Abstract
The mechanisms for tight-junction (TJ) stabilization by β-lactoglobulin (β-Lg) were studied. Treatment of Caco-2-SF cells with inhibitors for some enzymes in the intracellular signal transduction pathways and a cytoskeleton-disturbing agent (cytochalasin D) reduced the TJ-stabilizing activity of β-Lg. So β-Lg is suggested to modulate the cytoskeletal structure through the activation of phospholipase C and protein kinase C, resulting in the TJ st. © 1998, Taylor & Francis Group, LLC. All rights reserved.
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Hashimoto, K., Nakayama, T., & Shimizu, M. (1998). Effects of β-lactoglobulin on the tight-junctional stability of Caco-2-SF monolayer. Bioscience, Biotechnology and Biochemistry, 62(9), 1819–1821. https://doi.org/10.1271/bbb.62.1819
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