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

Guevara-Lora, Ibeth; Florkowska, Magdalena; Kozik, Andrzej

doi:10.18388/abp.2009_2488

Cited by 11 publications

(6 citation statements)

References 25 publications

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“…Interestingly, the stimulation of B1R mRNA expression by BK and INF‐γ was delayed as compared to the immediate effect of DAKD. Such a time lag in response suggested autoregulation of kinin receptors by their agonists in the endothelial cells as we previously reported for U937 cells [Guevara‐Lora et al, ]. In this study, we established that a similar regulation of B1R expression might occur in the endothelial cells.…”

Section: Discussionsupporting

confidence: 87%

Influence of kinin peptides on monocyte-endothelial cell adhesion

et al. 2014

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Adhesion of leukocytes to vascular endothelium in response to proinflammatory mediators is an important component of the overall inflammatory reaction. In the current work, we used a retinoic acid-differentiated human promonocytic cell line, U937 and a human microvascular endothelial cell line, HMEC-1 to analyze the effect of the potent pro-inflammatory bradykinin-related peptides (kinins) on cell adhesion. Bradykinin (BK) and kinin metabolites without the C-terminal arginine residue enhanced adhesion of the monocyte-like cells to fibronectin and to the HMEC-1 cells. Expression of adhesion proteins on the surface of both cell types was altered by the kinin peptides. In the monocyte-like cells, expression of CD11b, a subunit of Mac-1 integrin, was significantly increased whilst in the endothelial cells, a strong increase in the production of intercellular adhesion molecule 1 (ICAM-1) was observed. The positive bradykinin-induced effect on the cell-cell interaction was reversed by a carboxypeptidase inhibitor (MGTA), hence we suspected a significant role of the des-Arg kinin metabolites, which acted through the kinin receptor type 1. Indeed, the expression of this receptor was up-regulated not only by agonists but also by interferon-γ and bradykinin. Kinin peptides also regulated signal transducer and activator of transcription proteins (STATs) activated by cytokines. Taken together, the above observations support our hypothesis that kinins stimulate monocyte adhesion to the vessel wall, especially during pathological states of the circulatory system accompanied by proinflammatory cytokine release.

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Section: Discussionsupporting

confidence: 87%

Influence of kinin peptides on monocyte-endothelial cell adhesion

et al. 2014

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“…In addition, a more recent report suggested down-regulation of B1R responses by the B2R agonist that is associated with co-endocytosis of the B1R-B2R dimer (Zhang et al, 2015). The suggestions that B1R-B2R interactions may be involved in the regulation of receptor expression mediated by the agonist of the partner receptor agree with previous reports, indicating autoregulation between B1R and B2R (Phagoo et al, 1999;Guevara-Lora et al, 2009).…”

Section: Functional Relevance Of Kinin Receptor Couplingsupporting

confidence: 87%

Hypothetical orchestrated cooperation between dopaminergic and kinin receptors for the regulation of common functions

et al. 2016

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The G protein-coupled receptors (GPCRs), one of the largest protein families, are essential components of the most commonly used signal-transduction systems in cells. These receptors, often using common pathways, may cooperate in the regulation of signal transmission to the cell nucleus. Recent scientific interests increasingly focus on the cooperation between these receptors, particularly in a context of their oligomerization, e.g. the formation of dimers that are able to change characteristic signaling of each receptor. Numerous studies on kinin and dopamine receptors which belong to this family of receptors have shown new facts demonstrating their direct interactions with other GPCRs. In this review, current knowledge on signaling pathways and oligomerization of these receptors has been summarized. Owing to the fact that kinin and dopamine receptors are widely expressed in cell membranes where they act as mediators of numerous common physiological processes, the information presented here sheds new light on a putative crosstalk of these receptors and provides more comprehensive understanding of possible direct interactions that may change their functions. The determination of such interactions may be useful for the development of new targeted therapeutic strategies against many disorders in which kinin and dopamine receptors are involved.

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“…This observation may be associated with the emergence of other stimuli that can promote proinflammatory response, e.g. overexpression of B1R due to prolonged B2R stimulation (Guevara-Lora et al, 2009) or activation of signaling pathways promoting chemotactic activity (Koyama et al, 2000). Indeed, B1R mediation in the interaction between PMN and endothelial cells has been reported (Figueroa et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

Bradykinin B2 receptor and dopamine D2 receptor cooperatively contribute to the regulation of neutrophil adhesion to endothelial cells*

et al. 2018

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Leukocyte adhesion to the vascular endothelium contributes to many immunological and inflammatory disorders. These processes have been shown to be mediated by bradykinin receptor type 2 (B2R) and dopamine receptor type 2 (D2R). In a previous study, we reported the formation of a B2R-D2R heterodimer, possibly altering cellular functions. Hence, in the present study, we examined the effect of co-activation of endothelial cells with B2R and D2R agonists on the interaction of these cells with neutrophils. Bradykinin, the main B2R agonist, significantly increased cell adhesion, and this effect was reversed when the endothelial cells were additionally co-treated with a selective D2R agonist, sumanirole. These results were dependent on the incubation time, showing an opposite tendency after prolonged stimulation. Significant changes in the expression of adhesion proteins, such as E-selectin and intercellular adhesion molecule 1 in endothelial cells were observed. Additionally, the cells preincubated with tumor necrosis factor-α showed decreased cell adhesion and IL-8 release after long incubation with both agonists. The modulation of cell adhesion by D2R and B2R seem to be mediated via STAT3 phosphorylation. In summary, this study demonstrated a protective role of D2R in neutrophil-endothelial cell adhesion induced by bradykinin, especially in cytokine-stimulated endothelial cells.

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

Cited by 11 publications

References 25 publications

Influence of kinin peptides on monocyte-endothelial cell adhesion

Influence of kinin peptides on monocyte-endothelial cell adhesion

Hypothetical orchestrated cooperation between dopaminergic and kinin receptors for the regulation of common functions

Bradykinin B2 receptor and dopamine D2 receptor cooperatively contribute to the regulation of neutrophil adhesion to endothelial cells*

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