Effects of β-Lactoglobulin on the Tight-junctional Stability of Caco-2-SF Monolayer | Zendy

Kei Hashimoto | Zendy; Tsutomu Nakayama | Zendy; Makoto SHIMIZU | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Effects of β-Lactoglobulin on the Tight-junctional Stability of Caco-2-SF Monolayer

Author(s) -

Kei Hashimoto,

Tsutomu Nakayama,

Makoto SHIMIZU

Publication year - 1998

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.62.1819

Subject(s) - cytoskeleton , protein kinase c , microbiology and biotechnology , phospholipase c , caco 2 , chemistry , cytochalasin d , tight junction , signal transduction , biophysics , intracellular , cytochalasin b , phospholipase , enzyme , cell junction , biochemistry , biology , cell

The mechanisms for tight-junction (TJ) stabilization by beta-lactoglobulin (beta-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 beta-Lg. So beta-Lg is suggested to modulate the cytoskeletal structure through the activation of phospholipase C and protein kinase C, resulting in the TJ stabilization.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research