Down-regulation of RalGTPase-Activating Protein Promotes Colitis-Associated Cancer via NLRP3 Inflammasome Activation.


Journal

Cellular and molecular gastroenterology and hepatology
ISSN: 2352-345X
Titre abrégé: Cell Mol Gastroenterol Hepatol
Pays: United States
ID NLM: 101648302

Informations de publication

Date de publication:
2020
Historique:
received: 23 10 2018
revised: 02 10 2019
accepted: 03 10 2019
pubmed: 18 10 2019
medline: 6 5 2021
entrez: 18 10 2019
Statut: ppublish

Résumé

Ral guanosine triphosphatase-activating protein α2 (RalGAPα2) is the major catalytic subunit of the negative regulators of the small guanosine triphosphatase Ral, a member of the Ras subfamily. Ral regulates tumorigenesis and invasion/metastasis of some cancers; however, the role of Ral in colitis-associated cancer (CAC) has not been investigated. We aimed to elucidate the role of Ral in the mechanism of CAC. We used wild-type (WT) mice and RalGAPα2 knockout (KO) mice that showed Ral activation, and bone marrow chimeric mice were generated as follows: WT to WT, WT to RalGAPα2 KO, RalGAPα2 KO to WT, and RalGAPα2 KO to RalGAPα2 KO mice. CAC was induced in these mice by intraperitoneal injection of azoxymethane followed by dextran sulfate sodium intake. Intestinal epithelial cells were isolated from colon tissues, and we performed complementary DNA microarray analysis. Cytokine expression in normal colon tissues and CAC was analyzed by quantitative polymerase chain reaction. Bone marrow chimeric mice showed that immune cell function between WT mice and RalGAPα2 KO mice was not significantly different in the CAC mechanism. RalGAPα2 KO mice had a significantly larger tumor number and size and a significantly higher proportion of tumors invading the submucosa than WT mice. Higher expression levels of matrix metalloproteinase-9 and matrix metalloproteinase-13 were observed in RalGAPα2 KO mice than in WT mice. The expression levels of interleukin 1β, NLRP3, apoptosis associated speck-like protein containing a CARD, and caspase-1 were apparently increased in the tumors of RalGAPα2 KO mice compared with WT mice. NLRP3 inhibitor reduced the number of invasive tumors. Ral activation participates in the mechanism of CAC development via NLRP3 inflammasome activation.

Sections du résumé

BACKGROUND & AIMS
Ral guanosine triphosphatase-activating protein α2 (RalGAPα2) is the major catalytic subunit of the negative regulators of the small guanosine triphosphatase Ral, a member of the Ras subfamily. Ral regulates tumorigenesis and invasion/metastasis of some cancers; however, the role of Ral in colitis-associated cancer (CAC) has not been investigated. We aimed to elucidate the role of Ral in the mechanism of CAC.
METHODS
We used wild-type (WT) mice and RalGAPα2 knockout (KO) mice that showed Ral activation, and bone marrow chimeric mice were generated as follows: WT to WT, WT to RalGAPα2 KO, RalGAPα2 KO to WT, and RalGAPα2 KO to RalGAPα2 KO mice. CAC was induced in these mice by intraperitoneal injection of azoxymethane followed by dextran sulfate sodium intake. Intestinal epithelial cells were isolated from colon tissues, and we performed complementary DNA microarray analysis. Cytokine expression in normal colon tissues and CAC was analyzed by quantitative polymerase chain reaction.
RESULTS
Bone marrow chimeric mice showed that immune cell function between WT mice and RalGAPα2 KO mice was not significantly different in the CAC mechanism. RalGAPα2 KO mice had a significantly larger tumor number and size and a significantly higher proportion of tumors invading the submucosa than WT mice. Higher expression levels of matrix metalloproteinase-9 and matrix metalloproteinase-13 were observed in RalGAPα2 KO mice than in WT mice. The expression levels of interleukin 1β, NLRP3, apoptosis associated speck-like protein containing a CARD, and caspase-1 were apparently increased in the tumors of RalGAPα2 KO mice compared with WT mice. NLRP3 inhibitor reduced the number of invasive tumors.
CONCLUSIONS
Ral activation participates in the mechanism of CAC development via NLRP3 inflammasome activation.

Identifiants

pubmed: 31622786
pii: S2352-345X(19)30139-0
doi: 10.1016/j.jcmgh.2019.10.003
pmc: PMC6957823
pii:
doi:

Substances chimiques

GTPase-Activating Proteins 0
Inflammasomes 0
NLR Family, Pyrin Domain-Containing 3 Protein 0
Nlrp3 protein, mouse 0
Ralgapa2 protein, mouse 0
ral GTP-Binding Proteins EC 3.6.5.2
Azoxymethane MO0N1J0SEN

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

277-293

Commentaires et corrections

Type : CommentIn

Informations de copyright

Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.

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Auteurs

Tomoya Iida (T)

Department of Gastroenterology and Hepatology, Sapporo Medical University School of Medicine, Sapporo, Japan.

Daisuke Hirayama (D)

Department of Gastroenterology and Hepatology, Sapporo Medical University School of Medicine, Sapporo, Japan.

Naoki Minami (N)

Department of Gastroenterology and Hepatology, Kyoto University Graduate School of Medicine, Kyoto, Japan.

Minoru Matsuura (M)

Department of Gastroenterology and Hepatology, Kyoto University Graduate School of Medicine, Kyoto, Japan.

Kohei Wagatsuma (K)

Department of Gastroenterology and Hepatology, Sapporo Medical University School of Medicine, Sapporo, Japan.

Kentaro Kawakami (K)

Department of Gastroenterology and Hepatology, Sapporo Medical University School of Medicine, Sapporo, Japan.

Kanna Nagaishi (K)

Second Department of Anatomy, Sapporo Medical University School of Medicine, Sapporo, Japan.

Masanori Nojima (M)

Center for Translational Research, The Institute of Medical Science Hospital, The University of Tokyo, Tokyo, Japan.

Hiroki Ikeuchi (H)

Division of Lower Gastrointestinal, Department of Surgery, Hyogo College of Medicine, Nishinomiya, Japan; Inflammatory Bowel Disease Center, Hyogo College of Medicine, Nishinomiya, Japan.

Seiichi Hirota (S)

Department of Surgical Pathology, Hyogo College of Medicine, Nishinomiya, Japan.

Ryutaro Shirakawa (R)

Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.

Hisanori Horiuchi (H)

Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.

Hiroshi Nakase (H)

Department of Gastroenterology and Hepatology, Sapporo Medical University School of Medicine, Sapporo, Japan. Electronic address: hiropynakase@gmail.com.

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Classifications MeSH