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Bradykinin-related peptides up-regulate the expression of kinin B1 and B2 receptor genes in human promonocytic cell line U937

100%

Guevara-Lora I., Florkowska M., Kozik A.

Acta Biochimica Polonica

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2009

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tom 56

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nr 3

515-522

Kinins, universal mediators of inflammation, are recognized by two kinds of receptors, B1 and B2, which have been found to be expressed in numerous cell types of several species. However, the knowledge of the regulation of these receptors in leukocytes is still not satisfactory. In the current work, we have demonstrated a constitutive production of B2 receptor mRNA in the human promonocyte U937 cells and its two-fold augmentation after cell differentiation with retinoic acid and phorbol ester. Bradykinin and des-Arg10-kallidin induced the expression of both B2 and B1 receptors in cells before and after differentiation. Generally, the undifferentiated cells were more susceptible to bradykinin-dependent induction of kinin receptors (increases by approximately 250% and 200% for B2 and B1 receptors, respectively). The induction, by approx. 200%, of B1 receptor by des-Arg10-kallidin was detected on both mRNA and protein levels. In addition, an unexpected strong induction of B2 receptor by this compound was observed in the retinoic acid- and phorbol ester-differentiated cells (by 150% and 200%, respectively) that suggests a possible autoregulation of kinin receptors by own agonists during the inflammatory state. On the other hand, a strong enhancement of the expression of both receptors by interleukin 1β, especially in the phorbol ester-differentiated cells, indicates the involvement of kinin receptors in the propagation of the inflammatory processes.

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Kinin-generating cellular model obtained from human glioblastoma cell line U-373

100%

Guevara-Lora I., Blonska B., Faussner A., Kozik A.

Acta Biochimica Polonica

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2013

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tom 60

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nr 3

Kinins, a group of important pro-inflammatory peptides, are abundantly found in tissues and biological fluids of cancer patients. Bradykinin, the major representative of kinins, induces vascular permeability and, in consequence, promotes tumor expansion. Additionally, the kinin-induced inflammatory responses, especially those mediated by kinin metabolites without the C-terminal arginine residue, lead to enhanced tumor growth. The present study aimed at analyzing the ability of the human glioblastoma cell line U-373, derived from a malignant tumor, to produce kinin peptides. The proteins involved in kinin generation, i.e., the kininogens and the kallikreins, were shown to be expressed in these cells. Moreover, tumor necrosis factor α, a proinflammatory cytokine that mediates tumorigenesis, was found to enhance the expression of enzymes associated with kinin production. The strong binding of kininogen to the cell surface and the enzymatic degradation of this protein by cells suggest the activation of kinin-generating systems. Indeed, glioblastoma cells, pre-treated with tumor necrosis factor α, released kinin peptides from exogenous kininogen. The expression of kinin receptors in these cells was also shown to increase under the influence of this cytokine. Our results suggest that the human glioblastoma cell line U-373 constitutes a good cellular model that can be helpful in cancer research focused on kinin-induced inflammation. Furthermore, our findings can contribute to new approaches in cancer treatment with the use of kinin receptor antagonists and inhibitors of kinin production.

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Biostable analogs of insect kinin and insectatachykinin neuropeptides: A review of novel classes of antifeedants and aphicides

80%

Nachman R. J., Smagghe G.

Pestycydy

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2011

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nr 1-4

Neuropeptides are regulators of critical life processes in insects, but are subject to rapid degradation by peptidases in the hemolymph (blood), tissues and gut. This limitation can be overcome via replacement of peptidase susceptible portions of the insect neuropeptides with non-natural residues or moieties to create analogs with enhanced biostability. Two neuropeptide families, the insect kinins and insectatachykinins, stimulate gut motility and Malpighian tubule fluid secretion in certain insects but unmodified members demonstrate little or no effect when fed to pea aphids (Acyrthosiphon pisum) in an artificial diet. Nonetheless, biostable analogs developed via the strategic introduction of either bulky Aib residues and/or β-amino acids demonstrate potent antifeedant and aphicidal effects when administered orally; whereas other biostable analogs are inactive. Although the precise mechanism of action has not been delineated, the activity may be associated with disruption of the physiological processes that these neuropeptides regulate in insects. The most active of the biostable insect kinin and insectatachykinin analogs show LC50 values of 0.063 nmole/μl (LT50 = 1.68 days) and 0.0085 nmole/μl (LT50 = 1.1 days), respectively; matching or exceeding the potency of some commercially available aphicides. The biostable analogs represent important leads in the development of alternative, environmentally sound aphid control agents.

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Kinins and thrombolysis

80%

Swies J., Chlopicki S., Gryglewski R. J.

Journal of Physiology and Pharmacology

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1993

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tom 44

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nr 2

Ograniczanie wyników

2 Acta Biochimica Polonica

1 Journal of Physiology and Pharmacology

1 Pestycydy

2 Guevara-Lora I.

2 Kozik A.

1 Blonska B.

1 Chlopicki S.

1 Faussner A.

1 Florkowska M.

1 Gryglewski R. J.

1 Nachman R. J.

1 Smagghe G.

1 Swies J.

1 2013

1 2011

1 2009

1 1993

Bradykinin-related peptides up-regulate the expression of kinin B1 and B2 receptor genes in human promonocytic cell line U937

Kinin-generating cellular model obtained from human glioblastoma cell line U-373

Biostable analogs of insect kinin and insectatachykinin neuropeptides: A review of novel classes of antifeedants and aphicides

Kinins and thrombolysis