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The protein encoded by SPINK1 is a trypsin inhibitor, which is secreted from pancreatic acinar cells into pancreatic juice.
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Data show that alteration in beta-catenin (show CTNNB1 Proteins) expression, a core component of the CDH17/beta-catenin (show CTNNB1 Proteins) axis, in tumors affects serine peptidase inhibitor Kazal type 1 (SPINK1) serum levels in hepatocellular carcinoma (HCC (show FAM126A Proteins)) patients.
Findings indicate that the serine protease inhibitor, Kazal type 1 (SPINK1) p.N34S allele may cause reduced SPINK1 expression.
Having correlated our findings with current knowledge of SPINK1's role in exocrine pancreas pathophysiology, we propose that complete and partial functional losses of the SPINK1 gene are associated with quite distinct phenotypes, the former causing a new pediatric disease entity of severe infantile isolated exocrine pancreatic insufficiency (EPI (show TFPI Proteins)) .
results suggest that rs142703147:C>A, which disrupts a PTF1L-binding site within an evolutionarily conserved HNF1A (show HNF1A Proteins)-PTF1L cis (show CISH Proteins)-regulatory module located upstream of the SPINK1 promoter, contributes to the chronic pancreatitis risk haplotype.
Studied mutations in cationic trypsinogen (PRSS1 (show PRSS1 Proteins)) and serine protease inhibitor Kazal type 1 (SPINK1) and their association with alcoholic chronic pancreatitis (ACP (show NDUFAB1 Proteins)) and idiopathic chronic pancreatitis.
Studies indicate that serine peptidase inhibitor Kazal type 1 (SPINK1) gene, particularly the N34S mutation, has a genetic association with the development of pancreatitis [Meta-analysis].
association between SPINK1 p.N34S gene variation and chronic pancreatitis [review, meta-analysis]
We present the case of a child with a homozygous mutation N34S in the SPINK1 gene, leading to acute recurrent pancreatitis and ultimately to chronic pancreatitis
Used in silico splicing prediction programs to prioritize SPINK1 intronic variants for further quantitative RT-PCR analysis the non-pathological c.194 + 13T > G variant was predicted by different programs to generate a new & viable donor splice site, the prediction scores being comparable to those for the physiological c.194 + 2T donor splice site & even higher than those for the physiological c.87 + 1G donor splice site.
Gene mutations were present in PRSS1 (show PRSS1 Proteins) in 26 patients with acute recurrent and chronic pancreatitis, SPINK1 in 23, CTRC in 3, and CPA1 (show CPA1 Proteins) in 5. In the 31 patients with mutations in SPINK1, CTRC, or CPA1 (show CPA1 Proteins), 16 (51.6%) had homozygous or heterozygous mutations with other mutations.
Partially folded bovine pancreatic trypsin inhibitor analogues attain fully native structures when co-crystallized with S195A rat trypsin.
It is a trypsin-specific inhibitor in the pancreas.
IFN regulatory factor 2 (Irf2 (show IRF2 Proteins)) has a regulatory role in trypsinogen5 gene transcription, which is resistant to a major endogenous trypsin inhibitor, Spink3
SPINK3 modulates sperm physiology through a downstream reduction of endogenous NO concentration and independently of SPINK3 trypsin inhibitory activity.
uterine-gland-derived SPINK3, as a new paracrine modulator, might play an important role in embryo implantation through its influence on stromal decidualization in mice.
Spink3 may act as a growth factor, leading to cell proliferation and regeneration of tissue structure.
Results suggest that regulation of Prss1 (show PRSS1 Proteins) and Spink3 expression is involved in the susceptibility to experimentally induced pancreatitis.
Spink3 trypsin inhibitor is required for normal pancreatic development. Data indicate an important relationship between endogenous pancreatic trypsin and Spink3 and the development of pancreatitis.
SPINK3 mRNA is upregulated in chronic pancreatitis.
Spink3 may play important roles in proliferation and/or differentiation of various cell types during development.
The protein encoded by this gene is a trypsin inhibitor, which is secreted from pancreatic acinar cells into pancreatic juice. It is thought to function in the prevention of trypsin-catalyzed premature activation of zymogens within the pancreas and the pancreatic duct. Mutations in this gene are associated with hereditary pancreatitis and tropical calcific pancreatitis.
pancreatic secretory trypsin inhibitor
, serine protease inhibitor Kazal-type 1
, serine protease inhibitor, Kazal type 1
, tumor-associated trypsin inhibitor
, calcium transport inhibitor
, pancreatic secretory trypsin inhibitor II
, pancreatic secretory trypsin inhibitor type II (PSTI-II)
, serine peptidase inhibitor, Kazal type 3
, serine protease inhibitor Kazal-type 3
, serine protease inhibitor, Kazal type 3
, serine peptidase inhibitor, Kazal type 1
, prostatic secretory glycoprotein