Activation of protein phosphatase 2A is responsible for increased content and inactivation of respiratory chain complex i induced by all-trans retinoic acid in human keratinocytes

F Papa; N Sardaro; R Lippolis; D Panelli; S Scacco

Activation of protein phosphatase 2A is responsible for increased content and inactivation of respiratory chain complex i induced by all-trans retinoic acid in human keratinocytes

J Biol Regul Homeost Agents. 2016 Apr-Jun;30(2):389-98.

Authors

F Papa¹, N Sardaro¹, R Lippolis², D Panelli¹, S Scacco¹

Affiliations

¹ Department of Basic Medical Sciences, Neurosciences and Sense Organs. University of Bari Aldo Moro, Bari, Italy.
² Institute of Bioenergetics and Biomembranes (IBBE) of the Italian National Council of Researches (CNR), Bari, Italy.

PMID: 27358125

Abstract

This study presents the effect of all-trans retinoic acid (ATRA) on cell growth and respiratory chain complex I in human keratinocyte cultures. Keratinocyte treatment results in increased level of GRIM-19 and other subunits of complex I, in particular of their carbonylated forms, associated with inhibition of its enzymatic activity. The results show that in keratinocytes ATRA-promoted phosphatase activity controls the proteostasis and activity of complex I.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Apoptosis Regulatory Proteins / analysis
Cells, Cultured
Electron Transport Complex I / analysis
Electron Transport Complex I / drug effects*
Humans
Keratinocytes / drug effects*
Keratinocytes / metabolism
NADH, NADPH Oxidoreductases / analysis
Protein Phosphatase 2 / physiology*
Tretinoin / pharmacology*

Substances

Apoptosis Regulatory Proteins
Tretinoin
NADH, NADPH Oxidoreductases
NDUFA13 protein, human
Protein Phosphatase 2
Electron Transport Complex I