ADP-ribosylation of the rho rac proteins induces growth inhibition, neurite outgrowth and acetylcholine esterase in cultured PC-12 cells

Teiichi Nishiki; Shuh Narumiya; Narito Morii; Masamitsu Yamamoto; Motohatsu Fujiwara; Yoichi Kamata; Genji Sakaguchi; Shunji Kozaki

doi:10.1016/0006-291X(90)91760-P

ADP-ribosylation of the rho rac proteins induces growth inhibition, neurite outgrowth and acetylcholine esterase in cultured PC-12 cells

Teiichi Nishiki, Shuh Narumiya, Narito Morii, Masamitsu Yamamoto, Motohatsu Fujiwara, Yoichi Kamata, Genji Sakaguchi, Shunji Kozaki

Graduate School of Medicine Dentistry and Pharmaceutical Sciences

Research output: Contribution to journal › Article › peer-review

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Abstract

Botulinum ADP-ribosyltransferase C3 (C3 exoenzyme) was purified to homogeneity and added to cultured rat pheochromocytoma PC-12 cells. Incubation with this exoenzyme caused inhibition of cell growth and induced neurites as well as acetylcholine esterase in these cells. These changes were dependent on the amount of the enzyme added to the culture, which correlated with the in situ ADP-ribosylation of the rho rac proteins in the cells. Preincubation with a specific anti-C3 exoenzyme monoclonal antibody inhibited both the ADP-ribosyl-transferase activity and the neurite-inducing activity of the enzyme preparation. These results suggest that C3 exoenzyme affected the cellular function of the rho rac proteins by ADP-ribosylation to induce these changes in the cells.

Original language	English
Pages (from-to)	265-272
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	167
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(90)91760-P
Publication status	Published - Feb 28 1990

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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ADP-ribosylation of the rho rac proteins induces growth inhibition, neurite outgrowth and acetylcholine esterase in cultured PC-12 cells. / Nishiki, Teiichi; Narumiya, Shuh; Morii, Narito; Yamamoto, Masamitsu; Fujiwara, Motohatsu; Kamata, Yoichi; Sakaguchi, Genji; Kozaki, Shunji.

In: Biochemical and Biophysical Research Communications, Vol. 167, No. 1, 28.02.1990, p. 265-272.

Research output: Contribution to journal › Article › peer-review

Nishiki, T, Narumiya, S, Morii, N, Yamamoto, M, Fujiwara, M, Kamata, Y, Sakaguchi, G & Kozaki, S 1990, 'ADP-ribosylation of the rho rac proteins induces growth inhibition, neurite outgrowth and acetylcholine esterase in cultured PC-12 cells', Biochemical and Biophysical Research Communications, vol. 167, no. 1, pp. 265-272. https://doi.org/10.1016/0006-291X(90)91760-P

Nishiki, Teiichi ; Narumiya, Shuh ; Morii, Narito ; Yamamoto, Masamitsu ; Fujiwara, Motohatsu ; Kamata, Yoichi ; Sakaguchi, Genji ; Kozaki, Shunji. / ADP-ribosylation of the rho rac proteins induces growth inhibition, neurite outgrowth and acetylcholine esterase in cultured PC-12 cells. In: Biochemical and Biophysical Research Communications. 1990 ; Vol. 167, No. 1. pp. 265-272.

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abstract = "Botulinum ADP-ribosyltransferase C3 (C3 exoenzyme) was purified to homogeneity and added to cultured rat pheochromocytoma PC-12 cells. Incubation with this exoenzyme caused inhibition of cell growth and induced neurites as well as acetylcholine esterase in these cells. These changes were dependent on the amount of the enzyme added to the culture, which correlated with the in situ ADP-ribosylation of the rho rac proteins in the cells. Preincubation with a specific anti-C3 exoenzyme monoclonal antibody inhibited both the ADP-ribosyl-transferase activity and the neurite-inducing activity of the enzyme preparation. These results suggest that C3 exoenzyme affected the cellular function of the rho rac proteins by ADP-ribosylation to induce these changes in the cells.",

author = "Teiichi Nishiki and Shuh Narumiya and Narito Morii and Masamitsu Yamamoto and Motohatsu Fujiwara and Yoichi Kamata and Genji Sakaguchi and Shunji Kozaki",

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ADP-ribosylation of the rho rac proteins induces growth inhibition, neurite outgrowth and acetylcholine esterase in cultured PC-12 cells

Abstract

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