Open Access

ARTICLE

Identification of key pathways and gene expression in the activation of mast cells via calcium flux using bioinformatics analysis

by Xiaoyu Wang^1,2,#,*, Takeshi Yamamoto^2,#, Makoto Kadowaki², Yifu Yang¹

1 Laboratory of Immunology and Virology, Experiment Center for Science and Technology, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, China
2 Division of Gastrointestinal Pathophysiology, Institute of Natural Medicine, University of Toyama, Toyama, 9300194, Japan

* Address correspondence to: Xiaoyu Wang,
# These authors contributed equally to this work

(This article belongs to the Special Issue: New Insights in Biology of Depression: New Molecules and Approaches)

BIOCELL 2021, 45(2), 395-415. https://doi.org/10.32604/biocell.2021.012280

Received 23 June 2020; Accepted 15 October 2020; Issue published 19 February 2021

Abstract

Mast cells are the main effector cells in IgE-associated allergic disorders, and we have reported that mucosal mast cells (MMCs) play a more important role in the development of food allergy (FA). IgE with antigen or calcium ionophore stimulation can lead to the activation of MMCs via a calcium-dependent pathway. The purpose of the present study was to identify gene signatures with IgE/antigen (dinitrophenyl-bovine serum albumin, DNP-BSA) or calcium ionophore (A23187) on the activation of MMCs. Differentially expressed genes between the two types of samples were identified with microarray analysis. Gene ontology functional and pathway enrichment analyses of differentially expressed genes were performed using the database for annotation, visualization, and integrated discovery software. The results showed that IgE/antigen and A23187 could induce degranulation, increase vacuoles, and elevate the cytosolic calcium concentration in MMCs. Furthermore, GeneChip analysis showed that the same 134 mRNAs were altered with IgE/DNP-BSA and A23187, suggesting that DNP-BSA/IgE and A23187 affect the same signal pathway partly in degranulation. KEGG analysis showed that the data were enriched in NF-κB, TNF, MAPK, transcription factor activity, DNA binding, and nucleic acid binding, suggesting that activation of MMCs is a complex process. The results provide new insights on MMCs activation.

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