Difference between revisions of "Part:BBa K1328003"

Latest revision as of 23:04, 17 October 2014

Insulin

The insulin gene consists three exons, which encode B chain, C peptide and A chain.

We modified the protease recognition sites of insulin gene to make sure that the insulin gene product undergoes accurate modification.

The signal peptide and C peptide are removed after transcription and translation and two disulfide bonds form between A chain and B chain, undergoing folding to become functional insulin.

Insulin (modified protease recognition sites)

Encodes the human insulin gene (full length). Two 6 bp sequences were inserted into two separate sites within the insulin gene to allow enzymatic digestion by the protease furin. Originally, proinsulin is cleaved three times with three different enzymes, prohormone convertases (PC1 and PC2), and carboxypeptidase E before being secreted as mature insulin. Since PC1 and PC2 expression is tissue specific, we replaced their recognition sites with that of furin, which is universally expressed, thus allowing this insulin gene to be expressed and processed in any somatic cell type.

Sequence and Features