Matrix Metalloproteinase-9-Mediated Dendritic Cell Recruitment into the Airways Is a Critical Step in a Mouse Model of Asthma

Vermaelen, Karim; Cataldo, Didier; Tournoy, Kurt G.; Maes, Tania; D’hulst, An I.; Louis, Renaud; Foidart, Jean-Michel; Noël, Agnès; Pauwels, Romain

doi:10.4049/jimmunol.171.2.1016

Cited by 140 publications

(132 citation statements)

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“…Early recruitment of antigen-presenting cells into the airways, an important element of the initial inflammatory response, 24,49 paralleled release of TNF-α, with a peak 1 hour after allergen challenge of sensitized mice. On the other hand, appearance of high levels of SP-D 48 hours later coincided with a second wave of mononuclear cell influx but no TNF-α release.…”

Section: Discussionmentioning

confidence: 99%

Surfactant protein D inhibits TNF-α production by macrophages and dendritic cells in mice

Hortobagyi

Kierstein

Krytska

et al. 2008

Journal of Allergy and Clinical Immunology

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Section: Discussionmentioning

confidence: 99%

Surfactant protein D inhibits TNF-α production by macrophages and dendritic cells in mice

Hortobagyi

Kierstein

Krytska

et al. 2008

Journal of Allergy and Clinical Immunology

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“…The same MMP can have different roles in different conditions. For example, MMP9 contributes to inflammation in mouse models of stroke, heart attack, Alzheimer's disease, some aspects of asthma and other lung inflammatory conditions, aortic aneurysms and autoimmune encephalomyelitis 9,[106][107][108][109][110] ; however, it functions as an anti-inflammatory agent in models of inflammatory skin and kidney diseases 89,111,112 . Current data indicate that MMP12 contributes to emphysema 113,114 , whereas MMP3 and MMP9 contribute to skin inflammatory conditions 89,115 .…”

Section: Mmps In Human Inflammatory Disease Modelsmentioning

confidence: 99%

Matrix metalloproteinases and the regulation of tissue remodelling

Page-McCaw

Ewald

Werb

2007

Nat Rev Mol Cell Biol

2,516

2,124

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Matrix metalloproteinases (MMPs) were discovered because of their role in amphibian metamorphosis, yet they have attracted more attention because of their roles in disease. Despite intensive scrutiny in vitro, in cell culture and in animal models, the normal physiological roles of these extracellular proteases have been elusive. Recent studies in mice and flies point to essential roles of MMPs as mediators of change and physical adaptation in tissues, whether developmentally regulated, environmentally induced or disease associated.The founding member of the matrix metalloproteinase (MMP) family, collagenase, was identified in 1962 by Gross and Lapiere, who found that tadpole tails during metamorphosis contained an enzyme that could degrade fibrillar collagen 1,2 . Subsequently, an interstitial collagenase, collagenase-1 or MMP1, was found in diseased skin and synovium 3 . In vitro, MMP1 initiates degradation of native fibrillar collagens, crucial components of vertebrate extracellular matrix (ECM), by cleaving the peptide bond between Gly775-Ile776 or Gly775-Lys776 in native type I, II or III collagen molecules 3,4 . Further research led to the discovery of a family of structurally related proteinases (23 in human, 24 in mice), now referred to as the MMP family.Interest in MMPs increased in the late 1960s and early 1970s following observations that MMPs are upregulated in diverse human diseases including rheumatoid arthritis and cancer. Importantly, high levels of MMPs often correlated with poor prognosis in human patients (reviewed in REF. 5 ). However, recent clinical data indicate that the relationship between § These authors contributed equally to this paper. Competing interests statementThe authors declare no competing financial interests. DATABASESThe following terms in this article are linked online to: Entrez Genome: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene DmMmp1 | DmMmp2 NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author ManuscriptMMPs and disease is not simple; for example, increased MMP activity can enhance tumour progression or can inhibit it (reviewed in REF. 6 ). This complex relationship between MMP expression and cancer has increased the basic and clinical interest in understanding MMP function in vivo, but it has also focused attention on MMPs and pathology, and relatively less attention has been focused on the normal roles of these enzymes. MMP proteolysisMMPs are members of the metzincin group of proteases, which are named after the zinc ion and the conserved Met residue at the active site 11,12 . Recent work has generated a unified peptidase nomenclature 13 Functions of MMP proteolysisHistorically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. However, MMP proteolysis can create space for cells to migrate, can produce specific substrate-cleavage fragments with independent biological activity, can MMPs in bone modelling and remodellingBone is an important site of ongoing tissue remodelling during development...

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“…6 In a mouse asthma model, loss of the MMP9 gene was found to inhibit the development of allergic inflammation by impairing the recruitment of dendritic cells (DCs) into the alveoli and the local production of proallergic chemokines by DCs. 7 MMP9 levels in bronchoalveolar lavage and in the plasma are positively associated with allergen challenge 8 and severity of disease 9,10 in asthmatic patients, suggesting the involvement of MMP9 in asthma pathogenesis in humans. Compared with what is known about the role of MMP9 in asthma, knowledge regarding AR is limited.…”

Section: Introductionmentioning

confidence: 99%

Association of the MMP9 gene with childhood cedar pollen sensitization and pollinosis

et al. 2012

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Matrix metalloproteinase 9 (MMP9) gene has been shown to be involved in the pathogenesis of allergic rhinitis (AR) and asthma. Previous studies suggested that single-nucleotide polymorphisms (SNPs) of the MMP9 gene conferred a risk for childhood asthma. However, whether the SNPs confer a risk for AR has not been previously investigated. The objective of this study was to investigate whether SNPs of the MMP9 gene are associated with risk of seasonal AR (pollinosis), perennial AR and allergen sensitization. A total of 670 school children were recruited in Japan and genotyped for functional polymorphism in the promoter (-1590C/T: rs3918242) and three amino-acid substitutions (R297Q: rs17576; P574R: rs2250889; R668Q: rs17577). Serum levels of total and specific IgE were determined. Disease status and other clinical characteristics of the subjects were investigated using a questionnaire. Associations between the MMP9 SNPs and both AR and serum IgE levels were evaluated. -1590C/T showed significant association with cedar pollinosis (corrected P (Pcor)¼0.039). R668Q was in strong linkage disequilibrium (LD) with -1590C/T and showed significant association with cedar pollinosis (Pcor¼0.023) and serum cedar pollen-specific IgE level (Pcor¼0.022). A haplotype associated with -1590T and 668Q showed a significant association with cedar pollinosis, orchard grass pollinosis and cedar pollen-specific IgE (Pcor¼0.0012, Pcor¼0.0059 and Pcor¼0.0041, respectively). R297Q and P574R were in weak LD with the rest of the SNPs and did not show significant association with disease. Compared with wild-type MMP9 protein (279R-574P-668R), a variant enzyme (279R-574P-668Q) that showed association with pollinosis had lower activity. However, lower enzyme activity was not associated with disease risk because another variant (279Q-574R-668R) showed lower enzyme activity but was not associated with pollinosis. The -1590T allele and its corresponding haplotype was associated with higher promoter activity and with pollen-specific IgE levels and pollinosis, suggesting that -1590C/T may have more impact on sensitization and disease development than R668Q. Our results suggest that the MMP9 gene confers susceptibility to cedar pollinosis in Japanese children. The MMP9 gene may be associated with pollinosis through sensitization processes. Journal of Human Genetics (2012) 57, 176-183; doi:10.1038/jhg.2011.148; published online 12 January 2012 Keywords: allergic rhinitis; association; cedar pollinosis; haplotype; matrix metalloproteinase; MMP9 gene; serum IgE; SNP INTRODUCTIONThe main symptoms of allergic rhinitis (AR) are nasal congestion caused by mucosal edema; runny nose caused by hypersecretion; and repetitive sneezing. Pollinosis is a seasonal type of AR caused by an allergic reaction to pollen. Japanese cedar pollen is the most common causative allergen for pollinosis in Japan. According to a recent study, the prevalence rates of AR and cedar pollinosis in 2006 were 27.2 and 8.0%, respectively; both of which were higher than the rates in 1996. 1...

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Matrix Metalloproteinase-9-Mediated Dendritic Cell Recruitment into the Airways Is a Critical Step in a Mouse Model of Asthma

Cited by 140 publications

References 49 publications

Surfactant protein D inhibits TNF-α production by macrophages and dendritic cells in mice

Surfactant protein D inhibits TNF-α production by macrophages and dendritic cells in mice

Matrix metalloproteinases and the regulation of tissue remodelling

Association of the MMP9 gene with childhood cedar pollen sensitization and pollinosis

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