The granted patent issued by the USPTO now confers exclusive rights to the Company's lead product, PRP, by demonstrating that compositions comprising trypsinogen
and chymotrypsinogen exhibit a synergistic ability to inhibit the growth of various cancer cell lines.
The remarkable achievement to identify and develop a suitable method to measure four key analytes from PRP, the two proenzymes, trypsinogen
and chymotrypsinogen, as well as the activated enzymes, trypsin and chymotrypsin, is particularly significant due to the close structural similarity of each protein structure.
(IRT) as a biomarker for cystic fibrosis: challenges in newborn dried blood spot screening.
is produced as an inactive precursor of the enzyme trypsin and recognized by antibodies.
Number Enzyme Accepted name Other names number 1 EC Yeast proteinase A Saccharopepsin 188.8.131.52 2 EC Rhizopus acid Rhizopuspepsin 184.108.40.206 proteinase 3 EC Endothia acid Endothiapepsin 220.127.116.11 proteinase 4 EC Retropepsin HIV aspartyl 18.104.22.168 protease, HIV proteinase, retroproteinase, HIV- 1 protease, HIV-2 protease 5 EC Aspergillopepsin I Proteinase, 22.214.171.124 Aspergillus acid protease, Aspergillus acid proteinase, Aspergillus aspartic proteinase, Aspergillus carboxyl proteinase, denapsin, proctase B, P, proteinase B, sumizyme AP, trypsinogen
kinase, pepsin-type aspartic proteinase, carboxyl proteinase 6 EC Aspergillopepsin II Proteinase A, proctase 126.96.36.199 A, Aspergillus niger var.
Newborn screening (NBS) for CF started as a pilot study in Colorado in 1980  after the identification of elevated immunoreactive trypsinogen
(IRT) in the dried blood spot of newborns with CF .
The polymorphisms at PRSS1-PRSS2 rs10273739, which influence trypsinogen
expression, and MORC4 rs12688220, which associate with atypical localization of cludin-2 in pancreatic acinar cells, are associated with acute pancreatitis , related recurrent acute pancreatitis, and chronic pancreatitis [3, 4].
Prediction of the severity of acute pancreatitis on admission by urinary trypsinogen
activation peptide: A meta-analysis World J Gastroenterol 2013; 19: 4607-4615.
In the normal state these enzymes are synthesized in pancreatic acinar cells as inactive pro-enzymes (such as trypsinogen
) and are maintained in this state until activated by enterokinase upon entry into the gut lumen.
Serum C-reactive protein at 48 hours, urinary trypsinogen
activation peptides within 12-24 hours of onset14, serum levels of interleukins 6 and 8 are the areas attracting latest interest to predict severity and prognosis15.
First, a blood spot is obtained in the first few days of life to measure immunoreactive trypsinogen
Bovine serum albumin (66kDa), ovoalbumin (45kDa), glyceraldehyde 3-phosphate dehydrogenase (36kDa), carbonic anhydrase (29kDa), trypsinogen
(24kDa), trypsin inhibitor (20kDa) and lactoalbumin (14.2kDa) were used as molecular weight markers.