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Proteomic Data in Morphine Addiction Versus Real Protein Activity: Metabolic Enzymes
Author(s) -
Antolak Anna,
BodzońKułakowska Anna,
Cetnarska Ewa,
Pietruszka Monika,
MarszałekGrabska Marta,
Kotlińska Jolanta,
Suder Piotr
Publication year - 2017
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.26085
Subject(s) - morphine , addiction , proteome , enzyme , abstinence , proteomics , mitochondrion , pharmacology , biology , chemistry , psychology , microbiology and biotechnology , biochemistry , neuroscience , psychiatry , gene
Drug dependence is an escalating problem worldwide and many efforts are being made to understand the molecular basis of addiction. The morphine model is widely used in these investigations. To date, at least 29 studies exploring the influence of morphine on mammals’ proteomes have been published. Among various proteins indicated as up‐ or down‐regulated, the expression changes of enzymes engaged in energy metabolism pathways have often been confirmed. To verify whether proteomics‐indicated alterations in enzyme levels reflect changes in their activity, four enzymes: PK, MDH, Complex I, and Complex V were investigated in morphine addiction and abstinence models. After analyses of the rat brain mitochondria fraction in the model of morphine dependence, we found that one of the investigated enzymes (pyruvate kinase) showed statistically significant differences observed between morphine, control, and abstinence groups. J. Cell. Biochem. 118: 4323–4330, 2017. © 2017 Wiley Periodicals, Inc.