In the endoplasmic reticulum of beta cells the proinsulin molecule is cleaved in two places, yielding the A and B chains of insulin and an intervening, biologically inactive C peptide.
When the DNAzyme molecule is cleaved by the target, L-histidine, a partial substrate strand is produced, which in turn can hybridize with the capture probe, forming a DNA duplex.
Upon arrival in the MIIC, the Ii molecule is cleaved through the action of proteases leaving a peptide fragment termed CLIP in the MHCII peptide-binding groove [2].
Here, the molecule is cleaved by the sequential actions of beta site APP cleaving enzyme 1 (BACE 1) and the γ-secretase complex to produce a soluble N-terminal fragment (sAPPβ) and a 37 49 amino acid amyloid β-peptide (Aβ) – the so-called 'amylogenic pathway' [4].
Copeptin, the stable C-terminal part of the AVP precursor molecule, is cleaved from pro-AVP during processing and is secreted in an equimolar concentration with AVP.
Previously, gel electrophoresis has been used to show where the RNA molecule is cleaved during MOHCA, but combining MOHCA with deep sequencing provides much more detailed information and significantly increases throughput.
In one version, the assay measures the amount of thrombin generated over time in platelet poor or platelet rich plasma by monitoring the change in flourescence as a fluorogenic substrate molecule is cleaved by thrombin.
Epithelial cell adhesion molecule is cleaved by proteases present in cell membranes (sheddases) from EpCAM full length (EpCAM-FL) to EpCAM C-terminal fragment (EpCAM-CTF), which is a substrate for γ-secretase that is further processed to the intracellular signalling molecule EpICD Maetzel et al, 2009; Figure 4A).
