A surfactant protein C precursor protein BRICHOS domain mutation causes endoplasmic reticulum stress, proteasome dysfunction, and caspase 3 activation.
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Summary
Results support a model whereby proSP-C BRICHOS mutations induce a dynamic toxic gain-of-function, causing apoptotic cell death both by early ER accumulation leading to an exaggerated unfolded protein response and by enhanced deposition of cellular aggregates associated with proteasome dysfunction.
- Type
- article
- Published
- 2005-06-01
- Cited by
- 255
- References
- 31
- Access
- Open access
- OpenAlex
- https://openalex.org/W2117257160
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:40202807
Keywords
Unfolded protein response, Endoplasmic reticulum, Surfactant protein C, Cell biology, Proteasome
References
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- Association of calnexin with mutant peripheral myelin protein-22 ex vivo: A basis for “gain-of-function” ER diseases
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- Alpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy.
- Impairment of the ubiquitin-proteasome system by protein aggregation.
- Human stomach-specific gene, CA11, is down-regulated in gastric cancer.
- The anatomy and cell biology of peripheral myelin protein-22.
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- Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation.
- Expression of a Human Surfactant Protein C Mutation Associated with Interstitial Lung Disease Disrupts Lung Development in Transgenic Mice*
- Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes.
- Synthesis, processing and secretion of surfactant proteins B and C.
- Low molecular weight human pulmonary surfactant protein (SP5): isolation, characterization, and cDNA and amino acid sequences.
- Structure and properties of surfactant protein C.
- Nonspecific interstitial pneumonia and usual interstitial pneumonia with mutation in surfactant protein C in familial pulmonary fibrosis
Cited by
- Defects in surfactant synthesis: clinical implications.
- A novel surfactant protein C L55F mutation associated with interstitial lung disease alters subcellular localization of proSP-C in A549 cells
- Proteostasis in pediatric pulmonary pathology
- MiR-199a-5p, un « fibromiR » amplificateur de la voie du TGF-beta dans la fibrose pulmonaire idiopathique
- Regulation of the Proteasome: Evaluating the Lung Proteasome as a New Therapeutic Target
- Synthetic pulmonary surfactant : Effects of surfactant proteins B and C and their analogues
- Protein misfolding and amyloid formation
- Interstitial Lung Disease in Childhood: Clinical and Genetic Aspects
- Linking progression of fibrotic lung remodeling and ultrastructural alterations of alveolar epithelial type II cells in the amiodarone mouse model.
- Zellbiologische Charakterisierung von Surfactant Protein C Mutationen bei Interstitiellen Lungenkrankheiten
- The Genetic Approach in Pulmonary Fibrosis
- C‐terminal, endoplasmic reticulum‐lumenal domain of prosurfactant protein C – structural features and membrane interactions
- Pathogenesis of idiopathic pulmonary fibrosis: review of recent findings
- The three R's of lung health and disease: repair, remodeling, and regeneration.
- Protein C Mutation (A267T) Results in ER Retention and Unfolded Protein Response Activation
- Endoplasmic reticulum stress in alveolar epithelial cells is prominent in IPF: association with altered surfactant protein processing and herpesvirus infection.
- The surfactant protein C mutation A116D alters cellular processing, stress tolerance, surfactant lipid composition, and immune cell activation
- Idiopathic Pulmonary Fibrosis
- Fibrosis of Two: Epithelial Cell-Fibroblast Interactions in Pulmonary Fibrosis
- Clinical and ultrastructural spectrum of diffuse lung disease associated with surfactant protein C mutations
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