ArticleThe Journal of biological chemistry2013
Fibulin-3, -4, and -5 are highly susceptible to proteolysis, interact with cells and heparin, and form multimers.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 51 citations in OpenAlex.
- Fibulin-4 expressed in metastatic breast cancer is a target of peptide-based imaging probes and experimental therapeutics.Molecular therapy. Oncology · 2026Article
- Impact of N-linked glycans on the dual short fibulin/LTBP-4 axes regulating elastogenesis.The FEBS journal · 2025Article
- A spectrum of cysteine mutations in fibulin-3 highlight its disulfide bonding complexity and potential to induce ER stress.Scientific reports · 2025Article
- Induction of cardiac fibulin-4 protects against pressure overload-induced cardiac hypertrophy and heart failure.Communications biology · 2025Article
- Fibulin-4 and latent-transforming growth factor beta-binding protein-4 interactions with syndecan-2 and syndecan-3 are required for elastogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Exploring ocular fibulin-3 (EFEMP1): Anatomical, age-related, and species perspectives.Biochimica et biophysica acta. Molecular basis of disease · 2024Article
- Microfibril-associated glycoprotein 4 forms octamers that mediate interactions with elastogenic proteins and cells.Nature communications · 2024Article
- The role of periostin in cardiac fibrosis.Heart failure reviews · 2024Review
- Citrullination of matrisomal proteins in health and diseases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Review
- ADAMTS7: a Novel Therapeutic Target in Atherosclerosis.Current atherosclerosis reports · 2023Review
- Proteome-wide comparison of tertiary protein structures reveals molecular mimicry inFrontiers in parasitology · 2023Article
- TAILS Identifies Candidate Substrates and Biomarkers of ADAMTS7, a Therapeutic Protease Target in Coronary Artery Disease.Molecular & cellular proteomics : MCP · 2022Article
- PAD2-mediated citrullination of Fibulin-5 promotes elastogenesis.Matrix biology : journal of the International Society for Matrix Biology · 2021Article
- Fibulin-4 exerts a dual role in LTBP-4L-mediated matrix assembly and function.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Effect of Protease Inhibitors in Healing of the Vaginal Wall.Scientific reports · 2019Article
- Roles of fibronectin isoforms in neonatal vascular development and matrix integrity.PLoS biology · 2018Article
- Dysregulation of fibulin-5 and matrix metalloproteases in epithelial ovarian cancer.Oncotarget · 2018Article
- Periostin function in communication with extracellular matrices.Journal of cell communication and signaling · 2018Review
- Exogenous miR-29B Delivery Through a Hyaluronan-Based Injectable System Yields Functional Maintenance of the Infarcted Myocardium.Tissue engineering. Part A · 2018Article
- Introductory review: periostin-gene and protein structure.Cellular and molecular life sciences : CMLS · 2017Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Extracellular short fibulins, fibulin-3, -4, and -5, are components of the elastic fiber/microfibril system and are implicated in the formation and homeostasis of elastic tissues. In this study, we report new structural and functional properties of the short fibulins. Full-length human short fibulins were recombinantly expressed in human embryonic kidney cells and purified by immobilized metal ion affinity chromatography. All three fibulins showed various levels of degradation after the purification procedure. N-terminal sequencing revealed that all three fibulins are highly susceptible to proteolysis within the N-terminal linker region of the first calcium-binding epidermal growth factor domain. Proteolytic susceptibility of the linker correlated with its length. Exposure of these fibulins to matrix metalloproteinase (MMP)-1, -2, -3, -7, -9, and -12 resulted in similar proteolytic fragments with MMP-7 and -12 being the most potent proteases. Fibulin-3 proteolysis was almost completely inhibited in cell culture by the addition of 25 μm doxycycline (a broad spectrum MMP inhibitor). Reducible fibulin-4 dimerization and multimerization were consistently observed by SDS-PAGE, Western blotting, and mass spectrometry. Atomic force microscopy identified monomers, dimers, and multimers in purified fibulin-4 preparations with sizes of ∼10-15, ∼20-25, and ∼30-50 nm, respectively. All short fibulins strongly adhered to human fibroblasts and smooth muscle cells. Although only fibulin-5 has an RGD integrin binding site, all short fibulins adhere at a similar level to the respective cells. Solid phase binding assays detected strong calcium-dependent binding of the short fibulins to immobilized heparin, suggesting that these fibulins may bind cell surface-located heparan sulfate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.