Fibulin 1C peptide induces cell attachment and extracellular matrix deposition in lung fibroblasts
- Publication Type:
- Journal Article
- Citation:
- Scientific Reports, 2015, 5
- Issue Date:
- 2015-04-02
Open Access
Copyright Clearance Process
- Recently Added
- In Progress
- Open Access
This item is open access.
Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Ge, Q | en_US |
dc.contributor.author | Chen, L | en_US |
dc.contributor.author | Jaffar, J | en_US |
dc.contributor.author | Argraves, WS | en_US |
dc.contributor.author | Twal, WO | en_US |
dc.contributor.author |
Hansbro, P |
en_US |
dc.contributor.author | Black, JL | en_US |
dc.contributor.author | Burgess, JK | en_US |
dc.contributor.author |
Oliver, B |
en_US |
dc.date.available | 2015-03-05 | en_US |
dc.date.issued | 2015-04-02 | en_US |
dc.identifier.citation | Scientific Reports, 2015, 5 | en_US |
dc.identifier.uri | http://hdl.handle.net/10453/41769 | |
dc.description.abstract | Fibulin-1 is an extracellular matrix (ECM) protein, levels of which are elevated in serum and lung tissue from patients with idiopathic pulmonary fibrosis compared to healthy volunteers. Inhibition of fibulin-1C, one of four fibulin-1 isoforms, reduced proliferation and wound healing in human airway smooth muscle (ASM) cells. This study identified the bioactive region/s of fibulin-1C which promotes fibrosis. Seven fibulin-1C peptides were synthesized and used to pre-coat tissue culture plates before lung derived ASM cells and fibroblasts from patients with pulmonary fibrosis (PF), chronic obstructive pulmonary disease (COPD) or neither disease (Control) were plated. Peptide effects on in vitro measures of fibrosis: cell attachment, proliferation and viability, and ECM deposition, were examined. Among these peptides, peptide 1C1 (FBLN1C1) enhanced ASM cell and fibroblast attachment. FBLN1C1 increased mitochondrial activity and proliferation in fibroblasts. In addition, FBLN1C1 stimulated fibulin1 deposition in PF and COPD fibroblasts, and augmented fibronectin and perlecan deposition in all three groups. Peptides FBLN1C2 to FBLN1C7 had no activity. The active fibulin-1C peptide identified in this study describes a useful tool for future studies. Ongoing investigation of the role of fibulin-1 may reveal the mechanisms underlying the pathphysiology of chronic lung diseases. | en_US |
dc.relation.ispartof | Scientific Reports | en_US |
dc.relation.isbasedon | 10.1038/srep09496 | en_US |
dc.subject.mesh | Lung | en_US |
dc.subject.mesh | Extracellular Matrix | en_US |
dc.subject.mesh | Mitochondria | en_US |
dc.subject.mesh | Fibroblasts | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Pulmonary Disease, Chronic Obstructive | en_US |
dc.subject.mesh | Peptide Fragments | en_US |
dc.subject.mesh | Calcium-Binding Proteins | en_US |
dc.subject.mesh | Fibronectins | en_US |
dc.subject.mesh | Extracellular Matrix Proteins | en_US |
dc.subject.mesh | Cell Adhesion | en_US |
dc.subject.mesh | Cell Proliferation | en_US |
dc.subject.mesh | Cell Movement | en_US |
dc.subject.mesh | Cell Survival | en_US |
dc.subject.mesh | Transforming Growth Factor beta1 | en_US |
dc.subject.mesh | Heparan Sulfate Proteoglycans | en_US |
dc.subject.mesh | Calcium-Binding Proteins | en_US |
dc.subject.mesh | Cell Adhesion | en_US |
dc.subject.mesh | Cell Movement | en_US |
dc.subject.mesh | Cell Proliferation | en_US |
dc.subject.mesh | Cell Survival | en_US |
dc.subject.mesh | Extracellular Matrix | en_US |
dc.subject.mesh | Extracellular Matrix Proteins | en_US |
dc.subject.mesh | Fibroblasts | en_US |
dc.subject.mesh | Fibronectins | en_US |
dc.subject.mesh | Heparan Sulfate Proteoglycans | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Lung | en_US |
dc.subject.mesh | Mitochondria | en_US |
dc.subject.mesh | Peptide Fragments | en_US |
dc.subject.mesh | Pulmonary Disease, Chronic Obstructive | en_US |
dc.subject.mesh | Transforming Growth Factor beta1 | en_US |
dc.title | Fibulin 1C peptide induces cell attachment and extracellular matrix deposition in lung fibroblasts | en_US |
dc.type | Journal Article | |
utslib.description.version | Published | en_US |
utslib.citation.volume | 5 | en_US |
utslib.for | 1103 Clinical Sciences | en_US |
utslib.for | 1116 Medical Physiology | en_US |
utslib.for | 0601 Biochemistry and Cell Biology | en_US |
utslib.for | 0299 Other Physical Sciences | en_US |
pubs.embargo.period | Not known | en_US |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science/School of Life Sciences | |
pubs.organisational-group | /University of Technology Sydney/Strength - CHT - Health Technologies | |
utslib.copyright.status | open_access | |
pubs.publication-status | Published | en_US |
pubs.volume | 5 | en_US |
Abstract:
Fibulin-1 is an extracellular matrix (ECM) protein, levels of which are elevated in serum and lung tissue from patients with idiopathic pulmonary fibrosis compared to healthy volunteers. Inhibition of fibulin-1C, one of four fibulin-1 isoforms, reduced proliferation and wound healing in human airway smooth muscle (ASM) cells. This study identified the bioactive region/s of fibulin-1C which promotes fibrosis. Seven fibulin-1C peptides were synthesized and used to pre-coat tissue culture plates before lung derived ASM cells and fibroblasts from patients with pulmonary fibrosis (PF), chronic obstructive pulmonary disease (COPD) or neither disease (Control) were plated. Peptide effects on in vitro measures of fibrosis: cell attachment, proliferation and viability, and ECM deposition, were examined. Among these peptides, peptide 1C1 (FBLN1C1) enhanced ASM cell and fibroblast attachment. FBLN1C1 increased mitochondrial activity and proliferation in fibroblasts. In addition, FBLN1C1 stimulated fibulin1 deposition in PF and COPD fibroblasts, and augmented fibronectin and perlecan deposition in all three groups. Peptides FBLN1C2 to FBLN1C7 had no activity. The active fibulin-1C peptide identified in this study describes a useful tool for future studies. Ongoing investigation of the role of fibulin-1 may reveal the mechanisms underlying the pathphysiology of chronic lung diseases.
Please use this identifier to cite or link to this item:
Download statistics for the last 12 months
Not enough data to produce graph