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Phytate hydrolysate induces circumferential F‐actin ring formation at cell–cell contacts by a Rho‐associated kinase‐dependent mechanism in colorectal cancer HT‐29 cells
Author(s) -
Suzuki Takuya,
Hara Hiroshi
Publication year - 2010
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.200900606
Subject(s) - myosin light chain kinase , rho associated protein kinase , myosin , chemistry , kinase , microbiology and biotechnology , phosphorylation , protein kinase c , protein kinase a , biochemistry , biology
Phytate (inositol hexa‐phosphate or IP6) possessing anticancer activity is hydrolyzed by phytase in intestinal microbes and the metabolites are distributed throughout the colon. Cellular circumferential F‐actin rings, which are involved in cell polarity and structure, are lost early during tumorigenesis. We investigated F‐actin ring formation by the phytate hydrolysate in colorectal cancer HT‐29 cells to explore the novel mechanisms underlying the phytate‐mediated anticancer function. The phytate hydrolysate, but not inositol or phytate, induced F‐actin ring formation with a peak at 10 min in the cells and was associated with phosphorylation of myosin regulatory light chain. F‐actin ring formation and myosin regulatory light chain phosphorylation by the phytate hydrolysate were suppressed by inhibitors of Rho‐associated kinase (ROCK), Janus kinase (JAK), c‐Jun N ‐terminal kinase (JNK), and protein kinase Cδ (PKCδ). Activation of ROCK and JAK, but not JNK or PKCδ, was observed at 10 min and/or earlier after stimulation with the phytate hydrolysate. Altogether, the phytate hydrolysate induces circumferential F‐actin ring formation through a ROCK‐dependent myosin II activation in the HT‐29 cells, which requires JAK activation and basal activities of JNK and PKC. Hydrolysis products of phytate in the intestine may contribute to anticancer function of phytate.