ArticleMatrix biology : journal of the International Society for Matrix Biology2022
Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation.
Article in Matrix biology : journal of the International Society for Matrix Biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 31 citations in OpenAlex.
- Transforming growth factor-β in kidney disease in dogs and cats: a review of the evidence of its role in renal fibrosis.Journal of veterinary internal medicine · 2026Review
- Structural basis for the contribution of latent TGFβ binding protein to TGFβ latency and activation.Nature communications · 2026Article
- Genetic and molecular mechanisms of hereditary thoracic aortic aneurysm and dissection (Review).Molecular medicine reports · 2026Review
- Losartan shows limited benefit in preclinical models of Geleophysic dysplasia.Scientific reports · 2026Article
- Identification and regulatory mechanism analysis of macrophage-related key genes in diabetic nephropathy.Diabetology & metabolic syndrome · 2026Article
- ILC3s mediate intestinal immune-epithelial interactions via TGF-β1 activation.Mucosal immunology · 2026Article
- Pulmonary fibroblast activation during Aspergillus fumigatus infection enhances lung defense via immunomodulation and tissue remodeling.Nature communications · 2026Article
- TGF-β: The Molecular Mechanisms of Atherosclerosis - insights into SMAD Pathways and Gene Therapy Prospects.Current medicinal chemistry · 2026Review
- Composition and Influence of Fibrogenic Niche in Myocardial Fibrosis.Reviews in cardiovascular medicine · 2026Review
- Loss of fibronectin fiber tension is inherent to ECM remodeling in human myocarditis and post-inflammatory fibrosis.Matrix biology plus · 2025Article
- Comparison of Fibrillin-1 and Fibrillin-2 Gene Expression Level in Esophageal Squamous Cell Carcinoma Tumor Tissue and Tumor Margin Tissue.Iranian journal of medical sciences · 2025Article
- Critical Role for Transglutaminase 2 in Scleroderma Skin Fibrosis and in the Development of Dermal Sclerosis in a Mouse Model of Scleroderma.Arthritis & rheumatology (Hoboken, N.J.) · 2025Article
- Transglutaminase 2 Stimulates Cell Proliferation and Modulates Transforming Growth Factor-Beta Signaling Pathway Independently of Epithelial-Mesenchymal Transition in Hepatocellular Carcinoma Cells.International journal of molecular sciences · 2025Article
- Dysregulation of cell migration by matrix metalloproteinases in geleophysic dysplasia.Scientific reports · 2025Article
- A Review on the Role of DNA Methylation in Aortic Disease Associated With Marfan Syndrome.Cardiology research · 2025Review
- Recent advances in targeting obesity, with a focus on TGF-β signaling and vagus nerve innervation.Bioelectronic medicine · 2025Review
- ADAMTS2 promotes radial migration by activating TGF-β signaling in the developing neocortex.EMBO reports · 2024Article
- Transglutaminase 2 knockout mice are protected from bleomycin-induced lung fibrosis with preserved lung function and reduced metabolic derangements.Physiological reports · 2024Article
- TGF-β signaling in health, disease, and therapeutics.Signal transduction and targeted therapy · 2024Review
- Role of transforming growth factor-β in peripheral nerve regeneration.Neural regeneration research · 2024Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 2 countries.
Funding
Abstract
TGFβ superfamily members are potent growth factors in the extracellular matrix with essential roles in all aspects of cellular behaviour. Latent TGFβ binding proteins (LTBPs) are co-expressed with TGFβ, essential for correct folding and secretion of the growth factor, to form large latent complexes. These large latent complexes bind extracellular proteins such as fibrillin for sequestration of TGFβ in the matrix, essential for normal tissue function, and dysregulated TGFβ signalling is a hallmark of many fibrillinopathies. Transglutaminase-2 (TG2) cross-linking of LTBPs is known to play a role in TGFβ activation but the underlying molecular mechanisms are not resolved. Here we show that fibrillin is a matrix substrate for TG2 and that TG2 cross-linked complexes can be formed between fibrillin and LTBP-1 and -3, and their latent TGFβ complexes. The structure of the fibrillin-LTBP1 complex shows that the two elongated proteins interact in a perpendicular arrangement which would allow them to form distal interactions between the matrix and the cell surface. Formation of the cross-link with fibrillin does not change the interaction between latent TGFβ and integrin αVβ6 but does increase TGFβ activation in cell-based assays. The activating effect may be due to direction of the latent complexes to the cell surface by fibrillin, as competition with heparan sulphate can ameliorate the activating effect. Together, these data support that TGFβ activation can be enhanced by covalent tethering of LTBPs to the matrix via fibrillin.
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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 Socratic graph.