Disease relevance of Svs7

• Expression of caltrin in the baculovirus system and its purification in high yield and purity by cobalt (II) affinity chromatography [1].

High impact information on Svs7

• The SVS VII-sperm binding greatly enhanced sperm motility but did not induce sperm capacitation [2].
• A novel heat-labile phospholipid-binding protein, SVS VII, in mouse seminal vesicle as a sperm motility enhancer [2].
• The primary structure deduced from the corresponding cDNA was confirmed using amino acid sequence determination, which supported the finding that SVS VII consists of 76 amino acid residues with five disulfide bridges [2].
• SVS VII, one of seven major proteins in mouse seminal vesicle secretion, was purified to homogeneity [2].
• The results of TLC overlay assay for the binding of (125)I-SVS VII to phospholipids and the interaction between SVS VII and phospholipid liposomes demonstrated a specific binding of this protein to both phosphatidylethanolamine and phosphatidylserine [2].

Biological context of Svs7

• Testosterone-induced increases in caltrin mRNA levels were detected prior to S-phase progression and initiation of proliferation in this cell population [3].

Anatomical context of Svs7

• Within the dorsal prostate, in situ hybridization always localized caltrin mRNAs to the prostatic epithelial cells [3].
• Caltrin messenger RNA (mRNA) was highly expressed in the prostates of intact mice [3].
• Caltrin has been demonstrated previously to function as a calcium transport inhibitor at the plasma membrane [3].
• Here we report the expression and purification of caltrin, previously shown to hinder the influx of calcium into epididymal spermatozoa [1].

Regulatory relationships of Svs7

• Findings of this study indicate that caltrin is highly expressed and androgen-regulated in the murine prostate, where it is associated with androgen-induced proliferation and differentiation of epithelial cells [3].

Other interactions of Svs7

• The use of subtractive hybridization to isolate genes that are differentially expressed during the early phase of androgen-induced prostatic regrowth in castrated mice resulted in identification of the murine caltrin gene [3].

Analytical, diagnostic and therapeutic context of Svs7

• Five weeks following castration of mice, steady state caltrin mRNA levels were reduced by 70% [3].
• Reverse transcriptase-polymerase chain reaction analysis of prostate tissue localized caltrin mRNA transcripts to the dorsal but not the ventral or lateral prostate [3].
• Recombinant His-tagged caltrin was purified utilising both nickel (II)-nitrilotriacetic acid (Ni(2+)-NTA) and cobalt (II)-carboxymethylaspartate (Co(2+)-CmAsp) immobilised metal affinity chromatography (IMAC) [1].
• Cloning of the caltrin gene into the pCDNA3.1 V5/His-TOPO vector and the subsequent ligation of the caltrin-His sequence into the transfer vector pBacPAK9 allowed the expression of recombinant caltrin using the baculovirus expression vector system (BEVS) [1].

References