;Tsai and Silver, 1996). From in vitro studies on gamete interaction of a few mammalian species, an emerging generalization regarding primary sperm -zona-pellucida binding is the involvement of spermatozoal carbohydrate-binding proteins and oligosaccharides of the oocyte's glycoprotein vestment (Macek and Shur, 1988). This protein-carbohydrate complementarity mechanism appears to be conserved in the fertilization process throughout the whole evolutionary scale, from plants to humans (Dale, 1991).In the pig, we have characterized a family of sperm surfaceassociated 12-14-kDa lectins, the spermadhesins, some of Correspondence to Juan J. Calvete and E. Topfer-Petersen, Institut fur Reproduktionsmedizin, Tierarztliche Hochschule Hannover,

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Localization and concentration of a new bioactive acetic seminal fluid protein (aSFP) in bulls (Bos taurus)

Cited by 20 publications

References 0 publications

A cDNA cloned from pregnant mouse uterus exhibits temporo-spatial expression and predicts a novel protein

A cDNA cloned from pregnant mouse uterus exhibits temporo-spatial expression and predicts a novel protein

Bovine seminal plasma ASFP: Localization of disulfide bridges and detection of three different isoelectric forms

Primary Structure of Stallion Seminal Plasma Protein HSP‐7, a Zona‐Pellucida‐Binding Protein of the Spermadhesin Family

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