A novel enzyme with spermine oxidase properties in bovine liver mitochondria: Identification and kinetic characterization

Bonaiuto, Emanuela; Grancara, Silvia; Martinis, Pamela; Stringaro, Annarita; Colone, Marisa; Agostinelli, Enzo; Macone, Alberto; Stevanato, Roberto; Vianello, Fábio; Toninello, Antonio; Paolo, Maria Luisa Di

doi:10.1016/j.freeradbiomed.2015.01.001

Cited by 13 publications

(12 citation statements)

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“…Immunoblot analysis of mitochondrial fractions and immunogold electron microscopy observations of purified mitochondria unequivocally confirmed the presence of a protein immunodecorated by anti-spermine oxidase antibodies in the mitochondrial matrix. These findings indicated that the bovine liver mitochondrial matrix contains an enzyme belonging to the spermine oxidase class (Bonaiuto et al 2015). The observation that polyamines are transported in mitochondria by an energy-dependent mechanism ) thus reinforce the hypothesis that mitochondria contain the spermine catabolism enzyme.…”

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confidence: 71%

Polyamines and transglutaminases: future perspectives

Agostinelli

2016

Amino Acids

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Section: Editorialsupporting

confidence: 71%

Polyamines and transglutaminases: future perspectives

Agostinelli

2016

Amino Acids

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“…For discussing its physiological meaning it is to consider that spermine can exhibit a dual effect on mitochondria: induction or prevention of the phenomenon of mitochondrial permeability transition (MPT). In fact spermine can be oxidized in the cytoplasm by polyamine oxidase (PAO) and other amine oxidases, and in the mitochondrial matrix by mtSMO (Bonaiuto et al 2015). In both conditions the activity of these oxidases produces ROS causing an oxidative stress, with the oxidation of critical SH groups, that in the presence of Ca 2+ induce the MPT with the opening of the transition pore.…”

Section: Discussionmentioning

confidence: 99%

“…However, a very recent investigation that mitochondria constitutively contain an enzyme having spermine oxidase activity (mtSMO) (Bonaiuto et al 2015), supports the proposal that spermine may also behave as inducer of MPT. This should be due to the generation of reactive oxygen species (ROS) produced by spermine enzymatic oxidation catalyzed by mtSMO, that in the presence of Ca 2+ would induce MPT.…”

Section: Introductionmentioning

confidence: 86%

“…This should be due to the generation of reactive oxygen species (ROS) produced by spermine enzymatic oxidation catalyzed by mtSMO, that in the presence of Ca 2+ would induce MPT. It is to clarify that mtSMO, used in our study, has been characterized in mitochondria isolated from bovine liver (Bonaiuto et al 2015). However, preliminary results obtained in our laboratory have shown that this activity is also present in RLM (unpublished data).…”

Section: Introductionmentioning

confidence: 94%

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Spermine cycling in mitochondria is mediated by adenine nucleotide translocase activity: mechanism and pathophysiological implications

et al. 2016

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Spermine, besides to be transported in mitochondria by an energy dependent electrophoretic mechanism, can be also released by two different mechanisms. The first one is induced in deenergizing conditions by FCCP or antimycin A and it is mediated by an electroneutral exchange spermine protons. The second one takes place in energizing conditions during the activity of the adenine nucleotide translocase and is mediated by an electroneutral symport mechanism involving the efflux in co-transport of spermine and phosphate and the exchange of exogenous ADP with endogenous ATP. The triggering of this mechanism permits an alternating cycling of spermine across the mitochondrial membrane, that is spermine is transported or released by energized mitochondria in the absence or presence of ATP synthesis, respectively. The physiological implications of this cycling of spermine are related to the induction or prevention of mitochondrial permeability transition and, consequently, on apoptosis or its prevention.

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“…In particular, spermine can also flow from organelles by promoting the crossmembrane cycling which regulates the induction of MPT (Agostinelli et al 2010). Polyamines in cells are oxidized by cytosolic Agostinelli et al 2010) and mitochondrial amine oxidases (Stevanato et al 2011;Bonaiuto et al 2015) with the production of hydrogen peroxide and aminoaldehydes, both of which are involved in the induction and/or amplification of MPT. However, this phenomenon, which causes loss of the bioenergetic capacity of mitochondria, together with oxidative stress, is strongly inhibited by polyamines in isolated mitochondria ).…”

Section: Mitochondria As Targets Of "Mitochondrial Medicine"mentioning

confidence: 99%

Pathophysiological implications of mitochondrial oxidative stress mediated by mitochondriotropic agents and polyamines: the role of tyrosine phosphorylation

et al. 2015

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Mitochondria, once merely considered as the "powerhouse" of cells, as they generate more than 90 % of cellular ATP, are now known to play a central role in many metabolic processes, including oxidative stress and apoptosis. More than 40 known human diseases are the result of excessive production of reactive oxygen species (ROS), bioenergetic collapse and dysregulated apoptosis. Mitochondria are the main source of ROS in cells, due to the activity of the respiratory chain. In normal physiological conditions, ROS generation is limited by the anti-oxidant enzymatic systems in mitochondria. However, disregulation of the activity of these enzymes or interaction of respiratory complexes with mitochondriotropic agents may lead to a rise in ROS concentrations, resulting in oxidative stress, mitochondrial permeability transition (MPT) induction and triggering of the apoptotic pathway. ROS concentration is also increased by the activity of amine oxidases located inside and outside mitochondria, with oxidation of biogenic amines and polyamines. However, it should also be recalled that, depending on its concentration, the polyamine spermine can also protect against stress caused by ROS scavenging. In higher organisms, cell signaling pathways are the main regulators in energy production, since they act at the level of mitochondrial oxidative phosphorylation and participate in the induction of the MPT. Thus, respiratory complexes, ATP synthase and transition pore components are the targets of tyrosine kinases and phosphatases. Increased ROS may also regulate the tyrosine phosphorylation of target proteins by activating Src kinases or phosphatases, preventing or inducing a number of pathological states.

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A novel enzyme with spermine oxidase properties in bovine liver mitochondria: Identification and kinetic characterization

Cited by 13 publications

References 57 publications

Polyamines and transglutaminases: future perspectives

Polyamines and transglutaminases: future perspectives

Spermine cycling in mitochondria is mediated by adenine nucleotide translocase activity: mechanism and pathophysiological implications

Pathophysiological implications of mitochondrial oxidative stress mediated by mitochondriotropic agents and polyamines: the role of tyrosine phosphorylation

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