Inhibition of plant amine oxidases by a novel series of diamine derivatives

Stránská, Jana; Šebela, Marek; Tarkowski, Petr; Řehulka, Pavel; Chmelı́k, Josef; Popa, Igor; Peč, Pavel

doi:10.1016/j.biochi.2006.08.001

Cited by 15 publications

(7 citation statements)

References 26 publications

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“…Importantly, guazatine can discriminate between purified recombinant murine APAO and SMO, suggesting that it is possible to selectively inhibit these enzymes 182. Recently, a series of N,N’-bis[(pyridinyl) methyl]-diamines typified by BPOD ( 98 , Figure 21) were shown to produce competitive inhibition of purified plant polyamine oxidase (PAO) in vitro 183…”

Section: Polyamines and Lsd1 Inhibitionmentioning

confidence: 99%

Recent Advances in the Development of Polyamine Analogues as Antitumor Agents

2009

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Section: Polyamines and Lsd1 Inhibitionmentioning

confidence: 99%

Recent Advances in the Development of Polyamine Analogues as Antitumor Agents

2009

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“…Several groups have identified amines, guanidines or similar analogues that act as selective modulators of these 2 amine oxidases 33-39. We previously reported the synthesis of a novel series of (bis)guanidines and (bis)biguanides40 that are potent antitrypanosomal agents in vitro, with IC 50 values against Trypanosoma brucei as low as 90 nM.…”

Section: Introductionmentioning

confidence: 99%

(Bis)urea and (Bis)thiourea Inhibitors of Lysine-Specific Demethylase 1 as Epigenetic Modulators

et al. 2010

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The recently discovered enzyme lysine-specific demethylase 1 (LSD1) plays an important role in the epigenetic control of gene expression, and aberrant gene silencing secondary to LSD1 over expression is thought to contribute to the development of cancer. We recently reported a series of (bis)guanidines and (bis)biguanides that are potent inhibitors of LSD1, and induce the reexpression of aberrantly silenced tumor suppressor genes in tumor cells in vitro. We now report a series of isosteric ureas and thioureas that are also potent inhibitors of LSD1. These compounds induce increases in methylation at the histone 3 lysine 4 (H3K4) chromatin mark, a specific target of LSD1, in Calu-6 lung carcinoma cells. In addition, these analogues increase cellular levels of secreted frizzle-related proteins (SFRP) 2 and 5, and transcription factor GATA4. These compounds represent an important new series of epigenetic modulators with the potential for use as antitumor agents.

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“…Since the filtrate of pea seedling homogenate exerted the same antihistamine results of purified PSAO, its application in fish is more practical because the preparation process is less time and energy consuming. Despite the fruitful results of the study, it seems that the enzyme efficacy can vary due to the diversity and distribution of the enzyme inhibitors regarding the variety of fish species, their environment, and fishing styles [27,28].…”

Section: Discussionmentioning

confidence: 99%

Pea Seedling Amine Oxidase Application: an Emerging Antihistamine Strategy in Tuna Fish

Ebrahimnejad¹

2013

J Food Process Technol

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Despite the known antihistaminic effects of PSAO, this enzyme remains unrecognized as an antihistamine additive in the food industry. The objective of this study was to ascertain the plausible histamine-degrading effects of a new food-grade additive (pea seedling extract) in tuna fish. PSAO was purified from cultured pea seedlings via ionexchange and size-exclusion chromatography. SDS-PAGE results indicated that the PSAO subunit has an apparent molecular weight of about 95 kDa. To evaluate the optimized conditions for antihistaminic activity of the enzyme, the reaction of PSAO and histamine was carried out in KPi buffer under conditions relevant to the fish processing industry. 1 unit mL -1 of PSAO significantly reduced the histamine content at pH 7.0 but not at pH 5.0. Accordingly, its antihistaminic activity was assessed in homogenized skipjack tuna fish (Katsuwonus pelamis) using an ion-paired HPLC method. The results showed that PSAO can reduce 87.14% of the histamine content of the tuna fish at pH 7.0, 37°C. This study indicates that PSAO -purified or even filtrate of pea seedling homogenate -can degrade histamine, which suggests practical application of this enzyme in fish processing industry.Pea seeds (Pisum sativum L) were purchased from Nunhems Zaden BV, Haelen, Netherlands. The seeds, disinfected with a solution of sodium hypochlorite, were cultured in plastic plug-trays with a soilless media of cocopeat and perlite (1:1 v/v). The etiolated (dark-grown) seedlings were harvested above the roots after 12-days germination at room temperature. After harvesting, immediate purification of PSAO was carried out at 4°C.

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Inhibition of plant amine oxidases by a novel series of diamine derivatives

Cited by 15 publications

References 26 publications

Recent Advances in the Development of Polyamine Analogues as Antitumor Agents

Recent Advances in the Development of Polyamine Analogues as Antitumor Agents

(Bis)urea and (Bis)thiourea Inhibitors of Lysine-Specific Demethylase 1 as Epigenetic Modulators

Pea Seedling Amine Oxidase Application: an Emerging Antihistamine Strategy in Tuna Fish

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