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  1. Article ; Online: Association analysis of CUZD1 variants in European chronic pancreatitis patients.

    Just, Anna / Thiel, Franziska G / Weiss, Frank Ulrich

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

    2023  Volume 23, Issue 8, Page(s) 1041–1042

    MeSH term(s) Humans ; Crohn Disease ; Pancreas ; Pancreatitis, Chronic/genetics ; Genetic Predisposition to Disease ; Membrane Proteins/genetics
    Chemical Substances CUZD1 protein, human ; Membrane Proteins
    Language English
    Publishing date 2023-10-13
    Publishing country Switzerland
    Document type Letter ; Comment
    ZDB-ID 2056680-3
    ISSN 1424-3911 ; 1424-3903
    ISSN (online) 1424-3911
    ISSN 1424-3903
    DOI 10.1016/j.pan.2023.10.007
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  2. Book ; Thesis: Evaluierung der Uteruskürettage mit und ohne Einsatz der Randallschen Polypen-Faßzange an der Universitätsfrauenklinik Erlangen in den Jahren 1983 und 1995

    Weiß, Frank

    2000  

    Author's details vorgelegt von Frank Weiß
    Language German
    Size 46 Bl., graph. Darst.
    Edition [Mikrofiche-Ausg.]
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Erlangen, Nürnberg, Univ., Diss., 2000
    HBZ-ID HT013307797
    Database Catalogue ZB MED Medicine, Health

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  3. Article ; Online: A rare PRSS1 p.S127C mutation is associated with chronic pancreatitis and causes misfolding-induced ER-stress.

    Thiel, Franziska / Reiser, Markus / Weiss, Frank Ulrich

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

    2022  Volume 22, Issue 8, Page(s) 1112–1119

    Abstract: Background: /Objectives: Sequence variants in several genes have been identified as being associated with an increased inherited risk to develop chronic pancreatitis (CP). In a genetic survey of a CP patient we identified in the PRSS1gene a new c.380C >  ...

    Abstract Background: /Objectives: Sequence variants in several genes have been identified as being associated with an increased inherited risk to develop chronic pancreatitis (CP). In a genetic survey of a CP patient we identified in the PRSS1gene a new c.380C > G sequence variation, giving rise to a non-synonymous p.S127C mutation. Functional studies were performed to analyze the associated pathophysiology of the variant.
    Methods: Following generation of an expression vector for the new PRSS1 variant we compared its expression, secretion and catalytic activity with already known PRSS1 risk variants in HEK 293T cells. The intracellular protein accumulation and induction of endoplasmic reticulum (ER)-stress was analyzed.
    Results: Prediction tool analysis indicated a probably deleterious effect of the p.S127C variant on protein function which was confirmed by detection of a secretion defect in HEK293T cells leading to intracellular protein accumulation. While protein misfolding was associated with reduced trypsin activity, the increased expression of BIP and presence of spliced XBP1 indicated that the p.S127C variant induces ER stress and activates the UPR signaling pathway.
    Conclusions: The disease mechanism of the PRSS1 p.S127C variant involves defective protein secretion and the induction of ER-stress due to accumulation of presumably misfolded trypsinogen within the ER. The new variant should be considered disease-causing with an incomplete penetrance. Our results confirm that in addition to dysregulated trypsin-activity or reduced fluid secretion, ER-stress induction is an important trigger for acinar cell damage and the development of recurrent or chronic pancreatic inflammation.
    MeSH term(s) Humans ; Trypsin/genetics ; Trypsin/metabolism ; HEK293 Cells ; Pancreatitis, Chronic/genetics ; Pancreatitis, Chronic/metabolism ; Trypsinogen/genetics ; Mutation
    Chemical Substances Trypsin (EC 3.4.21.4) ; Trypsinogen (9002-08-8) ; PRSS1 protein, human (EC 3.4.21.4)
    Language English
    Publishing date 2022-11-03
    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.2022.10.005
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  4. Article ; Online: Immune response mechanisms in acute and chronic pancreatitis: strategies for therapeutic intervention.

    Glaubitz, Juliane / Asgarbeik, Saeedeh / Lange, Rabea / Mazloum, Hala / Elsheikh, Hager / Weiss, Frank Ulrich / Sendler, Matthias

    Frontiers in immunology

    2023  Volume 14, Page(s) 1279539

    Abstract: Acute pancreatitis (AP) is one of the most common inflammatory diseases of the gastrointestinal tract and a steady rising diagnosis for inpatient hospitalization. About one in four patients, who experience an episode of AP, will develop chronic ... ...

    Abstract Acute pancreatitis (AP) is one of the most common inflammatory diseases of the gastrointestinal tract and a steady rising diagnosis for inpatient hospitalization. About one in four patients, who experience an episode of AP, will develop chronic pancreatitis (CP) over time. While the initiating causes of pancreatitis can be complex, they consistently elicit an immune response that significantly determines the severity and course of the disease. Overall, AP is associated with a significant mortality rate of 1-5%, which is caused by either an excessive pro-inflammation, or a strong compensatory inhibition of bacterial defense mechanisms which lead to a severe necrotizing form of pancreatitis. At the time-point of hospitalization the already initiated immune response is the only promising common therapeutic target to treat or prevent a severe disease course. However, the complexity of the immune response requires fine-balanced therapeutic intervention which in addition is limited by the fact that a significant proportion of patients is in danger of development or progress to recurrent and chronic disease. Based on the recent literature we survey the disease-relevant immune mechanisms and evaluate appropriate and promising therapeutic targets for the treatment of acute and chronic pancreatitis.
    MeSH term(s) Humans ; Acute Disease ; Pancreatitis, Chronic/therapy ; Disease Progression
    Language English
    Publishing date 2023-10-10
    Publishing country Switzerland
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2023.1279539
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  5. Article ; Online: IRAK3-mediated suppression of pro-inflammatory MyD88/IRAK signaling affects disease severity in acute pancreatitis.

    Thiel, Franziska G / Asgarbeik, Saeedeh / Glaubitz, Juliane / Wilden, Anika / Lerch, Markus M / Weiss, Frank Ulrich / Sendler, Matthias

    Scientific reports

    2023  Volume 13, Issue 1, Page(s) 10833

    Abstract: Acute pancreatitis (AP), which is characterized by self-digestion of the pancreas by its own prematurely activated digestive proteases, is a major reason for hospitalization. The autodigestive process causes necrotic cell death of pancreatic acinar cells ...

    Abstract Acute pancreatitis (AP), which is characterized by self-digestion of the pancreas by its own prematurely activated digestive proteases, is a major reason for hospitalization. The autodigestive process causes necrotic cell death of pancreatic acinar cells and the release of damage associated molecular pattern which activate macrophages and drive the secretion of pro-inflammatory cytokines. The MYD88/IRAK signaling pathway plays an important role for the induction of inflammatory responses. Interleukin-1 receptor associated kinase-3 (IRAK3) is a counter-regulator of this pathway. In this study, we investigated the role of MYD88/IRAK using Irak3-/- mice in two experimental animal models of mild and severe AP. IRAK3 is expressed in macrophages as well as pancreatic acinar cells where it restrains NFκB activation. Deletion of IRAK3 enhanced the migration of CCR2
    MeSH term(s) Animals ; Mice ; Acute Disease ; Adaptor Proteins, Signal Transducing/metabolism ; Ceruletide/adverse effects ; Disease Models, Animal ; Inflammation ; Mice, Inbred C57BL ; Myeloid Differentiation Factor 88/genetics ; Myeloid Differentiation Factor 88/metabolism ; Necrosis ; Pancreas/metabolism ; Pancreatitis/metabolism ; Patient Acuity ; Signal Transduction ; Systemic Inflammatory Response Syndrome
    Chemical Substances Adaptor Proteins, Signal Transducing ; Ceruletide (888Y08971B) ; Myeloid Differentiation Factor 88 ; Irak3 protein, mouse (EC 2.7.11.1)
    Language English
    Publishing date 2023-07-04
    Publishing country England
    Document type 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/s41598-023-37930-3
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  6. Article ; Online: Plasma renalase levels are associated with the development of acute pancreatitis.

    Wang, Melinda / Weiss, Frank Ulrich / Guo, Xiaojia / Kolodecik, Thomas / Bewersdorf, Jan Philipp / Laine, Loren / Lerch, Markus M / Desir, Gary / Gorelick, Fred S

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

    2023  Volume 23, Issue 2, Page(s) 158–162

    Abstract: Background/objectives: Severe acute pancreatitis is associated with significant morbidity and mortality. Identifying factors that affect the risk of developing severe disease could influence management. Plasma levels of renalase, an anti-inflammatory ... ...

    Abstract Background/objectives: Severe acute pancreatitis is associated with significant morbidity and mortality. Identifying factors that affect the risk of developing severe disease could influence management. Plasma levels of renalase, an anti-inflammatory secretory protein, dramatically decrease in a murine acute pancreatitis model. We assessed this response in hospitalized acute pancreatitis patients to determine if reduced plasma renalase levels occur in humans.
    Methods: Plasma samples were prospectively and sequentially collected from patients hospitalized for acute pancreatitis. Two forms of plasma renalase, native (no acid) and acidified, were measured by ELISA and RNLS levels were compared between healthy controls and patients with mild and severe disease (defined as APACHE-II score ≥7) using nonparametric statistical analysis.
    Results: Control (33) and acute pancreatitis (mild, 230 (76.7%) and severe, 70 (23.3%) patients were studied. Acidified RNLS levels were lower in pancreatitis patients: Control: 10.1 μg/ml, Mild 5.1 μg/ml, Severe 6.0 μg/ml; p < 0.001. Native RNLS levels were increased in AP: Control: 0.4 μg/ml, Mild 0.9 μg g/ml, Severe 1.2 μg/ml p < 0.001; those with severe AP trended to have higher native RNLS levels than those with mild disease (p = 0.056). In patients with severe AP, higher APACHE-II scores at 24 h after admission correlated with lower acid-sensitive RNLS levels on admission (r = -0.31, p = 0.023).
    Conclusion: Low plasma acidified RNLS levels, and increased native RNLS levels are associated with AP. Additional studies should assess the clinical correlation between plasma RNLS levels and AP severity and outcomes.
    MeSH term(s) Humans ; Animals ; Mice ; Pancreatitis/complications ; Severity of Illness Index ; Acute Disease ; Monoamine Oxidase ; Prognosis
    Chemical Substances renalase (EC 1.4.3.4.) ; Monoamine Oxidase (EC 1.4.3.4)
    Language English
    Publishing date 2023-01-03
    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.2023.01.001
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  7. Article ; Online: Initiation of acute pancreatitis in mice is independent of fusion between lysosomes and zymogen granules.

    Zierke, Lukas / John, Daniel / Gischke, Marcel / Tran, Quang Trung / Sendler, Matthias / Weiss, Frank Ulrich / Bornscheuer, Uwe T / Ritter, Christoph / Lerch, Markus M / Aghdassi, Ali A

    Cellular and molecular life sciences : CMLS

    2024  Volume 81, Issue 1, Page(s) 207

    Abstract: The co-localization of the lysosomal protease cathepsin B (CTSB) and the digestive zymogen trypsinogen is a prerequisite for the initiation of acute pancreatitis. However, the exact molecular mechanisms of co-localization are not fully understood. In ... ...

    Abstract The co-localization of the lysosomal protease cathepsin B (CTSB) and the digestive zymogen trypsinogen is a prerequisite for the initiation of acute pancreatitis. However, the exact molecular mechanisms of co-localization are not fully understood. In this study, we investigated the role of lysosomes in the onset of acute pancreatitis by using two different experimental approaches. Using an acinar cell-specific genetic deletion of the ras-related protein Rab7, important for intracellular vesicle trafficking and fusion, we analyzed the subcellular distribution of lysosomal enzymes and the severity of pancreatitis in vivo and ex vivo. Lysosomal permeabilization was performed by the lysosomotropic agent Glycyl-L-phenylalanine 2-naphthylamide (GPN). Acinar cell-specific deletion of Rab7 increased endogenous CTSB activity and despite the lack of re-distribution of CTSB from lysosomes to the secretory vesicles, the activation of CTSB localized in the zymogen compartment still took place leading to trypsinogen activation and pancreatic injury. Disease severity was comparable to controls during the early phase but more severe at later time points. Similarly, GPN did not prevent CTSB activation inside the secretory compartment upon caerulein stimulation, while lysosomal CTSB shifted to the cytosol. Intracellular trypsinogen activation was maintained leading to acute pancreatitis similar to controls. Our results indicate that initiation of acute pancreatitis seems to be independent of the presence of lysosomes and that fusion of lysosomes and zymogen granules is dispensable for the disease onset. Intact lysosomes rather appear to have protective effects at later disease stages.
    MeSH term(s) Animals ; Lysosomes/metabolism ; Pancreatitis/metabolism ; Pancreatitis/pathology ; Pancreatitis/genetics ; Cathepsin B/metabolism ; Cathepsin B/genetics ; Mice ; Secretory Vesicles/metabolism ; rab GTP-Binding Proteins/metabolism ; rab GTP-Binding Proteins/genetics ; rab7 GTP-Binding Proteins/metabolism ; Acute Disease ; Acinar Cells/metabolism ; Acinar Cells/pathology ; Trypsinogen/metabolism ; Trypsinogen/genetics ; Ceruletide ; Enzyme Precursors/metabolism ; Enzyme Precursors/genetics ; Mice, Inbred C57BL ; Mice, Knockout
    Chemical Substances Cathepsin B (EC 3.4.22.1) ; rab GTP-Binding Proteins (EC 3.6.5.2) ; rab7 GTP-Binding Proteins ; rab7 GTP-binding proteins, mouse ; Trypsinogen (9002-08-8) ; Ceruletide (888Y08971B) ; Enzyme Precursors
    Language English
    Publishing date 2024-05-06
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-024-05247-7
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  8. Article: Etiology and Risk Factors of Acute and Chronic Pancreatitis.

    Weiss, Frank Ulrich / Laemmerhirt, Felix / Lerch, Markus M

    Visceral medicine

    2019  Volume 35, Issue 2, Page(s) 73–81

    Abstract: Based on the recognition of common etiological and genetic risk factors, acute and chronic pancreatitis are increasingly regarded as a continuum of the same disease, with a significant overlap of clinical manifestations and phenotypes but distinct ... ...

    Abstract Based on the recognition of common etiological and genetic risk factors, acute and chronic pancreatitis are increasingly regarded as a continuum of the same disease, with a significant overlap of clinical manifestations and phenotypes but distinct morphological and imaging appearances. Recent population-based and cohort studies have found that tobacco smoke conveys a greater risk than immoderate alcohol consumption for the development of chronic pancreatitis, and hypertriglyceridemia has been identified as a risk factor for acute pancreatitis - even when plasma levels are only mildly elevated. Hereditary pancreatitis, in its autosomal dominant form, is associated with mutations in the cationic trypsinogen gene (
    Language English
    Publishing date 2019-03-13
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2850733-2
    ISSN 2297-475X ; 2297-4725
    ISSN (online) 2297-475X
    ISSN 2297-4725
    DOI 10.1159/000499138
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  9. Book ; Online ; Thesis: Untersuchung der Rolle von Cathepsin B Sequenzvarianten als Risikofaktoren der chronischen Pankreatitis

    Ascholl, Theresa Sophie Verfasser] / [Weiß, Frank Ulrich [Akademischer Betreuer] / Lerch, Markus M. [Akademischer Betreuer] / Lerch, Markus M. [Gutachter] / Jaster, Robert [Gutachter]

    2023  

    Author's details Theresa Sophie Ascholl ; Gutachter: Markus M. Lerch, Robert Jaster ; Frank Ulrich Weiß, Markus M. Lerch
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language German
    Publisher Universität Greifswald
    Publishing place Greifswald
    Document type Book ; Online ; Thesis
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  10. Article ; Online: Genetic Analysis of the ATG16L1 c.898A>G (p.T300A) Variant in Acute and Chronic Pancreatitis.

    Neubauer, Claudia / Ewers, Maren / Schulz, Hans-Ulrich / Weiß, Frank Ulrich / Lämmerhirt, Felix / Lerch, Markus M / Bugert, Peter / Landt, Olfert / Algül, Hana / Rosendahl, Jonas / Witt, Heiko

    Pancreas

    2023  Volume 51, Issue 9, Page(s) 1231–1234

    Abstract: Objectives: Human and animal studies suggest an important role of autophagy in the pathogenesis of pancreatitis. ATG16L1 (autophagy-related 16 like 1) is part of a protein complex that is involved in the formation of autophagosomes. The c.898A > G (p ... ...

    Abstract Objectives: Human and animal studies suggest an important role of autophagy in the pathogenesis of pancreatitis. ATG16L1 (autophagy-related 16 like 1) is part of a protein complex that is involved in the formation of autophagosomes. The c.898A > G (p.T300A) variant of ATG16L1 is associated with Crohn disease. In this study, we analyzed ATG16L1 c.898A > G (p.T300A) for an association with pancreatitis.
    Methods: We genotyped 777 patients and 551 control subjects of German origin by melting curve analysis using fluorescence resonance energy transfer probes. The patient group included 429 patients with nonalcoholic chronic pancreatitis (CP), 141 patients with alcoholic CP, and 207 patients with acute pancreatitis (AP). We classified AP by severity according to the Atlanta symposium 1992.
    Results: Allele and genotype frequencies of ATG16L1 c.898A > G (p.T300A) did not differ significantly between patients and controls (G allele frequencies: nonalcoholic CP, 49.9%; alcoholic CP, 48.2%; AP, 49.5%; controls, 52.7%). We found no significant association with the severity of AP either.
    Conclusions: Our data do not support a role of ATG16L1 c.898A > G (p.T300A) in the pathogenesis of AP or CP or an influence on the severity of AP.
    MeSH term(s) Animals ; Humans ; Acute Disease ; Autophagy-Related Proteins/genetics ; Pancreatitis/genetics ; Crohn Disease ; Gene Frequency ; Genetic Predisposition to Disease ; Autophagy/genetics ; Polymorphism, Single Nucleotide
    Chemical Substances Autophagy-Related Proteins ; ATG16L1 protein, human
    Language English
    Publishing date 2023-04-20
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 632831-3
    ISSN 1536-4828 ; 0885-3177
    ISSN (online) 1536-4828
    ISSN 0885-3177
    DOI 10.1097/MPA.0000000000002177
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