[HTML][HTML] Exon skipping of cathepsin B: mitochondrial targeting of a lysosomal peptidase provokes cell death
The alternatively spliced messenger RNA of the human cysteine peptidase cathepsin B
missing exons 2 and 3 encodes a truncated form of the enzyme lacking the signal peptide
and part of the inhibitory propeptide. This deletion results in a new N-terminal leader
sequence characteristic of proteins predestined for transport into mitochondria. We
determined enzyme targeting to intracellular organelles by transfecting HeLa cells with
constructs containing segments of variable length of the N terminus of truncated cathepsin B …
missing exons 2 and 3 encodes a truncated form of the enzyme lacking the signal peptide
and part of the inhibitory propeptide. This deletion results in a new N-terminal leader
sequence characteristic of proteins predestined for transport into mitochondria. We
determined enzyme targeting to intracellular organelles by transfecting HeLa cells with
constructs containing segments of variable length of the N terminus of truncated cathepsin B …