Expression of a Disintegrin and Metalloproteinase 33 Protein in Nasal Polyposis: An Immunohistochemical Study

Erbek, Selim S.; Erinanç, Hilal; Erbek, Seyra; Topal, Özgül; Kiyici, Halil

doi:10.2500/ajra.2010.24.3480

Cited by 19 publications

(20 citation statements)

References 18 publications

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“…Previous researches have shown that ADAMs are active in NPs. An immunohistochemical study has found increased expression of ADAM33 protein in vessels and stroma of NPs tissues ( 39 ). Expression of ADAM8 was higher in NPs tissues than in normal nasal mucosa, and there was a positive correlation between the strength of ADAM8 immunostaining and the level of inflammation in NPs tissues ( 40 ).…”

Section: Discussionmentioning

confidence: 99%

A disintegrin and metalloprotease 10-containing exosomes derived from nasal polyps promote angiogenesis and vascular permeability

Zhang

Cheng

et al. 2018

Mol Med Report

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Abnormal angiogenesis and vascular permeability is important for the formation of nasal polyps (NPs). Increasing evidence has indicated that exosomes serve a vital role in modulating angiogenesis and vascular permeability. A disintegrin and metalloprotease 10 (ADAM10), an important type of proteinase that is overexpressed in various diseases, can influence angiogenesis and vascular permeability and has been observed in healthy nasal exosomes. To the best of our knowledge, the expression levels and the function of ADAM10 in NLF-derived exosomes from NPs has not been demonstrated previously. In order to determine the influence of exosomes derived from nasal lavage fluid (NLF) on angiogenesis and vascular permeability, 25 nasal polyp patients and 15 healthy volunteers were enrolled in the present study. NLF was collected from all of the subjects. Exosomes were isolated from NLF, visualized under transmission electron microscope and identified using western blot analysis. The effect of exosomes on human umbilical vein endothelial cells (HUVECs) was measured by tube formation and permeability assays in vitro. The expression of exosomal ADAM10 was also analyzed by western blotting. NLF-derived exosomes from NPs influenced proliferation, tube formation and the permeability of HUVECs. ADAM10 was highly expressed in NLF-derived exosomes from NPs when compared with healthy volunteers. Thus, NLF-derived exosomes from NPs promoted angiogenesis and vascular permeability, which may be associated with abundant ADAM10 in NP exosomes.

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Section: Discussionmentioning

confidence: 99%

A disintegrin and metalloprotease 10-containing exosomes derived from nasal polyps promote angiogenesis and vascular permeability

Zhang

Cheng

et al. 2018

Mol Med Report

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“…These patients' case records were reviewed and used to assess the patients' clinical characteristics. 10 This technique allows large numbers of small, punched-out tissue cores from different cases to be analysed in a single immunohistochemical staining experiment. 8 For statistical analysis, TNM classification, clinical stage and tumour differentiation were grouped as follows: T 1 and T 2 tumours versus T 3 and T 4 tumours; clinical stage I and II tumours versus stage III and IV tumours; moderately and poorly differentiated tumours versus well differentiated tumours, and metastatic node negative tumours versus node positive ones.…”

Section: Methodsmentioning

confidence: 99%

Expression of “a disintegrin and metalloproteinase-33” (ADAM-33) protein in laryngeal squamous cell carcinoma

et al. 2012

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“…and silencing of the ADAM33 promoter (14); however, ADAM33 protein has been localized to epithelial cells by immunohistochemistry (17)(18)(19). This might be because a soluble 55-kD protein (sADAM33) is present in the airways, and may bind to epithelial cells; high levels of sADAM33 have been reported in bronchoalveolar lavage fluid of subjects with asthma, and correlated both with disease severity and reduced lung function (20).…”

Section: Clinical Relevancementioning

confidence: 99%

Regulation of A Disintegrin And Metalloprotease-33 Expression by Transforming Growth Factor-β

Yang

Wicks

Haitchi

et al. 2012

Am J Respir Cell Mol Biol

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The asthma susceptibility gene, a disintegrin and metalloprotease-33 (ADAM33), is selectively expressed in mesenchymal cells, and the activity of soluble ADAM33 has been linked to angiogenesis and airway remodeling. Transforming growth factor (TGF)-b is a profibrogenic growth factor, the expression of which is increased in asthma, and recent studies show that it enhances shedding of soluble ADAM33. In this study, we hypothesized that TGF-b also affects ADAM33 expression in bronchial fibroblasts in asthma. Primary fibroblasts were grown from bronchial biopsies from donors with and those without asthma, and treated with TGF-b 2 to induce myofibroblast differentiation. ADAM33 expression was assessed using quantitative RT-PCR and Western blotting. To examine the mechanisms whereby TGF-b 2 affected ADAM33 expression, quantitative methylation-sensitive PCR, chromatin immunoprecipitation, and nuclear accessibility assays were conducted on the ADAM33 promoter. We found that TGF-b 2 caused a time-and concentration-dependent reduction in ADAM33 mRNA expression in normal and asthmatic fibroblasts, affecting levels of splice variants similarly. TGF-b 2 also induced ADAM33 protein turnover and appearance of a cellassociated C-terminal fragment. TGF-b 2 down-regulated ADAM33 mRNA expression by causing chromatin condensation around the ADAM33 promoter with deacetylation of histone H3, demethylation of H3 on lysine-4, and hypermethylation of H3 on lysine-9. However, the methylation status of the ADAM33 promoter did not change. Together, these data suggest that TGF-b 2 suppresses expression of ADAM33 mRNA in normal or asthmatic fibroblasts. This occurs by altering chromatin structure, rather than by gene silencing through DNA methylation as in epithelial cells. This may provide a mechanism for fine regulation of levels of ADAM33 expression in fibroblasts, and may self-limit TGF-b 2 -induced ectodomain shedding of ADAM33.Keywords: a disintegrin and metalloprotease-33; myofibroblast; transforming growth factor-b; histone modification Asthma is a disease caused by interactions between genetic and environmental factors. It is characterized by variable airflow obstruction and bronchial hyperresponsiveness (BHR) due to airway inflammation and remodeling. In chronic severe asthma, airway inflammation and structural changes both become more intense and are paralleled by an increase in BHR that is only partially or nonresponsive to treatment with corticosteroids (1).A disintegrin and metalloprotease-33 (ADAM33) is a susceptibility gene that has been strongly linked to asthma and BHR (2). There have been a number of case-control and family-based association studies focused on ADAM33, with the majority, including two meta-analyses, confirming the original finding across a wide range of populations (3-5). Furthermore, by applying a candidate gene approach to a genomewide association study data set, the strongest evidence for true association between a previous candidate single-nucleotide polymorphism and asthma was found for rs528557 in ADA...

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Expression of a Disintegrin and Metalloproteinase 33 Protein in Nasal Polyposis: An Immunohistochemical Study

Abstract: This study suggests that the increased expression of ADAM-33 protein may have a role in the pathogenesis of NP.

Cited by 19 publications

References 18 publications

A disintegrin and metalloprotease 10-containing exosomes derived from nasal polyps promote angiogenesis and vascular permeability

A disintegrin and metalloprotease 10-containing exosomes derived from nasal polyps promote angiogenesis and vascular permeability

Expression of “a disintegrin and metalloproteinase-33” (ADAM-33) protein in laryngeal squamous cell carcinoma

Regulation of A Disintegrin And Metalloprotease-33 Expression by Transforming Growth Factor-β

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