ArticleBiochemistry2011
Homocysteine modifies structural and functional properties of fibronectin and interferes with the fibronectin-fibrillin-1 interaction.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Case Report: NovelFrontiers in genetics · 2026Article
- Identification and evolutionary analysis of insect fibrillin with their closely related family proteins.PeerJ · 2026Article
- Exploring thoracic aorta ECM alterations in Marfan syndrome: insights into aorta wall structure.Scientific reports · 2025Article
- Extracellular matrix dysregulation in aging, calcification, and cancer diseases: insights into cellular senescence, inflammation, and novel therapeutic strategies.International journal of biological sciences · 2025Review
- Proteomic profiling of extracellular vesicles derived from human serum for the discovery of biomarkers in Avascular necrosis.Clinical proteomics · 2024Article
- Extracellular matrix and vascular dynamics in the kidney of a murine model for Marfan syndrome.PloS one · 2023Article
- Basic Components of Connective Tissues and Extracellular Matrix: Fibronectin, Fibrinogen, Laminin, Elastin, Fibrillins, Fibulins, Matrilins, Tenascins and Thrombospondins.Advances in experimental medicine and biology · 2021Article
- Roles of fibronectin isoforms in neonatal vascular development and matrix integrity.PLoS biology · 2018Article
- Tuning the interactions between chiral plasmonic films and living cells.Nature communications · 2017Article
- Mutations in Fibronectin Cause a Subtype of Spondylometaphyseal Dysplasia with "Corner Fractures".American journal of human genetics · 2017Article
- Moderately Elevated Homocysteine Does Not Contribute to Thoracic Aortic Aneurysm in Mice.The Journal of nutrition · 2017Article
- Tailoring protein nanomechanics with chemical reactivity.Nature communications · 2017Article
- Low bone mineral density is a common finding in patients with homocystinuria.Molecular genetics and metabolism · 2016Article
- Early fibrillin-1 assembly monitored through a modifiable recombinant cell approach.Biomacromolecules · 2014Article
- Epithelial-mesenchymal status influences how cells deposit fibrillin microfibrils.Journal of cell science · 2014Article
- Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Homocystinuria is a genetic disorder resulting in elevated levels of homocysteine in plasma and tissues. Some of the skeletal and ocular symptoms such as long bone overgrowth, scoliosis, and ectopia lentis overlap with symptoms seen in Marfan syndrome. Marfan syndrome is caused by mutations in the extracellular matrix protein fibrillin-1. We previously showed that fibrillin-1 is a target for homocysteine and that the deposition of homocysteinylated fibrillin-1 in the extracellular matrix is compromised. Since the assembly of fibrillin-1 is critically dependent on fibronectin, we analyzed the consequences of fibronectin homocysteinylation and its interaction with fibrillin-1. Cellular fibronectin and proteolytic fragments were homocysteinylated and tested in various interaction assays with recombinant fibrillin-1 and heparin. Fibronectin homocysteinylation consistently compromised the fibronectin-fibrillin-1 interaction, while the interaction with heparin was not affected. Fibronectin homocysteinylation, but not cysteinylation, reduced the fibronectin dimers to monomers as shown by Western blotting. ELISA analyses of homocysteinylated fibronectin with three monoclonal antibodies demonstrated structural changes in the disulfide-containing FNI domains FNI(2), FNI(4), and FNI(9). Using fluorescently labeled fibronectin, we studied the consequence of fibronectin homocysteinylation on assembly in cell culture. Modified fibronectin showed deficiencies in denovo matrix incorporation and initial assembly. In conclusion, we define here characteristic structural changes of fibronectin upon homocysteinylation that translate into functional deficiencies in the fibronectin-fibrillin-1 interaction and in fibronectin assembly. Since fibronectin is a major organizer of various extracellular protein networks, these structural and functional alterations may contribute to the pathogenesis of homocystinuria and Marfan syndrome.
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