The soluble form of a disintegrin and metalloprotease 33 promotes angiogenesis: Implications for airway remodeling in asthma

Puxeddu, Ilaria; Pang, Yun Yun; Harvey, A.; Haitchi, Hans Michael; Nicholas, Ben; Yoshisue, Hajime; Ribatti, Doménico; Clough, Geraldine F.; Powell, Rob M.; Murphy, Gillian; Hanley, Neil A.; Wilson, David I.; Howarth, Peter H.; Holgate, Stephen T.; Davies, Donna E.

doi:10.1016/j.jaci.2008.03.003

Cited by 92 publications

(99 citation statements)

References 33 publications

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“…Although no major effect on lung development was observed in a mouse deficient of Adam33, 17 this may have been compensated by other Adams or metalloproteases. In view of the expression of ADAM33 in mesenchymal progenitor cells, we suggest that it is involved in controlling their differentiation into smooth muscle, as well as influencing development of other bronchial structures such as the vascular 12 and neural networks of the airways and the submucosal fibroblasts/myofibroblasts and matrix that make up the airway wall.…”

Section: Discussionmentioning

confidence: 99%

“…However, TGF-b also enhances ectodomain shedding of ADAM33, causing the release of sADAM33. 12 Together, these TGF-b-mediated mechanisms might explain how ADAM33/ Adam33 mRNA is suppressed by IL-13 or maternal allergy in the human and murine lung models and why there is an increase in processing/degradation of Adam33 protein in lungs of offspring of mice with allergy in vivo. If these effects translate into human asthma, the presence of sADAM33 in amniotic fluid or BAL fluid of genetically susceptible young children might reflect the early-life influences of the maternal allergic environment on ADAM33 and may be a predictor for persistent wheezing in young children.…”

Section: Discussionmentioning

confidence: 99%

“…5 Full-length ADAM33/Adam33 is synthesized as a proenzyme that is inactivated by a cysteine switch mechanism. 11 Cleavage of the pro-domain by a furin-type protease results in activation of the enzymatically active metalloprotease enzyme, 11,12 which is proangiogenic 12 and can catalyze the shedding of a mutant form of CD23. 13 The ADAM33 disintegrin domain can also interact with the lymphocyte a 9 b 1 integrin and can mediate cell adhesion.…”

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confidence: 99%

“…14 Ectodomain shedding of ADAM33 to yield sADAM33 is enhanced by TGF-b. 12 The role of ADAM33/Adam33 in embryonic lung development has not been elucidated. In human fetal lung, ADAM33 expression has been shown in the mesenchymal progenitor 15 as well as in embryonic lung MRC-5 fibroblasts.…”

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confidence: 99%

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Induction of a disintegrin and metalloprotease 33 during embryonic lung development and the influence of IL-13 or maternal allergy

Haitchi

Bassett

Bucchieri

et al. 2009

Journal of Allergy and Clinical Immunology

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Background: Asthma pathogenesis involves gene and environmental interactions. A disintegrin and metalloprotease 33 (ADAM33)/Adam33 is a susceptibility gene for asthma and bronchial hyperresponsiveness in human beings and mice. ADAM33 is almost exclusively expressed in mesenchymal cells, including mesenchymal progenitors in developing lungs. Objective: Because maternal allergy is a risk factor for asthma, we hypothesized that an allergic environment affects ADAM33/ Adam33 expression during human and mouse lung development. Methods: Human embryonic/fetal lung (HEL) tissues were collected from first-trimester terminations of pregnancy. These were processed immediately or used for explant culture 6 IL-13. MF1 mice or ovalbumin-sensitized A/J mice (Bronchial hyperresponsivness (Bhr)1/Adam33 locus-positive) were timemated and challenged with ovalbumin (A/J mice only) during pregnancy. Lungs were harvested at different times during gestation and post partum. ADAM33/Adam33 expression was analyzed by using reverse transcriptase quantitative polymerase chain reaction and Western blotting. Results: ADAM33 mRNA was detectable in HELs in the pseudoglandular stage of development and showed a significant increase from 7 to 9 weeks postconception. IL-13 significantly suppressed ADAM33 mRNA in HEL explants. In developing murine lungs, Adam33 mRNA and protein expression increased significantly in the early pseudoglandular stage and showed another large increase post partum. In A/J mice, maternal

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Induction of a disintegrin and metalloprotease 33 during embryonic lung development and the influence of IL-13 or maternal allergy

Haitchi

Bassett

Bucchieri

et al. 2009

Journal of Allergy and Clinical Immunology

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“…The identification of ADAM33 (a disintegrase and metalloprotease 33 gene) as a major risk factor in the pathogenesis of bronchial hyperresponsiveness and airway wall remodelling provides insight into the pathogenesis of asthma and represents a novel therapeutic target for drug development. 92 Many patients with severe asthma also turn to alternative medicine. The approaches range from chiropractic to breathing exercises.…”

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confidence: 99%