Loss-of-function variant in chymotrypsin like elastase 3B (CELA3B) is associated with non-alcoholic chronic pancreatitis.


Journal

Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.]
ISSN: 1424-3911
Titre abrégé: Pancreatology
Pays: Switzerland
ID NLM: 100966936

Informations de publication

Date de publication:
Sep 2022
Historique:
received: 20 02 2022
revised: 20 05 2022
accepted: 19 06 2022
pubmed: 1 7 2022
medline: 15 9 2022
entrez: 30 6 2022
Statut: ppublish

Résumé

Genetic alterations in digestive enzymes have been associated with chronic pancreatitis (CP). Recently, chymotrypsin like elastase 3B (CELA3B) emerged as a novel risk gene. Thus, we evaluated CELA3B in two European cohorts with CP. We analyzed all 8 CELA3B exons in 550 German non-alcoholic CP (NACP) patients and in 241 German controls by targeted DNA sequencing. In addition, we analyzed exons 6 and 7 by Sanger sequencing and the c.129+1G>A variant by melting curve analysis in 1078 further German controls. As replication cohort, we investigated up to 243 non-German European NACP patients and up to 1665 controls originating from Poland, Hungary, and Sweden. We assessed the cellular secretion and the elastase activity of recombinant CELA3B variants. In the German discovery cohort, we detected a splice-site variant in intron 2, c.129+1G>A, in 9/550 (1.64%) CP patients and in 5/1319 (0.38%) controls (P=0.007, OR=4.4, 95% CI=1.5-13.0). In the European replication cohort, this variant was also enriched in patients (9/178 [5.06%]) versus controls (13/1247 [1.04%]) (P=0.001, OR=5.1, 95% CI=2.1-12.0). We did not find the two previously reported codon 90 variants, p.R90C and p.R90L. Our data indicate that CELA3B is a susceptibility gene for CP. In contrast to previous reports suggesting that increased CELA3B activity is associated with CP risk, the splice-site variant identified here is predicted to cause diminished CELA3B expression. How reduced CELA3B function predisposes to pancreatitis remains to be elucidated.

Sections du résumé

BACKGROUND BACKGROUND
Genetic alterations in digestive enzymes have been associated with chronic pancreatitis (CP). Recently, chymotrypsin like elastase 3B (CELA3B) emerged as a novel risk gene. Thus, we evaluated CELA3B in two European cohorts with CP.
METHODS METHODS
We analyzed all 8 CELA3B exons in 550 German non-alcoholic CP (NACP) patients and in 241 German controls by targeted DNA sequencing. In addition, we analyzed exons 6 and 7 by Sanger sequencing and the c.129+1G>A variant by melting curve analysis in 1078 further German controls. As replication cohort, we investigated up to 243 non-German European NACP patients and up to 1665 controls originating from Poland, Hungary, and Sweden. We assessed the cellular secretion and the elastase activity of recombinant CELA3B variants.
RESULTS RESULTS
In the German discovery cohort, we detected a splice-site variant in intron 2, c.129+1G>A, in 9/550 (1.64%) CP patients and in 5/1319 (0.38%) controls (P=0.007, OR=4.4, 95% CI=1.5-13.0). In the European replication cohort, this variant was also enriched in patients (9/178 [5.06%]) versus controls (13/1247 [1.04%]) (P=0.001, OR=5.1, 95% CI=2.1-12.0). We did not find the two previously reported codon 90 variants, p.R90C and p.R90L.
CONCLUSIONS CONCLUSIONS
Our data indicate that CELA3B is a susceptibility gene for CP. In contrast to previous reports suggesting that increased CELA3B activity is associated with CP risk, the splice-site variant identified here is predicted to cause diminished CELA3B expression. How reduced CELA3B function predisposes to pancreatitis remains to be elucidated.

Identifiants

pubmed: 35773178
pii: S1424-3903(22)00453-7
doi: 10.1016/j.pan.2022.06.258
pmc: PMC9474678
mid: NIHMS1831800
pii:
doi:

Substances chimiques

Chymotrypsin EC 3.4.21.1
CELA3B protein, human EC 3.4.21.36
Pancreatic Elastase EC 3.4.21.36

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

713-718

Subventions

Organisme : NIDDK NIH HHS
ID : R01 DK058088
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK082412
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK117809
Pays : United States

Informations de copyright

Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors report no conflicts of interest.

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Auteurs

Andrea Tóth (A)

Pediatric Nutritional Medicine & Else Kröner-Fresenius-Centre for Nutritional Medicine (EKFZ), Technical University Munich (TUM), Freising, Germany.

Alexandra Demcsák (A)

Center for Exocrine Disorders, Department of Molecular and Cell Biology, Boston University, Henry M. Goldman School of Dental Medicine, Boston, MA, 02118, United States; Department of Surgery, University of California Los Angeles, Los Angeles, CA, 90095, United States.

Florence Zankl (F)

Pediatric Nutritional Medicine & Else Kröner-Fresenius-Centre for Nutritional Medicine (EKFZ), Technical University Munich (TUM), Freising, Germany.

Grzegorz Oracz (G)

Department of Gastroenterology, Hepatology, Feeding Disorders and Pediatrics, The Children's Memorial Health Institute, Warsaw, Poland.

Lara Sophie Unger (LS)

Pediatric Nutritional Medicine & Else Kröner-Fresenius-Centre for Nutritional Medicine (EKFZ), Technical University Munich (TUM), Freising, Germany.

Peter Bugert (P)

Institute of Transfusion Medicine and Immunology, Medical Faculty Mannheim, Heidelberg University, German Red Cross Blood Service of Baden-Württemberg, Mannheim, Germany.

Helmut Laumen (H)

Pediatric Nutritional Medicine & Else Kröner-Fresenius-Centre for Nutritional Medicine (EKFZ), Technical University Munich (TUM), Freising, Germany; Department of Internal Medicine I, Martin-Luther-University Halle-Wittenberg, Halle (Saale), Germany.

Andrea Párniczky (A)

Heim Pál National Pediatric Institute, Budapest, Hungary; Institute for Translational Medicine, Medical School, Szentágothai Research Center, University of Pécs, Pécs, Hungary; Center for Translational Medicine, Semmelweis University, Budapest, Hungary.

Péter Hegyi (P)

Institute for Translational Medicine, Medical School, Szentágothai Research Center, University of Pécs, Pécs, Hungary; Center for Translational Medicine, Semmelweis University, Budapest, Hungary; Division of Pancreatic Diseases, Heart and Vascular Center, Semmelweis University, Budapest, Hungary.

Jonas Rosendahl (J)

Department of Internal Medicine I, Martin-Luther-University Halle-Wittenberg, Halle (Saale), Germany.

Tomasz Gambin (T)

Department of Medical Genetics, Institute of Mother and Child, Warsaw, Poland; Institute of Computer Science, Warsaw University of Technology, Warsaw, Poland.

Rafał Płoski (R)

Department of Medical Genetics, Medical University of Warsaw, Warsaw, Poland.

Dorota Koziel (D)

Collegium Medicum, Jan Kochanowski University of Kielce, Poland.

Stanisław Gluszek (S)

Collegium Medicum, Jan Kochanowski University of Kielce, Poland.

Fredrik Lindgren (F)

Department of Pediatric, Karolinska University Hospital, Stockholm, Sweden.

J Matthias Löhr (JM)

Department of Clinical Science, Intervention and Technology, Karolinska Institutet, Stockholm, Sweden.

Miklós Sahin-Tóth (M)

Center for Exocrine Disorders, Department of Molecular and Cell Biology, Boston University, Henry M. Goldman School of Dental Medicine, Boston, MA, 02118, United States; Department of Surgery, University of California Los Angeles, Los Angeles, CA, 90095, United States.

Heiko Witt (H)

Pediatric Nutritional Medicine & Else Kröner-Fresenius-Centre for Nutritional Medicine (EKFZ), Technical University Munich (TUM), Freising, Germany.

Agnieszka Magdalena Rygiel (AM)

Department of Medical Genetics, Institute of Mother and Child, Warsaw, Poland.

Maren Ewers (M)

Pediatric Nutritional Medicine & Else Kröner-Fresenius-Centre for Nutritional Medicine (EKFZ), Technical University Munich (TUM), Freising, Germany. Electronic address: maren.ewers@tum.de.

Eszter Hegyi (E)

Center for Exocrine Disorders, Department of Molecular and Cell Biology, Boston University, Henry M. Goldman School of Dental Medicine, Boston, MA, 02118, United States; Institute for Translational Medicine, Medical School, Szentágothai Research Center, University of Pécs, Pécs, Hungary. Electronic address: eszter.hegyi@aok.pte.hu.

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