High impact information on Svs1

• Seminal vesicle secretion IV gene: allelic difference due to a series of 20-base-pair direct tandem repeats within an intron [1].
• The 5'-flanking region contains three conserved elements found in other seminal vesicle secretion genes (SVS IV-VI proteins) within 250 bp of the transcription start site as well as a glucocorticoid response element at position -314 in the SVS II gene [2].
• Purification and cell-free synthesis of a major protein from rat seminal vesicle secretion. A potential marker for androgen action [3].
• Colony filter hybridization and restriction mapping was used to demonstrate that a 620 NTP long insert in a plasmid clone (pSV2) represents the almost full length structural gene coding for a precursor to the seminal vesicle secretion protein IV (SVS IV) [4].
• Use of a cloned double stranded cDNA coding for a major androgen dependent protein in rat seminal vesicle secretion: the effect of testosterone in gene expression [4].

Biological context of Svs1

• In the parotid gland, secretory acinar cells showed immunoreactivity with antibodies against prostatic binding protein, cystatin-related peptide and acid phosphatase (isoenzyme pI 8.0; 5.6) typical of ventral prostate, and seminal vesicle secretion VI [5].
• Phosphorylation of sperm-binding proteins from seminal vesicle secretion by sperm surface protein kinase [6].
• Mapping cis-DNA regulatory elements in seminal vesicle secretion genes, prostate C3(1) gene, and the mouse mammary tumor virus-long terminal repeat DNA [7].
• Depending on the sexual activity of the respective animal and the extraction conditions, the protein pattern of the seminal vesicle secretion varies to some extent [8].
• Our results suggest that SVS proteins are antigenic and that these antigens are bound to the spermatozoa and could take part in early pre-fertilisation events such as capacitation or sperm transport [9].

Anatomical context of Svs1

• Immunofluorescent localization studies of SVS IV, an androgen-dependent secretory protein purified from rat seminal vesicle secretion, show that cultured seminal vesicle epithelial cells are immunoreactive [10].
• A protein substance reacting with basic protein of rat seminal vesicle secretion, present in serum, testicular and epididymal homogenates and on unwashed spermatozoa, has been identified and isolated [11].
• Expression study of three secretory proteins (prostatic secretory protein of 94 amino acids, probasin, and seminal vesicle secretion II) in dysplastic and neoplastic rat prostates [12].
• The relationship between the quantity of seminal vesicle secretion in the ejaculate, the percentage of spermatozoa reaching the uterus and fertility was studied in rats [13].
• The number of fetuses did not show a close correlation with the quantity of seminal vesicle secretion [13].

Associations of Svs1 with chemical compounds

• Comparison of 35S- and digoxigenin-labeled RNA and oligonucleotide probes for in situ hybridization. Expression of mRNA of the seminal vesicle secretion protein II and androgen receptor genes in the rat prostate [14].
• However, since the protein could not be detected in blood, peritoneal fluid, saliva, milk, uterine fluid, seminal vesicle secretion, coagulating gland secretion or prostatic secretion, it would appear that the testis and epididymis may be unique in containing the protein in a soluble form within their luminal secretions [15].

Physical interactions of Svs1

• Purification of prolactin binding protein from rat seminal vesicle secretion [16].

Other interactions of Svs1

• A comparative study of hormonal regulation of three secretory proteins (prostatic secretory protein-PSP94, probasin, and seminal vesicle secretion II) in rat lateral prostate [17].
• SDS-PAGE and Western blotting of the seminal vesicle secretion revealed alterations in the protein pattern and loss of the caltrin-related immunoreactive bands [18].

Analytical, diagnostic and therapeutic context of Svs1

• The antibodies were also used in immunofluorescence histochemistry with the rat copulatory plug, showing for the first time that all the major proteins of seminal vesicle secretion are components of this reproductive structure [19].
• Effects of androgen status on the synthesis and secretion of rat caltrin have been studied by three different procedures: a) immunocytochemistry in seminal vesicle tissues; b) polyacrylamide gel electrophoresis and Western immunostaining of seminal vesicle secretion; and c) evaluation of trypsin inhibitory activity of the seminal vesicle secretion [18].

References