Disease relevance of AOC3

• Anti-tumoral effect of native and immobilized bovine serum amine oxidase in a mouse melanoma model [1].
• The effect of hyperthermia on cytotoxicity of spermine oxidized by purified bovine serum amine oxidase was investigated in Chinese hamster ovary cells [2].
• Contribution of serum and cellular semicarbazide-sensitive amine oxidase to amine metabolism and cardiovascular toxicity [3].
• Bovine SAO enhanced K+ channel currents in N1E-115 neuroblastoma cells in a time-dependent manner [4].

Psychiatry related information on AOC3

• Overexpression of semicarbazide sensitive amine oxidase in the cerebral blood vessels in patients with Alzheimer's disease and cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy [5].

High impact information on AOC3

• A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase [6].
• A full-length clone (2.7 kilobase pairs) for bovine serum amine oxidase was subsequently obtained through screening of the same cDNA library with the amplified 0.7-kilobase pair cDNA [7].
• Such stereospecificity and proton exchange uniquely differentiates lysyl oxidase from all but an aortic semicarbazide-sensitive amine oxidase among the pro-S-specific copper-dependent amine oxidases analyzed thus far [8].
• The recently discovered organic cofactor of bovine serum amine oxidase, topa quinone, is an uncommon amino acid residue in the polypeptide backbone (Janes, S. M., Mu, D., Wemmer, D., Smith, A. J., Kaur, S., Maltby, D., Burlingame, A. L., and Klinman, J. P. (1990) Science 248, 981-987) [9].
• The dopa-containing vitelline proteins and the 6-hydroxydopa-containing bovine serum amine oxidase are stained with the nitroblue tetrazolium/glycinate reagent [10].

Chemical compound and disease context of AOC3

• Allylamine-induced vascular toxicity in vitro: prevention by semicarbazide-sensitive amine oxidase inhibitors [11].

Biological context of AOC3

• The nucleotide sequence of this cDNA was found to be different from that of the previously published liver cDNA encoding bovine serum amine oxidase, another copper amine oxidase [12].
• An active site, cofactor-containing peptide has been obtained in high yield from bovine serum amine oxidase [6].
• Electrostatic control of oxidative deamination catalysed by bovine serum amine oxidase [13].
• Thermolytic digestion of porcine SSAO gave two cofactor-containing peptides that contained a TPQ consensus sequence, Asn-X-Asp-Tyr-Tyr, where X is a blank cycle corresponding to TPQ [14].
• SSAO obtained from bovine serum was relatively insensitive to MDL-72974A (IC50 = 3 x 10(-7) M [15].

Anatomical context of AOC3

• Time-dependent activation of the semicarbazide-sensitive amine oxidase (SSAO) from ox lung microsomes [16].
• These results definitively confirm the presence of SSAO in human and bovine cerebrovascular tissues and they demonstrate for the first time, the presence of this amine oxidase in endothelial cells from microvessels, through biochemical and immunological approaches [17].
• The IC50 values were estimated to be 2 x 10(-9) M, 5 x 10(-9) M, 8 x 10(-8) M and 2 x 10(-8) M for SSAO from dog aorta, rat aorta, bovine aorta and human umbilical artery, respectively [15].
• We have investigated the presence of SSAO in human and bovine brain microvessels by biochemical and immunohistological techniques, and we have compared it with SSAO present in meninges from the same species [17].
• SSAO activity towards dopamine was present in the choroid and the retina, but not in the iris or the optic nerve [18].

Associations of AOC3 with chemical compounds

• In a similar manner, alignment of a tryptic peptide from bovine serum amine oxidase implicates tyrosine as the precursor to topa quinone in mammals [9].
• Anaerobic, rapid-scanning stopped-flow spectroscopy has been used to investigate the UV-visible absorbance changes (300-540 nm) that occur in the spectrum of bovine serum amine oxidase during reduction by benzylamine, p-hydroxybenzylamine, and p-methoxybenzylamine [19].
• The ionic-strength-dependence of steady-state kinetic parameters (kc and Km') for non-biogenic (benzylamine, butylamine) and biogenic (spermine, spermidine) amines has been measured in the bovine serum amine oxidase reaction [13].
• Extensive digestion of SSAO enzymes, and of porcine kidney diamine oxidase, with pronase E yielded species with identical chromophoric properties characteristic of the dipeptide, TPQ(p-NPH)-Asp [14].
• The reactivity of SSAO with semicarbazide and phenylhydrazine suggests that the cofactor is a carbonyl type molecule [20].

Regulatory relationships of AOC3

• Cytotoxicity caused by bovine serum amine oxidase (5.7 x 10(-3) U/mL) and spermine (340 microM) was completely inhibited by catalase only during short incubation times after which time cytotoxicity occurred [21].

Other interactions of AOC3

• Interaction of bovine serum amine oxidase with the polyamine oxidase inactivator MDL 72527 [22].
• We investigated a new strategy to overcome multidrug resistance, using purified bovine serum amine oxidase, which generates two major toxic products from the polyamine spermine [23].

Analytical, diagnostic and therapeutic context of AOC3

• Following protocols established with bovine serum amine oxidase, yeast amine oxidase was derivatized with [14C]phenylhydrazine, followed by thermolytic digestion and isolation of a dominant radiolabeled peptide by high pressure liquid chromatography [9].
• Analysis of the thermal unfolding of bovine serum amine oxidase by differential scanning calorimetry reveals for the dimeric protein a four domain structure consisting of two sets of domains [24].
• We investigated the role of SSAO as a component of cell culture medium (through addition of fetal calf serum (FCS)) compared to intracellular SSAO in the in vitro cytotoxicity of three amines and metabolites [3].
• Serum amine oxidase can specifically recognize and oxidize aminohexyl (AH) chains on AH-Sepharose support: single-step affinity immobilization [25].
• Preparative affinity chromatography of bovine serum amine oxidase (SAO) on aminohexyl (AH)-Sepharose was often associated with an unexpected irreversible SAO retention on the support [25].

References