Antitumor effect of lysine-isopeptides

Szende, B.; Szókán, Gy.; Tyihá, E; K, Pál; Gáborjányi, R; Almás, M.; Khlafulla, A. R.

doi:10.1186/1475-2867-2-4

Cited by 16 publications

(9 citation statements)

References 6 publications

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“…It is widely used as a food preservative and is also reported having an antitumoral effect [28,[39][40]. Epsilon poly-L-lysine is of shorter length and has shorter sidechains than α-poly-L-lysine (Figure 3), and therefore, we hypothesize, carries less membrane cytotoxicity.…”

Section: Discussionmentioning

confidence: 99%

Cationic polypeptides in a concept of oppositely charged polypeptides as prevention of postsurgical intraabdominal adhesions

Isaksson¹,

Åkerberg²,

Said³

et al. 2011

JBiSE

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Background: Two differently charged polypeptides, α-poly-L-lysine and poly-L-glutamate, have previously been shown to effectively reduce postoperative intraabdominal adhesions. Though α-poly-L-lysine showed toxicity in doses too close to the lowest therapeutic dose, the aim in the present study was to investigate the possible antiadhesive effect of another four cationic polypeptides. Materials/Methods: 125 mice were studied with a standardized and reproducible adhesion model and given epsilon poly-Llysine, lactoferrin, lysozyme and polyarginine respectively in a combination with poly-L-glutamate. Epsilon poly-L-lysine was also tested in different concentrations and as single treatment. Results: All four cationic polypeptides above showed a significantly better anti-adhesive effect than the controls receiving saline (p < 0.05). Epsilon poly-L-lysine had the best antiadhesive effect of the new substances tested in the experiment. Single treatment with the epsilon poly-Llysine showed toxic side effects. Discussion: We have shown that epsilon poly-L-lysine, polyarginine, lysozyme and lactoferrin, in descending order, all can reduce postoperative intraabdominal adhesions in mice when combined with poly-L-glutamate. There were side effects of epsilon poly-L-lysine resembling those of α-poly-L-lysine, although less toxic. The antiadhesive effect of epsilon poly-L-lysine did not reach the level of α-poly-L-lysine. Further studies will concentrate on additional investigation, trying to modify the α-poly-L-lysine to lower its toxicity. The less toxic epsilon poly-L-lysine also needs further attention in our research of antiadhesive bioactive polypeptides.

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Section: Discussionmentioning

confidence: 99%

Cationic polypeptides in a concept of oppositely charged polypeptides as prevention of postsurgical intraabdominal adhesions

Isaksson¹,

Åkerberg²,

Said³

et al. 2011

JBiSE

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“…The change in the position of the signals (with respect to their positions in the spectrum of free ligand) assigned to C (6) near the ÀNH þ 3 group and C (1) of the carboxyl group (table 1) from lysine suggests involvement of these two groups in the formation of the molecular complex (ATP)H 4 (Lys). On the other hand, a change in the position of the signal assigned to C (2) by only 0.022 ppm excludes the participation of the α-amino group of the nucleotide from interaction.…”

Section: Atp-lys Systemmentioning

confidence: 97%

“…Treatment with lysine has been found to suppress the clinical symptoms of infection with herpes virus [2] and studies have shown that lysine benefits go beyond protein quality and growth [3]. Lysine is a strong inhibitor of collagen digestive enzymes spreading tumor cells in the tissues of living organisms [4][5][6][7]. This compound has two amine groups of positive charge at physiological pH and is incorporated into proteins strongly binding the negatively charged DNA helix fragments such as histones (components of nucleoprotein complex of chromatin).…”

Section: Introductionmentioning

confidence: 98%

“…As follows from analysis of the NMR data, the shifts in positions of the signals assigned to P α , P β , and P γ mean that all phosphate groups of ATP are involved in the interactions (although P α is a positive center). The changes in positions of the signals assigned to C (1) , C (2) , and C (6) in the spectrum of Lys with respect to those in the spectrum of the free ligand indicate that also the α ÀNH þ 3 group of the amino acid is involved in the interactions, while in the tetraprotonated species only the ω-amino group was engaged in the interaction, see table 1. Surprisingly, the equilibrium constants of (ATP)H 4 (Lys) and (ATP)H 3 (Lys) adduct formation are 4.85 and 4.66 (table 2), despite a different number of interacting centers.…”

mentioning

confidence: 94%

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Interactions of histone amino acid: lysine with copper(II) ions and adenosine 5′-triphosphate as well as in a metal-free system

Bregier-Jarzebowska

Gasowska

Lomozik

2014

Journal of Coordination Chemistry

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Thermodynamic stability and mode of coordination were studied in the binary system of copper(II)/ lysine, ternary system of copper(II)/ATP/lysine, and compared to the intermolecular interaction in the metal-free ATP/lysine system. In the system ATP/Lys, groups P β and P γ from ATP, participate in the interaction with the amino acid, while group P α from ATP is involved as reaction center only at high pH. The endocyclic nitrogens from the nucleotide N(1) and N(7) take part in the interactions only below physiological pH. In the binary complexes, oxygens from carboxylic group and nitrogen from the α-NH 2 amino group are involved in coordination. However, introduction of the second ligand, ATP, into the system Cu(II)/Lys changes the amino acid coordination in alkaline medium. In protonated mixed-ligand complexes, the α, β, and γ oxygens of the phosphate from ATP coordinate, but at higher pH, only α oxygens coordinate in Cu(ATP)(Lys). Although Cu(II) ions do not coordinate nitrogen from ATP in the ternary system, the presence of metal ions excludes interaction of these atoms over the whole pH range studied.

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“…For GO: 0018262 (isopeptide cross-linking), it was proven that lysine-isopeptides are associated with cancer (Szende et al, 2002). For GO: 0042772 (DNA damage response, signal transduction resulting in transcription), Karanika et al (2014) pointed out that DNA damage response is associated with prostate cancer (Karanika et al, 2014).…”

Section: Feature Analysismentioning

confidence: 99%

Biological Feature Selection and Disease Gene Identification using New Stepwise Random Forests

Hwang¹

2017

Industrial Engineering and Management Systems

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Identifying disease genes from human genome is a critical task in biomedical research. Important biological features to distinguish the disease genes from the non-disease genes have been mainly selected based on traditional feature selection approaches. However, the traditional feature selection approaches unnecessarily consider many unimportant biological features. As a result, although some of the existing classification techniques have been applied to disease gene identification, the prediction performance was not satisfactory. A small set of the most important biological features can enhance the accuracy of disease gene identification, as well as provide potentially useful knowledge for biologists or clinicians, who can further investigate the selected biological features as well as the potential disease genes. In this paper, we propose a new stepwise random forests (SRF) approach for biological feature selection and disease gene identification. The SRF approach consists of two stages. In the first stage, only important biological features are iteratively selected in a forward selection manner based on one-dimensional random forest regression, where the updated residual vector is considered as the current response vector. We can then determine a small set of important biological features. In the second stage, random forests classification with regard to the selected biological features is applied to identify disease genes. Our extensive experiments show that the proposed SRF approach outperforms the existing feature selection and classification techniques in terms of biological feature selection and disease gene identification.

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Antitumor effect of lysine-isopeptides

Cited by 16 publications

References 6 publications

Cationic polypeptides in a concept of oppositely charged polypeptides as prevention of postsurgical intraabdominal adhesions

Cationic polypeptides in a concept of oppositely charged polypeptides as prevention of postsurgical intraabdominal adhesions

Interactions of histone amino acid: lysine with copper(II) ions and adenosine 5′-triphosphate as well as in a metal-free system

Biological Feature Selection and Disease Gene Identification using New Stepwise Random Forests

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