ArticleThe Journal of biological chemistry2009
Latent transforming growth factor beta-binding proteins and fibulins compete for fibrillin-1 and exhibit exquisite specificities in binding sites.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.
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Who cites it
110 citing papers in PubMed, 168 citations in OpenAlex.
- Identification and characterization of a Fibrillin-1 derived matrikine for cardiac regeneration and repair.Biomaterials · 2026Article
- The pivotal role of etiology in managing Non-CAH primary adrenal insufficiency in pediatric and adolescent populations: A Single-Center study.Endocrine · 2026Article
- The ADAMTS family: from extracellular matrix proteases to orchestrators of fibrosis.Cell communication and signaling : CCS · 2026Review
- Fibulin 2 Deficiency Drives Epigenetic Hypertension.Hypertension (Dallas, Tex. : 1979) · 2026Article
- The Roles of the Membrane-Anchored Glycoprotein RECK in Animal Development, Tumor Suppression, and Beyond.Life (Basel, Switzerland) · 2026Review
- A latent TGF-β conjugated scaffold improves neocartilage development.Acta biomaterialia · 2026Article
- Identification and characterization of a Fibrillin-1 derived matrikine for cardiac regeneration and repair.bioRxiv : the preprint server for biology · 2025Article
- Structure and Function of the Extracellular Matrix in Normal and Pathological Conditions: Looking at the Bicuspid Aortic Valve.International journal of molecular sciences · 2025Review
- Novel Aortic Dissection Model Links Endothelial Dysfunction and Immune Infiltration.Circulation research · 2025Article
- Review
- New insights into the structural role of EMILINs within the human skin microenvironment.Scientific reports · 2024Article
- Elastogenesis in Focus: Navigating Elastic Fibers Synthesis for Advanced Dermal Biomaterial Formulation.Advanced healthcare materials · 2024Review
- Opposing roles for ADAMTS2 and ADAMTS14 in myofibroblast differentiation and function.The Journal of pathology · 2024Article
- Fibrillin microfibril structure identifies long-range effects of inherited pathogenic mutations affecting a key regulatory latent TGFβ-binding site.Nature structural & molecular biology · 2023Article
- The extracellular matrix glycoprotein fibrillin-1 in health and disease.Frontiers in cell and developmental biology · 2023Review
- Elastic Fibre Proteins in Elastogenesis and Wound Healing.International journal of molecular sciences · 2022Review
- Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation.Matrix biology : journal of the International Society for Matrix Biology · 2022Article
- Molecular Imaging of Aortic Aneurysm and Its Translational Power for Clinical Risk Assessment.Frontiers in medicine · 2022Review
- Genotype-phenotype correlations of marfan syndrome and related fibrillinopathies: Phenomenon and molecular relevance.Frontiers in genetics · 2022Review
- Structural studies of elastic fibre and microfibrillar proteins.Matrix biology plus · 2021Article
50 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
Abstract
Latent transforming growth factor (TGF) beta-binding proteins (LTBPs) interact with fibrillin-1. This interaction is important for proper sequestration and extracellular control of TGFbeta. Surface plasmon resonance interaction studies show that residues within the first hybrid domain (Hyb1) of fibrillin-1 contribute to interactions with LTBP-1 and LTBP-4. Modulation of binding affinities by fibrillin-1 polypeptides in which residues in the third epidermal growth factor-like domain (EGF3) are mutated demonstrates that the binding sites for LTBP-1 and LTBP-4 are different and suggests that EGF3 may also contribute residues to the binding site for LTBP-4. In addition, fibulin-2, fibulin-4, and fibulin-5 bind to residues contained within EGF3/Hyb1, but mutated polypeptides again indicate differences in their binding sites in fibrillin-1. Results demonstrate that these protein-protein interactions exhibit "exquisite specificities," a phrase commonly used to describe monoclonal antibody interactions. Despite these differences, interactions between LTBP-1 and fibrillin-1 compete for interactions between fibrillin-1 and these fibulins. All of these proteins have been immunolocalized to microfibrils. However, in fibrillin-1 (Fbn1) null fibroblast cultures, LTBP-1 and LTBP-4 are not incorporated into microfibrils. In contrast, in fibulin-2 (Fbln2) null or fibulin-4 (Fbln4) null cultures, fibrillin-1, LTBP-1, and LTBP-4 are incorporated into microfibrils. These data show for the first time that fibrillin-1, but not fibulin-2 or fibulin-4, is required for appropriate matrix assembly of LTBPs. These studies also suggest that the fibulins may affect matrix sequestration of LTBPs, because in vitro interactions between these proteins are competitive.
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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.