Explore chapters and articles related to this topic
Poly amines and Cell and Tissue Growth
Published in Jean Morisset, Travis E. Solomon, Growth of the Gastrointestinal Tract: Gastrointestinal Hormones and Growth Factors, 2017
Chris N. Conteas, Ann L. Silverman, Jeffrey A. Moshier, Peter P. McCann, Gordon D. Luk
Therefore, AdoMetDC has also been considered as a key regulatory enzyme in polyamine biosynthesis. Although the steps described are generally irreversible, some interconversion of polyamines occurs through the action of spermidine and spermine N’-acetyltransferases and polyamine oxidase (Figure 1). Putrescine may also be degraded by the enzyme diamine oxidase to aminobutyraldehyde and subsequently to gamma aminobutyric acid (GABA). Dc-AdoMet, after donating the aminopropyl group for the formation of spermidine and spermine, is itself converted to methylthioadenosine, which is then recycled through the purine pools and methionine pools and hence may also effect methylation reactions.
Cell-Mediated Immunity and its Role in Protection
Published in Mary M. Stevenson, Malaria: Host Responses to Infection, 2017
John H. L. Playfair, K. Rebecca Jones, Janice Taverne
Macrophages produce at least 80 different monokines and enzymes, in addition to ROI.33 One macrophage-derived enzyme known to increase with activation of the cell and to be secreted extracellularly is polyamine oxidase (PAO). Human PAO catalyzes the oxidation of the ubiquitous polyamines, such as spermine, which are present in serum and in erythrocytes, to aldehydes, NH4 and H2O2. Both PAO,34,35 which is found in increased concentrations in retroplacental serum,36 and the purified aminoaldehyde products of this reaction are toxic for P. falciparum in vitro.37 Hydrogen peroxide production in this system was not considered to contribute to the inhibition seen since catalase had no effect on the killing.35
Molecular Aspects of the Activity and Inhibition of the FAD-Containing Monoamine Oxidases
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
The two monoamine oxidase isoenzymes, MAO A and MAO B, are encoded by genes on the X-chromosome (MAOA and MAOB) and are expressed in all tissues. In addition to their well-known role in the brain, peripheral MAOs especially in gut (MAO A), liver (both), platelet (MAO B) and placenta (MAO A) play significant roles in protection against biogenic amines and contribute to Phase 1 drug metabolism. In heart, hydrogen peroxide and aldehydes produced by MAO oxidation of amines may contribute to heart failure. These flavoprotein oxidases (E.C. 1.4.3.4) are located on the mitochondrial outer membrane, and therefore metabolize intra-cellular amines. In contrast, the copper-dependent primary amine oxidases (the soluble semicarbazide-sensitive amine oxidase (SSAO) and its membrane form, Vascular Adhesion Protein-1, E.C. 1.4.3.21) act on extra-cellular amines and function in inflammation (Becchi et al., 2017). SSAO, lysyl oxidase (1.4.3.13) and diamine oxidase (E.C. 1.4.3.22 which metabolizes histamine) contain 2,4,5-trihydroxyphenylalaninequinone as the cofactor (www.brenda-enzymes.org). These non-FAD enzymes will not be considered in this article. Other FAD–containing oxidases include the related amino acid oxidases, l-amino acid oxidase (LAAO, E.C. 1.4.3.2) and D-amino acid oxidase (DAAO, E.C. 1.4.3.3), and the spermine metabolizing enzyme, polyamine oxidase (E.C. 1.5.3.13), all of which have covalently bound FAD. A possible evolutionary precursor of MAO is found in the peroxisomes of Aspergillus niger and has a non-covalently bound FAD co-factor (Sablin et al., 1998) making it interesting for chemical applications (Bailey et al., 2007).
Metalloproteinases and NAD(P)H-dependent oxidoreductase within of Bay nettle (Chrysaora chesapeakei) venom
Published in Toxin Reviews, 2022
Mayra Pamela Becerra-Amezcua, Mónica Alejandra Rincón-Guevara, Irma Hernández-Calderas, Xochitl Guzmán-García, Isabel Guerrero-Legarreta, Humberto González-Márquez
The protein of approx. 37 kDa is a NAD(P)/FAD-dependent oxidoreductase, although oxidoreductases have been detected in the jellyfish C. fuscescens (Ponce et al.2016), N. nomurai (Yue et al.2017b) and Cyanea sp. (Liang et al.2019), little is known about its effects. L-amino acid oxidases (LAAOs) had been found in venoms of snakes. These enzymes belong to the family called NAD(P)/FAD-dependent oxidoreductase that also comprises polyamine oxidase (PAO), flavin-containing monoamine oxidases (MAOs), D-amino acid dehydrogenase, and linoleic acid isomerase. Moreover, have various pathological and physiological activities, including induction of apoptosis, edema, platelet aggregation/inhibition, hemorrhagic, and anticoagulant activities (Ullah 2020). In general, the LAAOs are homodimers with molecular masses ranging from 120 to 150 kDa in their native form and 50 to 70 kDa in their monomeric forms (Costa et al.2014), but in jellyfish, homology with these enzymes has been found in proteins with smaller molecular weights (45–18 kDa) (Yue et al.2017b), which could indicate that in these organisms these enzymes are smaller.
Vaccine development against Helicobacter pylori: from ideal antigens to the current landscape
Published in Expert Review of Vaccines, 2021
Irineu Dos Santos Viana, Maria Luísa Cordeiro Santos, Hanna Santos Marques, Vinícius Lima de Souza Gonçalves, Breno Bittencourt de Brito, Filipe Antônio França da Silva, Natália Oliveira e Silva, Fillipe Dantas Pinheiro, Adriano Fernandes Teixeira, Davi Tanajura Costa, Briza Oliveira Souza, Cláudio Lima Souza, Márcio Vasconcelos Oliveira, Fabrício Freire de Melo
Besides the activation of the above-discussed inflammation in the gastric environment, H. pylori has the ability to evade immune mechanisms and to modulate the host defense system in order to favor its persistence in the gastric mucosa. Highly virulent CagA- and VacA-positive H. pylori strains have shown to be resistant to phagocytosis and, complementarily, the bacterium has the ability to induce macrophage apoptosis by stimulating the production of polyamine oxidase 1 by those cells, which leads to hydrogen peroxide release and depolarization of the mitochondrial membrane [33]. Moreover, CagA and VacA as well as γGT, another H. pylori virulence factor, promote a higher expression of IL-10 by dendritic cells, besides inducing the differentiation of T cells into CD4+ CD25+ FOXP3+ regulatory T (Treg) cells [34].
Plasma acrolein level in rheumatoid arthritis increases independently of the disease characteristics
Published in Modern Rheumatology, 2021
Chisato Kawabata, Toru Nagasawa, Mariko Ono, Nagayoshi Tarumoto, Narutaka Katoh, Yuko Hotta, Hirotaka Kawano, Kazuei Igarashi, Koichiro Shiokawa, Keita Nishimura
The reasons for this independency of PC-Acro from other variables remain uncertain. One possibility is that endogenous generations of acrolein in RA may be the key to revealing them. As mentioned previously, acrolein is endogenously generated through various pathways during cellular metabolism, and the catabolism of polyamines has been considered to be the main course among them [5,6]. Therefore, possible explanations are that polyamine oxidase activity increased in RA synovial fluid [24], polyamine levels increased in synovial tissues and synovial fluids [25], IL-1β induced elevation of SSAT1 activity and putrescine level in RA synovial adherent cells [26], and enzymatic activity of polyamine metabolism elevated in RA synovial fibroblasts [27]. However, the present data did not support this speculation where the catabolism of polyamines and metabolism of acrolein would be activated in local RA lesions. If it were true, PC-Acro levels would be correlated to RA inflammatory levels as with brain infarction [2,9,10] or renal dysfunction [7]. The earlier-mentioned question was: ‘Why did the PC-Acro levels in RA demonstrate no relation to RA background characteristics, even though they were correlated positively with condition severity in brain infarction or renal dysfunction?’