Literature DB >> 11828047

Cell specific expression of peroxiredoxins in human lung and pulmonary sarcoidosis.

V L Kinnula1, S Lehtonen, R Kaarteenaho-Wiik, E Lakari, P Pääkkö, S W Kang, S G Rhee, Y Soini.   

Abstract

BACKGROUND: Six proteins of the peroxiredoxin (Prx) family have recently been characterised which have the capacity to decompose hydrogen peroxide in vivo and in vitro. These proteins may have an important role in the protection of human lung against endogenous and exogenous oxidant stress. However, the expression and distribution of these proteins in healthy human lung and diseased lung tissue is unknown.
METHODS: The cell specific expression of Prxs in healthy lung tissue from four non-smokers and in parenchymal tissue from 10 subjects with pulmonary sarcoidosis was investigated by immunohistochemistry, and expression of these proteins in various cultured lung cells and cells of bronchoalveolar lavage (BAL) fluid of controls and patients with sarcoidosis was assessed by Western blot analysis.
RESULTS: All six Prxs could be synthesised in cultured human lung cells. The bronchial epithelium showed moderate to high expression of Prxs I, III, V and VI, the alveolar epithelium expressed mainly Prxs V and VI, and alveolar macrophages expressed mainly Prxs I and III. Granulomas of subjects with sarcoidosis expressed mainly Prxs I and III. Samples of BAL fluid from controls and from subjects with sarcoidosis had very similar findings, except that Prxs II and III had a tendency for increased immunoreactivity in sarcoidosis tissue.
CONCLUSIONS: Prxs I, III, V, and VI, in particular, have prominent and cell specific expression in human lung tissue. High expression of Prxs I and III in granulomas and alveolar macrophages of sarcoidosis parenchyma may have a significant effect on the oxidant burden and the progression of lung injury in this disease.

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Year:  2002        PMID: 11828047      PMCID: PMC1746258          DOI: 10.1136/thorax.57.2.157

Source DB:  PubMed          Journal:  Thorax        ISSN: 0040-6376            Impact factor:   9.139


  30 in total

1.  Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin.

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2.  Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation.

Authors:  D Y Jin; H Z Chae; S G Rhee; K T Jeang
Journal:  J Biol Chem       Date:  1997-12-05       Impact factor: 5.157

3.  Allergens of Aspergillus fumigatus and Candida boidinii share IgE-binding epitopes.

Authors:  S Hemmann; K Blaser; R Crameri
Journal:  Am J Respir Crit Care Med       Date:  1997-12       Impact factor: 21.405

4.  Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha.

Authors:  S W Kang; H Z Chae; M S Seo; K Kim; I C Baines; S G Rhee
Journal:  J Biol Chem       Date:  1998-03-13       Impact factor: 5.157

5.  Characterization of a mammalian peroxiredoxin that contains one conserved cysteine.

Authors:  S W Kang; I C Baines; S G Rhee
Journal:  J Biol Chem       Date:  1998-03-13       Impact factor: 5.157

6.  Catalase and glutathione reductase protection of human alveolar macrophages during oxidant exposure in vitro.

Authors:  P Pietarinen; K Raivio; R B Devlin; J D Crapo; L Y Chang; V L Kinnula
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7.  Manganese superoxide dismutase, but not CuZn superoxide dismutase, is highly expressed in the granulomas of pulmonary sarcoidosis and extrinsic allergic alveolitis.

Authors:  E Lakari; P Pääkkö; V L Kinnula
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Review 8.  Superoxide radical and superoxide dismutases.

Authors:  I Fridovich
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9.  Primary and immortalized (BEAS 2B) human bronchial epithelial cells have significant antioxidative capacity in vitro.

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10.  Immunocytochemical localization of extracellular superoxide dismutase in human lung.

Authors:  T D Oury; L Y Chang; S L Marklund; B J Day; J D Crapo
Journal:  Lab Invest       Date:  1994-06       Impact factor: 5.662

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  26 in total

Review 1.  Glutathione redox control of asthma: from molecular mechanisms to therapeutic opportunities.

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2.  Peroxiredoxin II expression and its association with oxidative stress and cell proliferation in human idiopathic pulmonary fibrosis.

Authors:  Kirsi Vuorinen; Steffen Ohlmeier; Outi Leppäranta; Kaisa Salmenkivi; Marjukka Myllärniemi; Vuokko L Kinnula
Journal:  J Histochem Cytochem       Date:  2008-07-07       Impact factor: 2.479

Review 3.  Redox control of asthma: molecular mechanisms and therapeutic opportunities.

Authors:  Suzy A A Comhair; Serpil C Erzurum
Journal:  Antioxid Redox Signal       Date:  2010-01       Impact factor: 8.401

Review 4.  Oxidative stress in chronic lung disease: From mitochondrial dysfunction to dysregulated redox signaling.

Authors:  Albert van der Vliet; Yvonne M W Janssen-Heininger; Vikas Anathy
Journal:  Mol Aspects Med       Date:  2018-08-22

Review 5.  Peroxiredoxin 6: a bifunctional enzyme with glutathione peroxidase and phospholipase A₂ activities.

Authors:  Aron B Fisher
Journal:  Antioxid Redox Signal       Date:  2011-03-31       Impact factor: 8.401

6.  Natural Dicarbonyls Inhibit Peroxidase Activity of Peroxiredoxins.

Authors:  V Z Lankin; M G Sharapov; R G Goncharov; A K Tikhaze; V I Novoselov
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Review 7.  Focus on antioxidant enzymes and antioxidant strategies in smoking related airway diseases.

Authors:  V L Kinnula
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8.  Molecular cloning, characterization and mRNA expression of peroxiredoxin in Zhikong scallop Chlamys farreri.

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9.  Peroxiredoxin V contributes to antioxidant defense of lung epithelial cells.

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Review 10.  Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling.

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