Disease relevance of Snn

• Cells in culture that do not express Snn show considerable resistance to TMT toxicity [1].

High impact information on Snn

• Triple label confocal microscopy of Snn-transfected cells and Percoll gradient purification of mitochondria showed Snn localized to the mitochondria and other membrane structures [1].
• In vitro, Snn peptide can bind TMT in a 1:1 ratio and can de-alkylate TMT to dimethyltin (DMT) [1].
• We now show that transfection with Snn sensitized TMT-resistant NIH-3T3 mouse fibroblasts to both TMT and DMT cytotoxicity [1].
• Snn is localized in tissues with known sensitivity to trimethyltin (TMT), including the central nervous system, immune system, spleen, kidney and lung [1].
• Stannin (Snn) is a highly conserved, 88-amino acid protein that may mediate the selective toxicity of organotins [1].

Chemical compound and disease context of Snn

• Stannin, a protein that localizes to the mitochondria and sensitizes NIH-3T3 cells to trimethyltin and dimethyltin toxicity [1].

Biological context of Snn

• We have also isolated a partial human stannin cDNA clone and analyzed the open reading frame [2].
• In this study, we have isolated a mouse stannin genomic clone and have characterized the gene's intron-exon organization, promoter region, and chromosomal location [2].
• Fluorescence in situ hybridization analysis localized stannin to mouse Chromosome (Chr) 16 at band A2 [2].

Associations of Snn with chemical compounds

• Stannin is a protein that has been localized to trimethyltin-sensitive cell populations, and evidence suggests it plays a role in the toxic effects of organotins [2].

References