Disease relevance of aminourea

• Here, we present a comparative study between semicarbazide and amine glass slides in an immunofluorescent serodetection assay using HIV (Gp120, Gp41), HCV (mix-HCV, core, NS3, and NS4), and HBV (HBs) recombinant antigens [1].
• In the recovery studies it was seen that semicarbazide does not allow displacement of all the AcH; treatment of the blood with the reactant sodium nitrite-sulfosalycilic acid and use of the hemolysis method gave levels of recovery lower than 50% [2].
• Semicarbazide also reduced HCHO-induced cytotoxicity in the Yoshida lymphosarcoma cell line, while no significant alteration in MDMS-induced cytotoxicity was observed [3].
• The spin-labeled derivative of podophyllotoxin, N'-podophyllic acid-N-[3-(2,2,5,5-tetramethyl pyrrolinenyloxy)] semicarbazide (GP-11), was synthesized and tested for its antitumor activity against mouse transplantable tumors, Sarcoma-180, Hepatoma-A, P388 leukemia and Ehrlich ascites carcinoma [4].
• Semicarbazide was ineffective against acrolein toxicity [5].

High impact information on aminourea

• Semicarbazide, a lathyrogen, was given to growing rats to elucidate the consequences of altering the molecular structure of fibrous proteins within the lung [6].
• The latter is mainly retained in the medium containing 5 mM semicarbazide, while the generated formaldehyde is more than 50% consumed by the mitochondria [7].
• In agreement with this suggestion, complexing of formaldehyde with semicarbazide was observed spectroscopically not to be an extremely rapid reaction even at 37 degrees C. This is believed to be the reason for the greater extent of consumption of formaldehyde generated by the endoplasmic reticulum [7].
• We report that in addition to supporting leukocyte adhesion, provision of specific substrate to VAP-1 results in hepatic endothelial cell activation, which can be abrogated by treatment with the enzyme inhibitor semicarbazide [8].
• Adding 5 mM semicarbazide to incubations increased the observed depentylation (except that due to CYP2E1) by >60% [9].

Chemical compound and disease context of aminourea

• These results suggest that in vivo pretreatment with semicarbazide at least partially protects aortic mitochondria from allylamine toxicity [10].
• Since BW 755C and NDGA had no effect on formaldehyde production, while sulfasalazine as well as semicarbazide, a protective agent against formaldehyde-producing toxicants, failed to protect the cells against Mel toxicity, mechanism(s) of Mel neurotoxicity appeared independent of the GSH-mediated metabolism of this compound [11].
• We postulate that some modulating influence of betaAPN (or phenelzine) on tissue distribution, metabolism, or detoxification pathways of AA increases AA's acute vascular toxicity, whereas semicarbazide offers protection by inhibiting the initial deamination of AA to a highly reactive aldehyde [12].
• Both inhibitors potentiated hydralazine hypotension, bromoethylamine having a longer latency and a shorter duration of action than semicarbazide [13].
• Presence of an inducible semicarbazide-sensitive amine oxidase in Mycobacterium sp. Strain JC1 DSM 3803 grown on benzylamine [14].

Biological context of aminourea

• Oxidative deamination of L-cysteine by L-amino acid oxidase yields the highly reactive imine, 2-imino-3-mercaptopropionic acid, which can be quantitatively trapped with semicarbazide [15].
• In this review, we summarize behavioral, immunohistochemical (brain Fos distribution) and electrophysiological (auditory evoked potentials) data obtained with the reduction of GABA transmission by local injections of a GABA receptor blocker (bicuculline, BIC) or a glutamic acid decarboxylase inhibitor (semicarbazide, SMC) into the MT [16].
• The binding site was concentrated in the mitochondrial fraction enriched with cytochrome c oxidase and semicarbazide-insensitive monoamine oxidase [17].
• Pretreatment with semicarbazide left the homosynaptic depression unchanged while suppressing the dorsal root reflex [18].
• OBJECTIVE: To explore the activity of monoamine oxidases (MAOs) and semicarbazide-sensitive amine oxidases (SSAOs) in adipose tissue and blood of lean and moderately obese subjects and to study whether there is a link between these hydrogen peroxide-generating enzymes and blood markers of oxidative stress [19].

Anatomical context of aminourea

• The procedure requires a 30-min incubation of erythrocytes in 30 mM semicarbazide and 12 mM aniline (pH 5, 38 degrees C) [20].
• Semicarbazide-sensitive amine oxidases (SSAOs) are located in cardiovascular smooth muscle, cartilage and brown adipose tissues of different species, including human [21].
• A similar effect of MAO and SSAO inhibitors was obtained in both the intact cells and the membranes: half of the activity was sensitive to semicarbazide and the other half more easily inhibited by MAO-A than by MAO-B inhibitors [22].
• The formation of this compound required the presence of NADPH, semicarbazide, and microsomes [23].
• Conditioned place aversion produced by microinjections of semicarbazide into the periaqueductal gray of the rat [24].

Associations of aminourea with other chemical compounds

• A semicarbazide-sensitive clorgyline-resistant amine oxidase (SSAO) was solubilized from membrane fractions of rat brown adipose tissue by the non-ionic detergent, Triton X-100 [25].
• Pargyline and semicarbazide, specific inhibitors of MAO and SSAO, respectively, canceled this negative effect of MAO substrates on NOS2 expression [26].
• Bovine serum amine oxidase: half-site reactivity with phenylhydrazine, semicarbazide, and aromatic hydrazides [27].
• A unique combination of active pharmacophores led us to a series of semicarbazide-based inhibitors that are highly potent against CDK2 and CDK4 while maintaining selectivity against other relevant serine/threonine kinases [28].
• This effect was insensitive to pargyline (an MAO inhibitor), but was inhibited by semicarbazide (an SSAO inhibitor) and by N-acetylcysteine (an antioxidant agent), suggesting the involvement of the H(2)O(2) generated during SSAO-dependent amine oxidation [29].

Gene context of aminourea

• Glutathione, methoxylamine, and semicarbazide did not prevent adduction of reactive menthofuran metabolites to CYP2A6, however [30].
• Special attention has been paid to treatments that are known to affect the activity of diamine oxidase (DAO, histaminase, EC, 1.4.3.6), a copper-containing enzyme characteristically inhibited by semicarbazide [31].
• In mice deprived of food for 12 h, the i.c.v. or i.p. administration of benzylamine, a substrate common to both monoamine oxidase B and semicarbazide-sensitive benzylamine oxidases, dose-dependently inhibited feeding [32].
• In this series, semicarbazide 8b and bromoacetamides 18b,c were found to be potent HDAC inhibitors for non-hydroxamates [33].
• The reactivity of SSAO with semicarbazide and phenylhydrazine suggests that the cofactor is a carbonyl type molecule [34].

Analytical, diagnostic and therapeutic context of aminourea

• Lesions of the vPAG did not change the amount of freezing or escape responses produced by microinjections of semicarbazide into the dlPAG [35].
• We report a novel generation of peptide arrays fabricated by site-specific ligation of glyoxylyl peptides onto glass slides covered by a semicarbazide sol-gel layer [36].
• Additional data concerning the characterization of the semicarbazide surface (homogeneity of the slides, chemical stability, contact angle measurements, atomic force microscopy studies, reproducibility of serodetection results) are also presented and discussed [1].
• 5. When intrapulmonary metabolism of phenylethylamine was inhibited by simultaneous perfusion with semicarbazide (10 mM) and pargyline (10 micronM), the removal rate was unaltered, establishing that uptake of the amine from the vascular space is not dependent on metabolism at least for 4 min infusions [37].
• We describe novel peptide-protein microarrays, which were fabricated using semicarbazide glass slides that permitted the immobilization of glyoxylyl peptides by site-specific ligation and the immobilization of proteins by physisorption [38].

References