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Validated All-in-One™ qPCR Primer for PRSS1(NM_002769.4) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. This enzyme is secreted by the pancreas and cleaved to its active form in the small intestine. It is active on peptide linkages involving the carboxyl group of lysine or arginine. Mutations in this gene are associated with hereditary pancreatitis. This gene and several other trypsinogen genes are localized to the T cell receptor beta locus on chromosome 7. [provided by RefSeq].
Gene References into function
- Reviews aspects of the molecular evolution and normal physiology of trypsinogen revealed by studies of PRSS1 in pancreatitis, and proposes three defensive mechanisms against premature trypsin activation within the pancreas.
- This study reports a new pancreatitis-associated mutation--R116C (CGT > TGT: c.346C > T)--in the gene.
- Here we report a family with hereditary pancreatitis that carries a novel PRSS1 mutation (R122C).
- Presence of cathepsin B in the human pancreatic secretory pathway and its role in trypsinogen activation during hereditary pancreatitis
- No difference was observed in the frequency of PRSS1 or PSTI polymorphisms in neonates carrying or not carrying CF mutations.
- "Loss of function" mutations in the cationic trypsinogen gene may act as a protective factor against pancreatitis
- This paper proposed that while "gain of function" mutations in the PRSS1 gene predispose one to pancreatitis, "loss of function" mutations in the gene may protect one against the disease.
- trypsin plays a role in the growth of PAR-2-positive pancreatic cancer cells and serves as a potent mitogen in vitro, functioning as a growth factor
- No mutation was found in the PRSS1 gene among pancreatitis Brazilian patients.
- pancreatitis-associated cationic trypsin mutations causes increased transactivation of anionic trypsinogen.
- Protease serine 1 (PRSS1) gene mutation is an important casuative factor in patients with hereditary pancreatitis.
- Expression of trypsinogen 1 and 2 is better preserved than prostate specific antigen in high-grade prostatic neoplasms
- Trypsin activates p42,44 MAP kinase phosphorylation via protein kinase C(epsilon)and proteinase activated receptor 2 in human cultured prostate stromal cells. This may be an important mechanism of BPH pathophysiology.
- family of hereditary pancreatitis associated with the CT gene mutation, an arginine to histidine amino acid substitution at residue 122
- the risk of pancreatic cancer is not related to PRSS1 mutation type and does not appear to be related to the mode of inheritance
- gene conversion between PRSS1 and PRSS2 trypsinogen genes can occur and cause genetically determined chronic pancreatitis
- Autosomal dominant pancreatitis with increased cancer risk in the studied Thai family is most likely due to missense (R116C) mutation in the PRSS1 gene.
- study suggested a balanced expression of TATI and trypsinogen is required in normal tissue and that this balance is disrupted during tumor progression
- Cathepsin B caused activation of trypsinogen-1 with a trypsin yield of about 30% of that produced by enterokinase.
- Immunoreactive TAP in urine in acute pancreatitis is mainly composed of the C-terminal pentapeptide, DDDDK.
- Genetic mutation in the pancreatic secretory trypsin inhibitor has been described to play a role in the development of pancreatitis.
- protease serine 1 protease(PRSS1) defects seem to be causative for pancreatitis, whereas defects in protease serine 1 protease(SPINK1) are suggested to be associated with the disease
- Mutations and variations in pancreatitis patients.
- R122H human cationic trypsinogen transgenic mouse failed to develop a spontaneous pancreatitis but a repeatedly provoked cerulein-induced pancreatitis led to a slightly more severe pancreatitis.
- Human cationic trypsinogen is sulfated on Tyr154.
- Isoform B of trypsinogen 4, with a leucine N terminus, is the predominant (if not exclusive) form of the enzyme in post mortem human brain, but that both isoforms are expressed in transiently transfected cells
- the mutation of PRSS1 gene, may not confer a high risk for recurrent pancreatitis.
- in the investigated Finnish pedigree with hereditary pancreatitis, the PRSS1 mutation R122H is linked with chronic disease; although the SPINK1 mutation (N34S) was also observed in two individuals, it was not linked with the disease
- Hereditary pancreatitis is associated with R122H mutation in exon 3 of PRSS1 gene.
- Patients with HP have a marked relative and absolute increased risk of PA as compared to the general population, especially in smokers. There is no correlation with the type of PRSS1 mutation.
- Novel mutation and polymorphism of PRSS1 gene in the Chinese patients with hereditary pancreatitis and chronic pancreatitis.
- Total immunoreactivity of soluble urinary MMP-14 and the levels of trypsin (TRY)-1 and TRY-2, but not of TATI, were also significantly increased in diabetic nephropathy
- A fusion with PRSS2 is associated with hereditary pancreatitis.
- study reports a novel A121T mutation; this novel PRSS1 A121T mutation highlights the surface exposed region PRSS1 A121-R122-V123 as a hotspot for hereditary pancreatitis
- Multisite mutations of PRSS1 were found in a patient with chronic pancreatitis. C to A mutation occurred in exon 3 of PRSS1, and T to A mutation in the same exon.
- Benign pancreatic hyperenzymemia cannot be explained by mutations in PRSS1.
- In members from 10 unrelated HP families (all R122H-positive), we found 7 different haplotypes to segregate with the R122H mutation.
- Hereditary pancreatitis patients with the different mutations in the PRSS1 gene had similar histopathological features and the same clinical outcome.
