Increased expression of ADAM33 and ADAM8 with disease progression in asthma

Foley, Susan; Mogas, Andrea; Olivenstein, Ron; Fiset, Pierre; Chakir, Jamila; Bourbeau, Jean; Ernst, Pierre; Lemière, Catherine; Martin, James G.; Hamid, Qutayba

doi:10.1016/j.jaci.2006.12.665

Cited by 137 publications

(144 citation statements)

References 33 publications

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“…The latter study showed ADAM33 to be expressed in human pulmonary fibroblasts and bronchial smooth muscle tissue, yet not in epithelial cells. Our findings are in line with more recent publications that showed ADAM33 to be localized in epithelium [8,28]. Low mRNA levels of ADAM33 are shown in bronchial biopsies although no mRNA was found in epithelial cells from bronchial brushes [29].…”

Section: Discussionsupporting

confidence: 93%

Expression of ADAMs (“a disintegrin and metalloprotease”) in the human lung

et al. 2009

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In view of the associations of "a disintegrin and metalloprotease" (ADAM) with respiratory diseases, we assessed the expression of various ADAMs in human lung tissue. Lung tissue was obtained from nine individuals who underwent surgery for lung cancer or underwent lung transplantation for emphysema. Also, 16HBE 14o-(human bronchial epithelial) and A549 (alveolar type II epitheliumlike) cell lines were used. Immunohistochemistry was performed with antibodies recognizing different ADAM domains. The ADAMs were typically distributed over the bronchial epithelium. ADAM8 and ADAM10 were expressed diffusely in all layers of the epithelium. ADAM9, ADAM17, and ADAM19 were predominantly expressed in the apical part of the epithelium, and ADAM33 was predominantly and strongly expressed in basal epithelial cells. In smooth muscle, ADAM19 and ADAM17 were strongly expressed, as was ADAM33, though this expression was weaker. ADAM33 was strongly expressed in vascular endothelium. All ADAMs were generally expressed in inflammatory cells. The typical distribution of ADAMs in the lung, especially in the epithelium, is interesting and suggests a localized function. As most ADAMs are involved in release of (pro-) inflammatory mediators and growth factors, they may play an important role in the first line of defense and in initiation of repair events in the airways.

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Section: Discussionsupporting

confidence: 93%

Expression of ADAMs (“a disintegrin and metalloprotease”) in the human lung

et al. 2009

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“…ADAM-17 expression and activity are increased in inflammatory bowel diseases [47]. A strong association has been established between ADAM-33 and asthma-related bronchial hyperresponsiveness in humans [48][49][50]. ADAM-8 expression is increased in an animal model of asthma following allergen exposure [51] and in the bronchi of human asthmatics [48,52].…”

Section: Implication Of Adams and Adamtss In Physiology And Pathologymentioning

confidence: 99%

“…A strong association has been established between ADAM-33 and asthma-related bronchial hyperresponsiveness in humans [48][49][50]. ADAM-8 expression is increased in an animal model of asthma following allergen exposure [51] and in the bronchi of human asthmatics [48,52]. ADAMTS-4 and TS-5 are involved in the turnover of aggrecan from cartilage resulting in loss of functionality of tissue and joint disability [53][54][55][56].…”

Section: Implication Of Adams and Adamtss In Physiology And Pathologymentioning

confidence: 99%

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

et al. 2008

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A disintegrin and metalloproteinases (ADAMs) are a recently discovered family of proteins that share the metalloproteinase domain with matrix metalloproteinases (MMPs). Among this family, structural features distinguish the membrane-anchored ADAMs and the secreted ADAMs with thrombospondin motifs referred to as ADAMTSs. By acting on a large panel of membrane-associated and extracellular substrates, they control several cell functions such as adhesion, fusion, migration and proliferation. The current review addresses the contribution of these proteinases in the positive and negative regulation of cancer progression as mainly mediated by the regulation of growth factor activities and integrin functions.

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“…Conditional deletion of ADAM8 shows no apparent phenotype, despite its marked expression in bronchioepithelial cells in the lungs, salivary glands and kidney (Kelly et al, 2005). ADAM8 has been shown to participate in the allergic inflammatory response (Foley et al, 2007, King et al, 2004, Matsuno et al, 2006. in vitro ADAM8 has been shown to process CD23 (Fourie et al, 2003), myelin basic protein (Amour et al, 2002) and a peptide derived from interleukin (IL)-1 type II receptor .…”

Section: Introductionmentioning

confidence: 99%

Novel alternatively spliced ADAM8 isoforms contribute to the aggressive bone metastatic phenotype of lung cancer

et al. 2010

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ADAMs (a disintegrin and metalloprotease) are transmembrane proteins involved in a variety of physiological processes and tumorigenesis. Recently, ADAM8 has been associated with poor prognosis of lung cancer. However, its contribution to tumorigenesis in the context of lung cancer metastasis remains unknown. Native ADAM8 expression levels were lower in lung cancer cell lines. In contrast, we identified and characterized two novel spliced isoforms encoding truncated proteins, D18a and D14 0 , which were present in several tumor cell lines and not in normal cells. Overexpression of D18a protein resulted in enhanced invasive activity in vitro. ADAM8 and its D14 0 isoform expression levels were markedly increased in lung cancer cells, in conditions mimicking tumor microenvironment. Moreover, addition of supernatants from D14 0 -overexpressing cells resulted in a significant increase in tartrate-resistant acid phosphatase þ cells in osteoclast cultures in vitro. These findings were associated with increased pro-osteoclastogenic cytokines interleukin (IL)-8 and IL-6 protein levels. Furthermore, lung cancer cells overexpressing D14 0 increased prometastatic activity with a high tumor burden and increased osteolysis in a murine model of bone metastasis. Thus, the expression of truncated forms of ADAM8 by the lung cancer cells may result in the specific upregulation of their invasive and osteoclastogenic activities in the bone microenvironment. These findings suggest a novel mechanism of tumor-induced osteolysis in metastatic bone colonization.

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Increased expression of ADAM33 and ADAM8 with disease progression in asthma

Cited by 137 publications

References 33 publications

Expression of ADAMs (“a disintegrin and metalloprotease”) in the human lung

Expression of ADAMs (“a disintegrin and metalloprotease”) in the human lung

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

Novel alternatively spliced ADAM8 isoforms contribute to the aggressive bone metastatic phenotype of lung cancer

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