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Article ; Online: Heterozygous Spink1 deficiency promotes trypsin-dependent chronic pancreatitis in mice.

Demcsák, Alexandra / Sahin-Tóth, Miklós

Cellular and molecular gastroenterology and hepatology

2024

Abstract: Background and aims: Heterozygous SPINK1 mutations are strong risk factors for chronic pancreatitis in humans yet heterozygous disruption of mouse Spink1 yielded no pancreatic phenotype. To resolve this contradiction, we used CRISPR/Cas9-mediated genome ...

Abstract	Background and aims: Heterozygous SPINK1 mutations are strong risk factors for chronic pancreatitis in humans yet heterozygous disruption of mouse Spink1 yielded no pancreatic phenotype. To resolve this contradiction, we used CRISPR/Cas9-mediated genome editing to generate heterozygous Spink1-deleted mice (Spink1-KO Methods: We investigated severity of acute pancreatitis and progression to chronic pancreatitis in Spink1-KO Results: . Prolonged but not transient cerulein stimulation resulted in increased intrapancreatic trypsin activity and more severe acute pancreatitis in Spink1-KO Conclusions: Heterozygous Spink1 deficiency caused more severe acute pancreatitis after prolonged cerulein stimulation, and promoted chronic pancreatitis after the cerulein-induced acute episode, and in two strains of trypsinogen mutant mice with spontaneous disease. In contrast, acute pancreatitis induced with limited cerulein hyperstimulation was unaffected by heterozygous Spink1 deletion, in agreement with recent observations that trypsin activity does not mediate pathologic responses in this model. Taken together, the findings strongly support the notion that loss-of-function SPINK1 mutations in humans increase chronic pancreatitis risk in a trypsin-dependent manner.
Language	English
Publishing date	2024-05-18
Publishing country	United States
Document type	Journal Article
ZDB-ID	2819778-1
ISSN	2352-345X ; 2352-345X
ISSN (online)	2352-345X
ISSN	2352-345X
DOI	10.1016/j.jcmgh.2024.05.009
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Article ; Online: Rate of Autoactivation Determines Pancreatitis Phenotype in Trypsinogen Mutant Mice.

Demcsák, Alexandra / Sahin-Tóth, Miklós

Gastroenterology

2022 Volume 163, Issue 3, Page(s) 761–763

MeSH term(s)	Animals ; Chymotrypsin/genetics ; Mice ; Pancreatitis/genetics ; Phenotype ; Trypsin/genetics ; Trypsinogen/genetics
Chemical Substances	Trypsinogen (9002-08-8) ; Chymotrypsin (EC 3.4.21.1) ; Trypsin (EC 3.4.21.4)
Language	English
Publishing date	2022-06-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80112-4
ISSN	1528-0012 ; 0016-5085
ISSN (online)	1528-0012
ISSN	0016-5085
DOI	10.1053/j.gastro.2022.06.001
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Article ; Online: Modelling chronic pancreatitis as a complex genetic disease in mice.

Jancsó, Zsanett / Demcsák, Alexandra / Sahin-Tóth, Miklós

Gut

2022 Volume 72, Issue 2, Page(s) 409–410

MeSH term(s)	Mice ; Animals ; Pancreatitis, Chronic/genetics ; Trypsinogen/genetics ; Trypsin/genetics ; Chronic Disease ; Acute Disease
Chemical Substances	Trypsinogen (9002-08-8) ; Trypsin (EC 3.4.21.4)
Language	English
Publishing date	2022-05-16
Publishing country	England
Document type	Letter ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Comment
ZDB-ID	80128-8
ISSN	1468-3288 ; 0017-5749
ISSN (online)	1468-3288
ISSN	0017-5749
DOI	10.1136/gutjnl-2022-327601
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Article ; Online: Misfolding-induced chronic pancreatitis in CPA1 N256K mutant mice is unaffected by global deletion of Ddit3/Chop.

Németh, Balázs Csaba / Demcsák, Alexandra / Geisz, Andrea / Sahin-Tóth, Miklós

Scientific reports

2022 Volume 12, Issue 1, Page(s) 6357

Abstract: Genetic mutations in pancreatic digestive enzymes may cause protein misfolding, endoplasmic reticulum (ER) stress and chronic pancreatitis. The CPA1 N256K mouse model carries the human p.N256K carboxypeptidase A1 (CPA1) mutation, a classic example of a ... ...

Abstract	Genetic mutations in pancreatic digestive enzymes may cause protein misfolding, endoplasmic reticulum (ER) stress and chronic pancreatitis. The CPA1 N256K mouse model carries the human p.N256K carboxypeptidase A1 (CPA1) mutation, a classic example of a pancreatitis-associated misfolding variant. CPA1 N256K mice develop spontaneous, progressive chronic pancreatitis with moderate acinar atrophy, acinar-to-ductal metaplasia, fibrosis, and macrophage infiltration. Upregulation of the ER-stress associated pro-apoptotic transcription factor Ddit3/Chop mRNA was observed in the pancreas of CPA1 N256K mice suggesting that acinar cell death might be mediated through this mechanism. Here, we crossed the CPA1 N256K strain with mice containing a global deletion of the Ddit3/Chop gene (Ddit3-KO mice) and evaluated the effect of DDIT3/CHOP deficiency on the course of chronic pancreatitis. Surprisingly, CPA1 N256K x Ddit3-KO mice developed chronic pancreatitis with a similar time course and features as the CPA1 N256K parent strain. In contrast, Ddit3-KO mice showed no pancreas pathology. The observations indicate that DDIT3/CHOP plays no significant role in the development of misfolding-induced chronic pancreatitis in CPA1 N256K mice and this transcription factor is not a viable target for therapeutic intervention in this disease.
MeSH term(s)	Acinar Cells/pathology ; Animals ; Carboxypeptidases A/genetics ; Endoplasmic Reticulum Stress/genetics ; Gene Deletion ; Mice ; Pancreas/metabolism ; Pancreatitis, Chronic/genetics ; Pancreatitis, Chronic/pathology ; Proteostasis Deficiencies/genetics ; Proteostasis Deficiencies/pathology ; Transcription Factor CHOP/genetics
Chemical Substances	Ddit3 protein, mouse ; Transcription Factor CHOP (147336-12-7) ; Carboxypeptidases A (EC 3.4.17.1)
Language	English
Publishing date	2022-04-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-09595-x
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Article ; Online: Mouse model of PRSS1 p.R122H-related hereditary pancreatitis highlights context-dependent effect of autolysis-site mutation.

Jancsó, Zsanett / Morales Granda, Nataly C / Demcsák, Alexandra / Sahin-Tóth, Miklós

Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.

2023 Volume 23, Issue 2, Page(s) 131–142

Abstract: Mutation p.R122H in human cationic trypsinogen (PRSS1) is the most frequently identified cause of hereditary pancreatitis. The mutation blocks protective degradation of trypsinogen by chymotrypsin C (CTRC), which involves an obligatory trypsin-mediated ... ...

Abstract	Mutation p.R122H in human cationic trypsinogen (PRSS1) is the most frequently identified cause of hereditary pancreatitis. The mutation blocks protective degradation of trypsinogen by chymotrypsin C (CTRC), which involves an obligatory trypsin-mediated cleavage at Arg122. Previously, we found that C57BL/6N mice are naturally deficient in CTRC, and trypsinogen degradation is catalyzed by chymotrypsin B1 (CTRB1). Here, we used biochemical experiments to demonstrate that the cognate p.R123H mutation in mouse cationic trypsinogen (isoform T7) only partially prevented CTRB1-mediated degradation. We generated a novel C57BL/6N mouse strain harboring the p.R123H mutation in the native T7 trypsinogen locus. T7R123H mice developed no spontaneous pancreatitis, and severity parameters of cerulein-induced pancreatitis trended only slightly higher than those of C57BL/6N mice. However, when treated with cerulein for 2 days, more edema and higher trypsin activity was seen in the pancreas of T7R123H mice compared to C57BL/6N controls. Furthermore, about 40% of T7R123H mice progressed to atrophic pancreatitis in 3 days, whereas C57BL/6N animals showed full histological recovery. Taken together, the observations indicate that mutation p.R123H inefficiently blocks chymotrypsin-mediated degradation of mouse cationic trypsinogen, and modestly increases cerulein-induced intrapancreatic trypsin activity and pancreatitis severity. The findings support the notion that the pathogenic effect of the PRSS1 p.R122H mutation in hereditary pancreatitis is dependent on its ability to defuse chymotrypsin-dependent defenses.
MeSH term(s)	Mice ; Humans ; Animals ; Chymotrypsin/genetics ; Trypsin/genetics ; Trypsinogen/genetics ; Ceruletide ; Mice, Inbred C57BL ; Pancreatitis/pathology ; Mutation
Chemical Substances	Chymotrypsin (EC 3.4.21.1) ; Trypsin (EC 3.4.21.4) ; Trypsinogen (9002-08-8) ; Ceruletide (888Y08971B) ; PRSS1 protein, human (EC 3.4.21.4)
Language	English
Publishing date	2023-02-09
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2056680-3
ISSN	1424-3911 ; 1424-3903
ISSN (online)	1424-3911
ISSN	1424-3903
DOI	10.1016/j.pan.2023.02.003
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Article ; Online: Preclinical testing of dabigatran in trypsin-dependent pancreatitis.

Pesei, Zsófia Gabriella / Jancsó, Zsanett / Demcsák, Alexandra / Németh, Balázs Csaba / Vajda, Sandor / Sahin-Tóth, Miklós

JCI insight

2022 Volume 7, Issue 21

Abstract: Pancreatitis, the inflammatory disorder of the pancreas, has no specific therapy. Genetic, biochemical, and animal model studies revealed that trypsin plays a central role in the onset and progression of pancreatitis. Here, we performed biochemical and ... ...

Abstract	Pancreatitis, the inflammatory disorder of the pancreas, has no specific therapy. Genetic, biochemical, and animal model studies revealed that trypsin plays a central role in the onset and progression of pancreatitis. Here, we performed biochemical and preclinical mouse experiments to offer proof of concept that orally administered dabigatran etexilate can inhibit pancreatic trypsins and shows therapeutic efficacy in trypsin-dependent pancreatitis. We found that dabigatran competitively inhibited all human and mouse trypsin isoforms (Ki range 10-79 nM) and dabigatran plasma concentrations in mice given oral dabigatran etexilate well exceeded the Ki of trypsin inhibition. In the T7K24R trypsinogen mutant mouse model, a single oral gavage of dabigatran etexilate was effective against cerulein-induced progressive pancreatitis, with a high degree of histological normalization. In contrast, spontaneous pancreatitis in T7D23A mice, which carry a more aggressive trypsinogen mutation, was not ameliorated by dabigatran etexilate, given either as daily gavages or by mixing it with solid chow. Taken together, our observations showed that benzamidine derivatives such as dabigatran are potent trypsin inhibitors and show therapeutic activity against trypsin-dependent pancreatitis in T7K24R mice. Lack of efficacy in T7D23A mice is probably related to the more severe pathology and insufficient drug concentrations in the pancreas.
MeSH term(s)	Animals ; Humans ; Mice ; Dabigatran ; Disease Models, Animal ; Pancreas ; Pancreatitis/chemically induced ; Pancreatitis/drug therapy ; Pancreatitis/genetics ; Trypsin/genetics ; Trypsinogen/genetics
Chemical Substances	Dabigatran (I0VM4M70GC) ; Trypsin (EC 3.4.21.4) ; Trypsinogen (9002-08-8)
Language	English
Publishing date	2022-11-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.161145
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Article ; Online: No evidence for the benefit of PPIs in the treatment of acute pancreatitis: a systematic review and meta-analysis.

Horváth, István László / Bunduc, Stefania / Hankó, Balázs / Kleiner, Dénes / Demcsák, Alexandra / Szabó, Bence / Hegyi, Péter / Csupor, Dezső

Scientific reports

2023 Volume 13, Issue 1, Page(s) 2791

Abstract: Although current guidelines do not recommend the use of proton pump inhibitors (PPIs) in the standard of care of acute pancreatitis (AP), they are often prescribed in clinical practice, mainly for ulcer stress prophylaxis. In this systematic review and ... ...

Abstract	Although current guidelines do not recommend the use of proton pump inhibitors (PPIs) in the standard of care of acute pancreatitis (AP), they are often prescribed in clinical practice, mainly for ulcer stress prophylaxis. In this systematic review and meta-analysis we evaluated the association between the use of PPIs in the management of AP and various clinical outcomes. We conducted the systematic research in six databases without restrictions on January 24th, 2022. We investigated adult patient with AP, who were treated with PPI compared to conventional therapy. The pooled odds ratios, mean differences, and corresponding 95% confidence intervals were calculated with random effect model. We included six RCTs and three cohort studies, consisting of 28,834 patients. We found a significant decrease in the rate of pancreatic pseudocyst formation in patients who received PPI treatment. PPI use was associated with a higher risk of GI bleeding, however this finding could be due to the patients' comorbid conditions. We found no significant difference in the rates of 7-day mortality, length of hospital stay, and acute respiratory distress syndrome between the groups. The available data on this topic are limited; therefore, further well designed RCTs are needed to evaluate the potential benefits and adverse effects of PPIs in AP.
MeSH term(s)	Adult ; Humans ; Proton Pump Inhibitors/adverse effects ; Acute Disease ; Pancreatitis/drug therapy ; Peptic Ulcer/drug therapy ; Gastrointestinal Hemorrhage/drug therapy
Chemical Substances	Proton Pump Inhibitors
Language	English
Publishing date	2023-02-16
Publishing country	England
Document type	Meta-Analysis ; Systematic Review ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-023-29939-5
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Article ; Online: Engineering mouse cationic trypsinogen for rapid and selective activation by cathepsin B.

Demcsák, Alexandra / Geisz, Andrea / Sahin-Tóth, Miklós

Scientific reports

2019 Volume 9, Issue 1, Page(s) 9188

Abstract: Intra-pancreatic activation of trypsin is an early event in pancreatitis. Trypsinogen can be activated to trypsin either through autoactivation (trypsin-mediated trypsinogen activation) or by the lysosomal protease cathepsin B (CTSB). Experimental ... ...

Abstract	Intra-pancreatic activation of trypsin is an early event in pancreatitis. Trypsinogen can be activated to trypsin either through autoactivation (trypsin-mediated trypsinogen activation) or by the lysosomal protease cathepsin B (CTSB). Experimental separation of CTSB-mediated activation from autoactivation in mice is possible through knocking in mutations that render trypsinogen sensitive to CTSB but resistant to trypsin. Here we present biochemical studies on novel mouse cationic trypsinogen (isoform T7) mutants engineered for selective CTSB activation. First, we demonstrated that mutation K24G, which alters the activation site Lys in T7 trypsinogen, abolished autoactivation while activation by CTSB was stimulated 4-fold at pH 4.0. Interestingly, CTSB-mediated activation of the K24G mutant became more sensitive to inhibition by increasing pH. Next, Ala-scanning of the five Asp residues preceding the activation site Lys revealed that mutation D22A accelerated CTSB-mediated activation by 2-fold. Finally, combination of mutations D22A and K24G resulted in a trypsinogen mutant that exhibited 14-fold increased activation by CTSB and normal pH sensitivity. We conclude that we successfully engineered a mouse T7 trypsinogen mutant (D22A,K24G), which is robustly activated by CTSB but cannot undergo autoactivation. These studies set the stage for the generation of a preclinical mouse model of CTSB-dependent pancreatitis.
MeSH term(s)	Animals ; Cathepsin B/metabolism ; Cathepsin L/metabolism ; Enzyme Activation ; Humans ; Liver/metabolism ; Mice ; Mutation ; Protein Engineering ; Trypsinogen/genetics ; Trypsinogen/metabolism
Chemical Substances	Trypsinogen (9002-08-8) ; CTSB protein, human (EC 3.4.22.1) ; Cathepsin B (EC 3.4.22.1) ; Ctsb protein, mouse (EC 3.4.22.1) ; CTSL protein, human (EC 3.4.22.15) ; Cathepsin L (EC 3.4.22.15)
Language	English
Publishing date	2019-06-24
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-019-45631-z
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Article ; Online: Measuring digestive protease activation in the mouse pancreas.

Mosztbacher, Dóra / Demcsák, Alexandra / Sahin-Tóth, Miklós

Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.

2019 Volume 20, Issue 2, Page(s) 288–292

Abstract: Intrapancreatic activation of digestive proteases, trypsin and chymotrypsin in particular, is a hallmark of pancreatitis. In experimental rodent models, protease activation is routinely measured from pancreatic homogenates using fluorogenic peptide ... ...

Abstract	Intrapancreatic activation of digestive proteases, trypsin and chymotrypsin in particular, is a hallmark of pancreatitis. In experimental rodent models, protease activation is routinely measured from pancreatic homogenates using fluorogenic peptide substrates. Here we investigated the optimal conditions for the determination of intrapancreatic trypsin and chymotrypsin activation elicited by a single intraperitoneal injection of cerulein in C57BL/6N mice. We found that these protease assays were significantly improved by using lower amounts of pancreatic homogenate and exclusion of bovine serum albumin from the assay buffer. Furthermore, pancreatic homogenates had to be freshly prepared and assayed; as freezing and thawing stimulated protease activation. Finally, replacement of the widely used Boc-Gln-Ala-Arg-AMC trypsin substrate with Z-Gly-Pro-Arg-AMC reduced the background activity in saline-treated control mice and thereby increased the extent of cerulein-induced trypsin activation. Using the optimized protocol, we reproducibly measured 20-fold and 200-fold increases in the intrapancreatic trypsin and chymotrypsin activity, respectively, in mice given cerulein.
MeSH term(s)	Animals ; Ceruletide/pharmacology ; Chymotrypsin/metabolism ; Enzyme Activation ; Female ; Male ; Mice ; Mice, Inbred C57BL ; Pancreas/enzymology ; Pancreatitis/chemically induced ; Pancreatitis/enzymology ; Peptide Hydrolases/analysis ; Serum Albumin, Bovine/pharmacology ; Sodium Chloride/pharmacology ; Trypsin/metabolism
Chemical Substances	Serum Albumin, Bovine (27432CM55Q) ; Sodium Chloride (451W47IQ8X) ; Ceruletide (888Y08971B) ; Peptide Hydrolases (EC 3.4.-) ; Chymotrypsin (EC 3.4.21.1) ; Trypsin (EC 3.4.21.4)
Language	English
Publishing date	2019-12-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2056680-3
ISSN	1424-3911 ; 1424-3903
ISSN (online)	1424-3911
ISSN	1424-3903
DOI	10.1016/j.pan.2019.12.020
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Article ; Online: Defective binding of SPINK1 variants is an uncommon mechanism for impaired trypsin inhibition in chronic pancreatitis.

Szabó, András / Toldi, Vanda / Gazda, Lívia Diána / Demcsák, Alexandra / Tőzsér, József / Sahin-Tóth, Miklós

The Journal of biological chemistry

2021 Volume 296, Page(s) 100343

Abstract: The serine protease inhibitor Kazal type 1 (SPINK1) protects the pancreas from intrapancreatic trypsin activation that can lead to pancreatitis. Loss-of-function genetic variants of SPINK1 increase the risk for chronic pancreatitis, often by diminishing ... ...

Abstract	The serine protease inhibitor Kazal type 1 (SPINK1) protects the pancreas from intrapancreatic trypsin activation that can lead to pancreatitis. Loss-of-function genetic variants of SPINK1 increase the risk for chronic pancreatitis, often by diminishing inhibitor expression or secretion. Variants that are secreted normally have been presumed to be pathogenic because of defective trypsin inhibition, but evidence has been lacking. Here, we report quantitative studies on the inhibition of human trypsins by wildtype SPINK1 and seven secreted missense variants. We found that tyrosine sulfation of human trypsins weakens binding of SPINK1 because of altered interactions with Tyr43 in the SPINK1 reactive loop. Using authentic sulfated human trypsins, we provide conclusive evidence that SPINK1 variants N34S, N37S, R65Q, and Q68R have unimpaired inhibitory activity, whereas variant P55S exhibits a small and clinically insignificant binding defect. In contrast, rare variants K41N and I42M that affect the reactive-site peptide bond of SPINK1 decrease inhibitor binding by 20,000- to 30,000-fold and three- to sevenfold, respectively. Taken together, the observations indicate that defective trypsin inhibition by SPINK1 variants is an uncommon mechanism in chronic pancreatitis. The results also strengthen the notion that a decline in inhibitor levels explains pancreatitis risk associated with the large majority of SPINK1 variants.
MeSH term(s)	HEK293 Cells ; Humans ; Models, Molecular ; Mutation, Missense ; Pancreatitis, Chronic/genetics ; Pancreatitis, Chronic/metabolism ; Protein Binding ; Trypsin/metabolism ; Trypsin Inhibitor, Kazal Pancreatic/genetics ; Trypsin Inhibitor, Kazal Pancreatic/metabolism
Chemical Substances	SPINK1 protein, human ; Trypsin Inhibitor, Kazal Pancreatic (50936-63-5) ; Trypsin (EC 3.4.21.4)
Language	English
Publishing date	2021-01-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.100343
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