Preclinical study demonstrates transcellular absorption and persistent IgE reactivity of parvalbumin in mice, highlighting mechanisms driving potent fish allergenicity.
Key Points
To evaluate the digestion-dependent changes in IgE reactivity and in vivo intestinal transport of parvalbumin across three fish species to clarify the mechanisms of its strong allergenicity.
Assessed in vitro enzymatic digestion of parvalbumin from salmon, flounder, and herring using pepsin-trypsin and measured the IgE reactivity of resulting fragments.
Evaluated in vivo gastrointestinal digestion, intestinal retention, and epithelial transport into venous blood following oral administration of parvalbumin in mice.
In vitro pepsin-trypsin cleavage rapidly degraded parvalbumin into low-molecular-weight fragments that retained substantial IgE reactivity.
Orally administered parvalbumin persisted in the mouse small intestine and was rapidly absorbed into the venous bloodstream via transcellular transport through intestinal epithelial cells across all three species.