Induction of lactoferrin and IL‐8 release from human neutrophils by tryptic enzymes via proteinase activated receptor‐2

Wang, Haoyang; He, Shaoheng

doi:10.1016/j.cellbi.2006.04.007

Cited by 22 publications

(19 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This is consistent with our recent finding that recombinant human tryptase mimicked the effect of purified tryptase on the cleavage of eotaxin and RANTES only in the presence of heparin (13). This is also consistent with the findings that rh-tryptase induces IL-8 production from eosinophils (5) and neutrophils (6). Purified tryptase did not require exogenous heparin to induce IL-8 production because heparin was present in the tryptase preparation.…”

Section: Discussionsupporting

confidence: 92%

“…' Research on tryptase so far has revealed a large number of potential functions for this enzyme and identified it as a key inflammatory mediator in mast cell-related diseases and a potential target for therapeutic intervention (2). Tryptase has been shown to stimulate the release of chemokine IL-8 from various inflammatory and structural cells such as eosinophils (5), neutrophils (6), endothelial cells (7,8), and epithelial cells (9), but the mechanisms involved are poorly defined. Since IL-8 is a potent chemoattractant for a number of granulocytes, particularly neutrophils and eosinophils, and to a lesser extent mast cells, tryptase may play a key role in neutrophilic and eosinophilic inflammatory diseases.…”

mentioning

confidence: 99%

“…The cleavage of the extracellular part of PAR-2, as for all of the PARs, leads to the exposure of a ''tethered'' ligand, which subsequently binds to the receptor, thereby inducing signaling events and receptor/ligand internalization (14). Studies so far have demonstrated that tryptaseinduced IL-8 production is mediated by PAR-2 in eosinophils and fibroblasts (5), neutrophils (6), endothelial cells (8), and epithelial cells (9). However, it is interesting to note that some effects of tryptase, notably ASM cell proliferation, are mediated via a PAR-2-independent nonproteolytic mechanism (15).…”

mentioning

confidence: 99%

See 2 more Smart Citations

β-Tryptase Regulates IL-8 Expression in Airway Smooth Muscle Cells by a PAR-2–Independent Mechanism

Mullan

Riley

Clarke

et al. 2008

Am J Respir Cell Mol Biol

View full text Add to dashboard Cite

Mast cells are central in the development of several allergic diseases and contain a number of pre-formed mediators. b-tryptase, the most abundant mast cell product, is increasingly recognized as a key inflammatory mediator, as it causes the release of cytokines, particularly the chemokine IL-8, from both inflammatory and structural cells. The molecular mechanisms, however, remain largely unknown. In this study we sought to investigate whether b-tryptase could induce IL-8 expression in human airway smooth muscle (ASM) cells and to explore the molecular mechanisms involved. We found that purified human b-tryptase stimulated IL-8 production in a timeand concentration-dependent manner, which was inhibited by protease inhibitors and mimicked by recombinant human b-tryptase, but not by the protease-activated receptor-2 (PAR-2) agonist SLIGKV-NH 2 , consistent with the low-level expression of PAR-2 protein in these cells. b-tryptase also up-regulated IL-8 mRNA expression, as analyzed by RT-PCR and real-time PCR, which was abolished by the transcription inhibitor actinomycin D. Reporter gene assay showed that b-tryptase-induced IL-8 transcription was mediated by the transcription factors activator protein-1, CCAAT/enhancer binding protein, and NF-kB, and chromatin immunoprecipitation assay demonstrated that b-tryptase induced in vivo binding of these transcription factors to the IL-8 gene promoter. Furthermore, b-tryptase stabilized IL-8 mRNA, suggesting additional post-transcriptional regulation. Collectively these findings show that b-tryptase upregulates IL-8 expression in ASM cells through a PAR-2-independent proteolytic mechanism and coordinated transcriptional and posttranscriptional regulation, which may be of particular importance in understanding the role and the mechanisms of action of b-tryptase in regulating chemokine expression in mast cell-related disorders.

show abstract

Section: Discussionsupporting

confidence: 92%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

β-Tryptase Regulates IL-8 Expression in Airway Smooth Muscle Cells by a PAR-2–Independent Mechanism

Mullan

Riley

Clarke

et al. 2008

Am J Respir Cell Mol Biol

View full text Add to dashboard Cite

show abstract

“…In addition, tryptase can stimulate human endothelial cells for increased production of MCP-1 and IL-8 [24, 25, 91], chemokines which can attract neutrophils and many other cells of the immune system. Furthermore, tryptase activates peripheral blood mononuclear cells for TNF-, IL-6 and IL-1 production [109], human neutrophils for IL-8 secretion [197], and human T cells for IL-6 release [101]. Activation of these cells is very likely mediated via activation of the proteinase-activated receptor-2 (PAR-2) by tryptase.…”

Section: Mast Cell Serine Proteinases In Psoriasismentioning

confidence: 99%

Is there a role for mast cells in psoriasis?

et al. 2008

View full text Add to dashboard Cite

Mast cells have traditionally been considered as eVector cells in allergy but during the last decade it has been realized that mast cells are essentially involved in the mechanisms of innate and acquired immunity. Upon activation by anaphylactic, piecemeal degranulation or degranulation-independent mechanisms mast cells can secrete rapidly or slowly a number of soluble mediators, such as serine proteinases, histamine, lipid-derived mediators, cytokines, chemokines and growth factors. Mast cells can express cell surface co-stimulatory receptors and ligands, and they can express MHC class II molecules and thereby present antigens. These soluble factors and cell surface molecules can interact with other cells, such as endothelial cells, keratinocytes, sensory nerves, neutrophils, T cell subsets and antigen presenting cells which are essential eVectors in the development of skin inXammation. Besides promoting inXammation, mast cells may attempt in some circumstances to suppress the inXammation and epidermal growth but the regulation between suppressive and proinXammatory mechanisms is unclear. Psoriasis is characterized by epidermal hyperplasia and chronic inXammation where tryptase-and chymase-positive MC TC mast cells are activated early in the developing lesion and later the cells increase in number in the upper dermis with concomitant expression of cytokines and TNF superfamily ligands as well as increased contacts with neuropeptide-containing sensory nerves. Due to the intimate involvement of mast cells in immunity and chronic inXammation the role of mast cells in psoriasis is discussed in this review.

show abstract

“…Cells were incubated directly with 1 in 20 dilution of PE-conjugated mouse anti-human PAR-1 monoclonal antibody and mouse anti-human PAR-2 monoclonal antibody (Santa Cruz Biotechnology, Inc. Santa Cruz, USA) respectively for 30 min at 25 C, followed by two washes with staining buffer [PBS, 0.02% sodium azide, 0.1% bovine serum albumin (BSA), pH 7.4] [17][18]. Finally, cells were resuspended in PBS and labeled cells were analyzed by flow cytometry mentioned above.…”

Section: Flow Cytometry Analysismentioning

confidence: 99%

Antisense Oligodeoxynucleotide Against Tissue Factor Inhibits Human Umbilical Vein Endothelial Cells Injury Induced by Anoxia-Reoxygenation

Yin

Luo²,

Yao³

et al. 2010

Cell Physiol Biochem

View full text Add to dashboard Cite

Aims: The role of antisense oligodeoxynucleotide against tissue factor (aODN/TF) in cultured human umbilical vein endothelial cells (HUVECs) subjected to anoxia-reoxygenation (A/R) was investigated. Methods: HUVECs were divided randomly into control group, A/R group, aODN/TF+A/R group, sense oligodeoxynucleotide (sODN/TF) + A/R group and mismatched oligodeoxynucleotide (mODN/TF) + A/R group, in the latter 3 groups, HUVECs were transfected with aODN/TF, sODN/TF and mODN/TF respectively. HUVECs in all A/R groups underwent 3 hrs of anoxia and followed by 2 hrs of reoxygenation. In order to investigate the potential mechanisms of how increased TF may contribute to A/R injury in HUVECs, another set of HUVECs were incubated with human recombinant active site blocked factor VII (FVIIai) during A/R. Results: After A/R, TF expression at both mRNA and protein level was increased, furthermore, cell viability and the concentrations of SOD, GSH-PX and NO were declined, while LDH, MDA and ET-1 were overproduced (P<0.05 to 0.001 versus control group). In HUVECs of aODN/TF+A/R group, however, TF expression was inhibited, while the declined cell viability and the concentrations of SOD, GSH-PX, NO as well as the enhanced LDH, MDA and ET-1 levels occurred during A/R were ameliorated and reversed effectively (P<0.05 to 0.01 versus those in other A/R groups). The results also showed that ROS was increased and PAR-1, PAR-2, p38 MAP kinase and p42/44 MAP kinase were all activated after A/R (P<0.001 versus HUVECs under normoxia), while FVIIai inhibited the increment of ROS, PAR-1, PAR-2, p38 MAP kinase and p42/44 MAP kinase, and improved the changes of TF:C, MDA, SOD, GSH-PX, cell viability and LDH occurred during A/R (P<0.05 to 0.001 versus HUVECs without FVIIai treatment). Conclusion: Tissue factor plays an important role in the development of HUVECs injury induced by anoxia-reoxygenation, inhibition of TF with antisense oligodeoxynucleotide is an effective approach to ameliorate the damage.

show abstract

Induction of lactoferrin and IL‐8 release from human neutrophils by tryptic enzymes via proteinase activated receptor‐2

Cited by 22 publications

References 23 publications

β-Tryptase Regulates IL-8 Expression in Airway Smooth Muscle Cells by a PAR-2–Independent Mechanism

β-Tryptase Regulates IL-8 Expression in Airway Smooth Muscle Cells by a PAR-2–Independent Mechanism

Is there a role for mast cells in psoriasis?

Antisense Oligodeoxynucleotide Against Tissue Factor Inhibits Human Umbilical Vein Endothelial Cells Injury Induced by Anoxia-Reoxygenation

Contact Info

Product

Resources

About