Fibulins: a versatile family of extracellular matrix proteins
Abstract
Fibulins are a newly recognized family of extracellular matrix proteins. The five known members of the family share an elongated structure and many calcium-binding sites, owing to the presence of tandem arrays of epidermal growth factor-like domains. They have overlapping binding sites for several basement-membrane proteins, tropoelastin, fibrillin, fibronectin and proteoglycans, and they participate in diverse supramolecular structures. New insights into their biological roles are now emerging from studies of transgenic mice and of some inherited human diseases.
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Fibulin-1 is a secreted glycoprotein that binds to a number of ECMs including fibronectin, versican, and basal membrane proteins.
“Fibulin-1 is a secreted glycoprotein that binds to a number of ECMs including fibronectin, versican, and basal membrane proteins (27).”
From Reprogramming of three-dimensional microenvironments for in vitro hair follicle induction (2022) · cites this paper as [27]
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Extracellular Matrix Assembly: A Multiscale Deconstruction
Mouw, J. K., Ou, G., & Weaver, V. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3902 · Cited by 1,534 · see citing works
Missense Variations in the Fibulin 5 Gene and Age-Related Macular Degeneration
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Self-citationExtracellular matrix alterations in brains lacking four of its components
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Reprogramming of three-dimensional microenvironments for in vitro hair follicle induction
Kageyama, T., Shimizu, A., Anakama, R., Nakajima, R., Suzuki, K., Okubo, Y., & Fukuda, J. (2022) · Science Advances · doi:10.1126/sciadv.add4603 · Cited by 73 · see citing works
Fibulin-2 is a key mediator of the pro-neurogenic effect of TGF-beta1 on adult neural stem cells
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- Authors
- Timpl, R., Sasaki, T., Kostka, G., & Chu, M.-L.
- Affiliations
- Max Planck Society (DE)
- Thomas Jefferson University (US)
- Corresponding author
- Timpl, Rupert
- ORCID
- Sasaki, Takako
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2003-06-01
- Volume
- 4
- Issue
- 6
- Pages
- 479-489
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2014725746
- Cited by
- 494
- References
- 2
- Citations by year
- 2026: 8 · 2025: 19 · 2024: 29 · 2023: 17 · 2022: 24 · 2021: 21 · 2020: 34 · 2019: 10 · 2018: 20 · 2017: 19 · 2016: 21 · 2015: 25 · 2014: 20 · 2013: 19 · 2012: 21
- FWCI
- 2.52
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- National Institutes of Health
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Connective Tissue Growth Factor Research
- Keywords
- fibulin, extracellular matrix proteins, epidermal growth factor-like domain, calcium binding sites, basement membrane, tropoelastin, fibrillin, fibronectin, proteoglycans, supramolecular structure, transgenic mice
- MeSH terms
- Animals, Binding Sites, Calcium, Calcium-Binding Proteins, Cell Division, Chromosome Mapping, Exons, Extracellular Matrix, Introns, Ligands, Mice, Transgenic, Models, Biological, Models, Molecular, Protein Binding, Alternative Splicing, Protein Structure, Tertiary, Dimerization, Protein Isoforms, Mice
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