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Prodigiosin 25‐C uncouples vacuolar type H + ‐ATPase, inhibits vacuolar acidification and affects glycoprotein processing
Author(s) -
Kataoka Takao,
Muroi Makoto,
Ohkuma Shoji,
Waritani Takaki,
Magae Junji,
Takatsuki Akira,
Kondo Shunzo,
Yamasaki Makari,
Nagai Kazuo
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01446-8
Subject(s) - prodigiosin , bafilomycin , acridine orange , atpase , biochemistry , chemistry , proton pump , golgi apparatus , v atpase , vacuole , mitochondrion , microbiology and biotechnology , biology , cytoplasm , enzyme , endoplasmic reticulum , escherichia coli , apoptosis , autophagy , serratia marcescens , gene
Prodigiosin 25‐C inhibited the accumulation of 3‐(2,4‐dinitroanilino)‐3′‐amino‐ N ‐methyldipropylamine and acridine orange in the acidic compartments of baby hamster kidney cells with little perturbation of cellular ATP levels. In rat liver lysosomes, prodigiosin 25‐C inhibited the proton pump activity with an IC 50 of approximately 30 nM, but did not affect ATPase activity up to 1 μM. It also delayed the transport of vesicular stomatitis virus G protein and induced a drastic swelling of Golgi apparatus and mitochondria. These results indicate that prodigiosin 25‐C raises the pH of acidic compartments through inhibition of the proton pump activity of vacuolar type H + ‐ATPase, thereby causing the functional and morphological changes to the Golgi apparatus.