- Title
- Fibulin1C peptide induces cell attachment and extracellular matrix deposition in lung fibroblasts
- Creator
- Ge, Qi; Chen, Ling; Jaffar, Jade; Argraves, William Scott; Twal, Waleed O.; Hansbro, Phil; Black, Judith L.; Burgess, Janette K.; Oliver, Brian
- Relation
- Scientific Reports Vol. 5
- Publisher Link
- http://dx.doi.org/10.1038/srep09496
- Publisher
- Nature Publishing Group
- Resource Type
- journal article
- Date
- 2015
- Description
- 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.
- Subject
- metalloproteins; respiratory tract diseases; cell adhesion; cell growth
- Identifier
- http://hdl.handle.net/1959.13/1310867
- Identifier
- uon:22104
- Identifier
- ISSN:2045-2322
- Language
- eng
- Full Text
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