Amino Acids

, Volume 42, Issue 2, pp 441–450

Spermine oxidase: ten years after

  • Manuela Cervelli
  • Roberto Amendola
  • Fabio Polticelli
  • Paolo Mariottini
Minireview Article

DOI: 10.1007/s00726-011-1014-z

Cite this article as:
Cervelli, M., Amendola, R., Polticelli, F. et al. Amino Acids (2012) 42: 441. doi:10.1007/s00726-011-1014-z

Abstract

Spermine oxidase (SMO) was discovered much more recently than other enzymes involved in polyamine metabolism; this review summarizes 10 years of researches on this enzyme. Spermine oxidase (SMO) is a FAD-dependent enzyme that specifically oxidizes spermine (Spm) and plays a dominant role in the highly regulated mammalian polyamines catabolism. SMO participates in drug response, apoptosis, response to stressful stimuli and etiology of several pathological conditions, including cancer. SMO is a highly inducible enzyme, its deregulation can alter polyamine homeostasis, and dysregulation of polyamine catabolism is often associated with several disease states. The oxidative products of SMO activity are spermidine, and the reactive oxygen species H2O2 and the aldehyde 3-aminopropanal each with the potential to produce cellular damages and pathologies. The SMO substrate Spm is a tetramine that plays mandatory roles in several cell functions, such as DNA synthesis, cellular proliferation, modulation of ion channels function, cellular signaling, nitric oxide synthesis and inhibition of immune responses. The goal of this review is to cover the main biochemical, cellular and physiological processes in which SMO is involved.

Keywords

Spermine oxidase Spermine Gene expression Enzyme activity Inhibitors Differentiation Cancer Brain 

Abbreviations

AMPA

Alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid

AP

Aminopropanal

APAO

N1-acetylspermine oxidase

BC

Breat cancer

BENSpm

Bis(ethyl)norspermine

CPENSpm

N1-ethyl-N11-(cyclopropyl)-methyl-4,8-diazaundecane

ETBF

Enterotoxigenic Bacteroides fragilis

FAD

Flavin-adenine-dinucleotide

FMS1

Fenpropimorph resistance multicopy suppressor 1

Kir

Inward rectifier K+ channels

H2O2

Hydrogen peroxide

MDL 72527

N1,N4-bis(2,3-butadienyl)-1,4-butanediamine

NB

Neuroblastoma

NMDA

N-methyl-D-aspartate

ODC

Ornithine decarboxylase

PA

Polyamines

PC-Acro

Protein-conjugated acrolein

ROS

Reactive oxygen species

SBI

Silent brain infarction

Spd

Spermidine

SMO

Spermine oxidase

SMS

Spermine synthase

Spm

Spermine

SSAT

Spermidine/spermine N1-acetyltransferase

TBI

Traumatic brain injury

TNF-α

Tumor-necrosis factor-α

ZmPAO

Maize polyamine oxidase

Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  • Manuela Cervelli
    • 1
  • Roberto Amendola
    • 2
  • Fabio Polticelli
    • 1
    • 3
  • Paolo Mariottini
    • 1
  1. 1.Department of BiologyUniversity Roma TreRomeItaly
  2. 2.ENEA, CR CasacciaBAS.BIOTEC MEDRomeItaly
  3. 3.National Institute for Nuclear PhysicsRoma Tre SectionRomeItaly