The role of copper in bovine serum amine oxidase

1990 ◽  
Vol 3 (2) ◽  
pp. 114-117 ◽  
Author(s):  
Laura Morpurgo ◽  
Enzo Agostinelli ◽  
Bruno Mondov� ◽  
Luciana Avigliano
Keyword(s):  
Bovine Serum ◽  
Amine Oxidase

scholarly journals Electrostatic compared with hydrophobic interactions between bovine serum amine oxidase and its substrates

2003 ◽  
Vol 371 (2) ◽  
pp. 549-556 ◽  
Author(s):  
Maria Luisa DI PAOLO ◽  
Roberto STEVANATO ◽  
Alessandra CORAZZA ◽  
Fabio VIANELLO ◽  
Lorenzo LUNELLI ◽  
...  
Keyword(s):  
Active Site ◽  
Bovine Serum ◽  
Hydrophobic Interactions ◽  
Amine Oxidase ◽  
Amino Acid Residues ◽  
Deprotonated Form ◽  
Steady State Kinetic ◽  
Wide Range ◽  
Order Of Magnitude

A steady-state kinetic study of bovine serum amine oxidase activity was performed, over a wide range of pH values (5.4–10.2) and ionic strength (10–200mM), using various (physiological and analogue) substrates as specific probes of the active-site binding region. Relatively small changes in kcat values (approx. one order of magnitude) accompanied by marked changes in Km and kcat/Km values (approx. six orders of magnitude) were observed. This behaviour was correlated with the presence of positively charged groups or apolar chains in the substrates. In particular, it was found that the docking of the physiological polyamines, i.e. spermidine and spermine, appears to be modulated by three amino acid residues of the active site, which we have named L-H+, G-H+ and IH+, characterized by pKa values of 6.2±0.2 [Di Paolo, Scarpa, Corazza, Stevanato and Rigo (2002) Biophys. J. 83, 2231–2239], 8.2±0.3 and 7.8±0.4 respectively. The electrostatic interaction between the protonated substrates and the enzyme containing the residues L-H+, G-H+ and IH+ in the deprotonated form, the on/off role of the IH+ residue and the role of hydrophobic interactions with substrates characterized by apolar chains are discussed.

Aldehyde dehydrogenase and cytotoxicity of purified bovine serum amine oxidase and spermine in Chinese hamster ovary cells

1994 ◽  
Vol 72 (1-2) ◽  
pp. 36-42 ◽  
Author(s):  
Diana A. Averill-Bates ◽  
Enzo Agostinelli ◽  
Ewa Przybytkowski ◽  
Bruno Mondovi
Keyword(s):  
Hydrogen Peroxide ◽  
Aldehyde Dehydrogenase ◽  
Chinese Hamster Ovary ◽  
Bovine Serum ◽  
Amine Oxidase ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Oxidation Products ◽  
Ovary Cells

Bovine serum amine oxidase (EC 1.4.3.6) catalyses the oxidative deamination of polyamines giving rise to the corresponding aldehydes, ammonia, and hydrogen peroxide. It has been suggested that the dialdehyde produced during the oxidation of spermine subsequently undergoes spontaneous β-elimination to form acrolein. Oxidation of the aldehydes by aldehyde dehydrogenase (EC 1.2.1.5) thus eliminates these reactive species and prevents the formation of acrolein. This work studies the role of each of the oxidation products of spermine in cytotoxicity induced by purified bovine serum amine oxidase. The inhibition patterns of NAD-dependent aldehyde dehydrogenase and catalase against cytotoxicity of bovine serum amine oxidase were determined in Chinese hamster ovary cells at 37 °C. Cytotoxicity caused by exogenous hydrogen peroxide, added directly (> 10 μM) or generated by glucose oxidase (0.5 U/mL), was completely inhibited by catalase. Cytotoxicity caused by bovine serum amine oxidase (5.7 × 10−3 U/mL) and spermine (340 μM) was completely inhibited by catalase only during short incubation times after which time cytotoxicity occurred. This indicates that hydrogen peroxide was the only species contributing to cytotoxicity at this stage of the reaction. Aldehyde dehydrogenase alone caused partial inhibition of cytotoxicity, but only later in the reaction. Cytotoxicity was completely eliminated in the presence of both catalase and aldehyde dehydrogenase. Exogenous acrolein (> 50 μM) also caused cytotoxicity in Chinese hamster ovary cells. However, hydrogen peroxide was toxic to cells at lower concentrations and at shorter exposure times relative to aldehydes. These data show that both peroxide and aldehydes contribute to cytotoxicity of oxidation products of spermine. Aldehydes such as acrolein are responsible for cytotoxicity that cannot be accounted for by hydrogen peroxide.Key words: acrolein, hydrogen peroxide, catalase, polyamine.

The role of copper in bovine serum amine oxidase (BSAO)

1989 ◽  
Vol 36 (3-4) ◽  
pp. 328
Author(s):  
L. Avigliano ◽  
L. Morpurgo ◽  
E. Agostinelli ◽  
B. Mondovi'
Keyword(s):  
Bovine Serum ◽  
Amine Oxidase

N-alkanamines as substrates to probe the hydrophobic region of bovine serum amine oxidase active site: A kinetic and spectroscopic study

2007 ◽  
Vol 465 (1) ◽  
pp. 50-60 ◽  
Author(s):  
Maria Luisa Di Paolo ◽  
Carmine Pesce ◽  
Michele Lunelli ◽  
Marina Scarpa ◽  
Adelio Rigo
Keyword(s):  
Spectroscopic Study ◽  
Active Site ◽  
Bovine Serum ◽  
Amine Oxidase ◽  
Hydrophobic Region

Stability of spermine oxidase to thermal and chemical denaturation: comparison with bovine serum amine oxidase

Amino Acids ◽  
2016 ◽  
Vol 48 (10) ◽  
pp. 2283-2291 ◽  
Author(s):  
Manuela Cervelli ◽  
Alessia Leonetti ◽  
Laura Cervoni ◽  
Shinji Ohkubo ◽  
Marla Xhani ◽  
...  
Keyword(s):  
Bovine Serum ◽  
Amine Oxidase ◽  
Spermine Oxidase ◽  
Chemical Denaturation

scholarly journals Stimulatory Role of Glycated Fetal Bovine Serum Along with Iron on In Vitro Production of Insulin by Differentiated Mouse Embryonic Stem Cells

2011 ◽  
Vol 57 (4) ◽  
pp. 356-361
Author(s):  
Ikuo Nishigaki ◽  
Gowri Rangasamy Gunassekaran ◽  
Panjan Nagappan Venkatesan ◽  
Mandupal Chaco Sabu ◽  
Sabu Priya ◽  
...  
Keyword(s):  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Bovine Serum ◽  
Fetal Bovine Serum ◽  
Embryonic Stem ◽  
In Vitro Production ◽  
Fetal Bovine ◽  
Vitro Production

scholarly journals Renalase and Biomarkers of Contrast-Induced Acute Kidney Injury

2015 ◽  
Vol 6 (1) ◽  
pp. 25-36 ◽  
Author(s):  
Maciej T. Wybraniec ◽  
Katarzyna Mizia-Stec
Keyword(s):  
Acute Kidney Injury ◽  
Renal Injury ◽  
Amine Oxidase ◽  
Kidney Injury ◽  
Cardiorenal Syndrome ◽  
Creatinine Concentration ◽  
Invasive Cardiology ◽  
Proximal Tubular ◽  
Novel Biomarkers

Background: Contrast-induced acute kidney injury (CI-AKI) remains one of the crucial issues related to the development of invasive cardiology. The massive use of contrast media exposes patients to a great risk of contrast-induced nephropathy and chronic kidney disease development, and increases morbidity and mortality rates. The serum creatinine concentration does not allow for a timely and accurate CI-AKI diagnosis; hence numerous other biomarkers of renal injury have been proposed. Renalase, a novel catecholamine-metabolizing amine oxidase, is synthesized mainly in proximal tubular cells and secreted into urine and blood. It is primarily engaged in the degradation of circulating catecholamines. Notwithstanding its key role in blood pressure regulation, renalase remains a potential CI-AKI biomarker, which was shown to be markedly downregulated in the aftermath of renal injury. In this sense, renalase appears to be the first CI-AKI marker revealing an actual loss of renal function and indicating disease severity. Summary: The purpose of this review is to summarize the contemporary knowledge about the application of novel biomarkers of CI-AKI and to highlight the potential role of renalase as a functional marker of contrast-induced renal injury. Key Messages: Renalase may constitute a missing biochemical link in the mutual interplay between kidney and cardiac pathology known as the cardiorenal syndrome.

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