Growth Inhibition, Morphological Change, and Ectoenzyme Release of LLC-PK1 Cells by Phosphatidylinositol-specific Phospholipase C ofBacillus thuringiensis
Author(s) -
Chisako Itami,
Yukio Kimura,
Ryo Taguchi,
Hiroh Ikezawa,
Toshikatsu Nakabayashi
Publication year - 1997
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.61.776
Subject(s) - phospholipase c , phosphatidylinositol , bacillus thuringiensis , alkaline phosphatase , pi , biochemistry , biology , cell growth , cell , cell culture , phosphodiesterase , microbiology and biotechnology , enzyme , bacteria , signal transduction , genetics
Phosphatidylinositol-specific phospholipase C (PI-PLC) from Bacillus thuringiensis added to a culture of LLC-PK1 cells inhibited cell growth by 40%. In contrast with normal cells, the cells cultured in the presence of PI-PLC showed needle-like appendages which seemed to have been formed due to portions of the cell remaining adhered to the culture dish as the cell shrank. When LLC-PK1 cells were treated with PI-PLC, significant amounts of alkaline phosphatase and alkaline phosphodiesterase I were released specifically from the apical surface of the LLC-PK1 cells. Furthermore, PI-PLC treatment caused a delay of enzyme production and dome formation. These data indicate that glycosyl-phosphatidylinositol (GPI)-anchored proteins on the surface of LLC-PK1 cells are important in cell growth and differentiation. Also, the combined use of LLC-PK1 cells and PI-PLC of B. thuringiensis is effective for investigating the function of GPI-anchor proteins.
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