Effect of malonaldehyde cross-linking on the ability of shrimp tropomyosin to elicit the release of inflammatory mediators and cytokines from activated RBL-2H3 cells

Song, Yongna; Liu, Zhenxing; Gao, Qing; Pavase, Tushar Ramesh; Lin, Hong

doi:10.1002/jsfa.7637

Cited by 14 publications

(7 citation statements)

References 27 publications

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“…In general, the data indicate that TM oxidation may have significant effects on the suppression of the release of mediators related to allergic symptoms. This was in agreement with a previous study in which the treatment of TM with MDA decreased degranulation . The proposed explanation was that the response of RBL‐2H3 cells to the allergen by oxidation may be due to altered IgE epitopes on the surface of acrolein‐treated TM, hindering successful basophil degranulation.…”

Section: Resultssupporting

confidence: 92%

Allergenicity of acrolein‐treated shrimp tropomyosin evaluated using RBL‐2H3 cell and mouse model

Lin

Ahmed

et al. 2018

J Sci Food Agric

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Section: Resultssupporting

confidence: 92%

Allergenicity of acrolein‐treated shrimp tropomyosin evaluated using RBL‐2H3 cell and mouse model

Lin

Ahmed

et al. 2018

J Sci Food Agric

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“…Two additional studies have reported detection of tryptase in RBL‐2H3 cells (Small‐Howard & Turner, ; Song, Li, Gao, Pavase, & Lin, ). However, these two studies measured tryptase (via ELISA in Song et al and via substrate activity assay in Small‐Howard & Turner) within cell lysates, not from the supernatants of stimulated intact cells.…”

Section: Discussionmentioning

confidence: 99%

Searching for tryptase in the RBL‐2H3 mast cell model: Preparation for comparative mast cell toxicology studies with zebrafish

Shim

Kennedy

Weatherly

et al. 2018

J of Applied Toxicology

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Mast cells comprise a physiologically and toxicologically important cell type that is ubiquitous among species and tissues. Mast cells undergo degranulation, in which characteristic intracellular granules fuse with the plasma membrane and release many bioactive substances, such as enzymes β‐hexosaminidase and tryptase. Activity of mast cells in the toxicology model organism, zebrafish, has been monitored via tryptase release and cleavage of substrate N‐α‐benzoyl‐dl‐Arg‐p‐nitroanilide (BAPNA). An extensively used in vitro mast cell model for studying toxicant mechanisms is the RBL‐2H3 cell line. However, instead of tryptase, granule contents such as β‐hexosaminidase have usually been employed as RBL‐2H3 degranulation markers. To align RBL‐2H3 cell toxicological studies to in vivo mast cell studies using zebrafish, we aimed to develop an RBL‐2H3 tryptase assay. Unexpectedly, we discovered that tryptase release from RBL‐2H3 cells is not detectable, using BAPNA substrate, despite optimized assay that can detect as little as 1 ng tryptase. Additional studies performed with another substrate, tosyl‐Gly‐Pro‐Lys‐pNA, and with an enzyme‐linked immunosorbent assay, revealed a lack of tryptase protein released from stimulated RBL‐2H3 cells. Furthermore, none of the eight rat tryptase genes (Tpsb2, Tpsab1, Tpsg1, Prss34, Gzmk, Gzma, Prss29, Prss41) is expressed in RBL‐2H3 cells, even though all are found in RBL‐2H3 genomic DNA and even though β‐hexosaminidase mRNA is constitutively expressed. Therefore, mast cell researchers should utilize β‐hexosaminidase or another reliable marker for RBL‐2H3 degranulation studies, not tryptase. Comparative toxicity testing in RBL‐2H3 cells in vitro and in zebrafish mast cells in vivo will require use of a degranulation reporter different from tryptase.

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“…Furthermore, RBL‐2H3 cells were considered to evaluate food‐allergic hypersensitivity reactions (Song et al ., 2016). To evaluate the release of mediators and cytokines by sensitised cells, we used mouse TM‐specific serum to sensitise RBL‐2H3 cells and assay the allergenicity of shrimp TM after glycation by ribose treatment (Ahmed et al ., 2019).…”

Section: Discussionmentioning

confidence: 99%

“…The cells were cultured following the previous study (Song et al ., 2016). The mouse sera were provided in our group, which was acquired with the method of Ahmed et al .…”

Section: Methodsmentioning

confidence: 99%

Effect of the structure and potential allergenicity of glycated tropomyosin, the shrimp allergen

Ahmed

et al. 2022

Int J of Food Sci Tech

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The aim is to elucidate whether the structural changes of shrimp tropomyosin (TM) following ribose treatment affected its potential allergenicity. The structural changes of glycated TM were analysed by fluorescence, ultraviolet spectrum (UV), circular dichroism (CD) and liquid chromatography-tandem mass spectrometry (LC-MS/MS), and the changes in allergenicity were investigated by enzyme-linked immunosorbent assay (ELISA) and RBL-2H3 cell model. The result indicated that ribose could cause the conformational structural changes of TM. Moreover, the phenylalanine, isoleucine and DL-methionine residues were altered by ribose by LC-MS/MS analysis. These modified amino acids also appeared in the shrimp allergic epitopes region. Furthermore, the glycated TM (4000 mmol L À1 ribose) could significantly decrease the IgE-binding capacity and inhibit the release of cytokines and mediators from RBL-2H3 cells. These findings suggest that ribose-induced glycation could damage the allergic epitope of TM, decreasing the potential allergenicity and could be considered for alleviating TM-induced food allergy.

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Effect of malonaldehyde cross-linking on the ability of shrimp tropomyosin to elicit the release of inflammatory mediators and cytokines from activated RBL-2H3 cells

Abstract: Cross-linking strongly modulates the ability of shrimp tropomyosin to induce release of inflammatory cytokines and mediators from activated RBL-2H3 cells. © 2016 Society of Chemical Industry.

Cited by 14 publications

References 27 publications

Allergenicity of acrolein‐treated shrimp tropomyosin evaluated using RBL‐2H3 cell and mouse model

Allergenicity of acrolein‐treated shrimp tropomyosin evaluated using RBL‐2H3 cell and mouse model

Searching for tryptase in the RBL‐2H3 mast cell model: Preparation for comparative mast cell toxicology studies with zebrafish

Effect of the structure and potential allergenicity of glycated tropomyosin, the shrimp allergen

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