Proteomic analysis of post-nuclear supernatant fraction and percoll-purified membranes prepared from brain cortex of rats exposed to increasing doses of morphine

Ujcikova, Hana; Eckhardt, Adam; Kagan, Dmytro; Roubalova, Lenka; Svoboda, Petr

doi:10.1186/1477-5956-12-11

Table 1 Functional significance of proteins identified in PNS as altered by chronic morphine

From: Proteomic analysis of post-nuclear supernatant fraction and percoll-purified membranes prepared from brain cortex of rats exposed to increasing doses of morphine

Protein name	Change (dependence vs.control)	Subcellular localization	Functional category	Protein characterization - PNS
Guanine deaminase	Up-regulated	Cytoplasm	Metabolism	Purine metabolism, guanine degradation [13]
V-type proton ATP subunit B, brain isoform	Up-regulated	Cell membrane	Trafficking	ATP hydrolysis coupled proton transport, vacuolar acidification [14]
Protein disulfide-isomerase A3	Up-regulated	Endoplasmatic reticulum lumen	Cellular development and regulation	Up-regulation of this protein causes apoptotic cell death [15], alterations in its level were revealed during neurodegenerative processes [16]
Dihydropyrimidinase-related protein 2	Up-regulated	Cytoplasm	Neuronal development and regulation	Neuronal development and polarity [8], cone collapse and cell migration; one of major determinants in the control of oxidative stress [17]
N-ethylmaleimide sensitive fusion protein, isoform CRA_a	Up-regulated	Cytoplasm	Trafficking	ATP binding, regulating protein membrane trafficking, involved in vesicle priming [18]
Malate dehydrogenase, mitochondrial precursor	Up-regulated	Mitochondrion matrix	Metabolism	L-malate dehydrogenase activity, protein self-association; up-regulation of the mitochondrial malate dehydrogenase is caused by oxidative stress [19]
Glyceraldehyde-3-phosphate dehydrogenase	Up-regulated	Cytoplasm	Metabolism	Glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities; surprising role in apoptosis [20]; is known as a major target protein in oxidative stress [21]
Aldolase A	Up-regulated	Mitochondrion	Metabolism	Role in glycolysis and gluconeogenesis, scaffolding protein;potential role in regulating the free intracellular concentration of InsP3, and subsequently intracellular calcium dynamics[22, 23]; the expression of aldolase A may be regulated by chronic lithium administration [24]
Creatine kinase B-type	Down-regulated	Cytoplasm	Metabolism	Energy-related (skeletal muscle, heart, brain and spermatozoa), brain development [25]
Aconitate hydratase, mitochondrial precursor	Up-regulated	Mitochondrion	Metabolism	Isomerization of citrate to isocitrate via cis-aconitate;an iron-sulfur protein, the particular susceptibility to oxidative damage may be related to the iron-sulfur cluster [4Fe-4S]in its active site [26]

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