ArticleToxicology and applied pharmacology2021
Selectivity of the collagen-binding integrin inhibitors, TC-I-15 and obtustatin.
Article in Toxicology and applied pharmacology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
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- Breast cancer cell coculture induces normal lung fibroblast transition to CAFs, promoting tumor cell dormancy and therapy resistance.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Surface Acoustic Waves-Based Molecular Recognition of a Collagen Receptor on Human Erythrocytes.International journal of molecular sciences · 2025Article
- Integrins and pulmonary fibrosis: Pathogenic roles and therapeutic opportunities.Biomolecules & biomedicine · 2025Review
- Article
- Mesenchymal cell contractility regulates villus morphogenesis and intestinal architecture.Developmental biology · 2025Article
- Structure-Inspired Lineage-Specific Matrix for Endogenous Neurogenesis in Spinal Cord Injury.Research (Washington, D.C.) · 2025Article
- Integrins play a role in stress relaxation of perivascular adipose tissue.Pharmacological research · 2024Article
- The effects of inhibition and siRNA knockdown of collagen-binding integrins on human umbilical vein endothelial cell migration and tube formation.Scientific reports · 2022Article
- Natural Polymers in Heart Valve Tissue Engineering: Strategies, Advances and Challenges.Biomedicines · 2022Review
- Mechanosignals in abdominal aortic aneurysms.Frontiers in cardiovascular medicine · 2022Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Integrins are a family of 24 adhesion receptors which are both widely-expressed and important in many pathophysiological cellular processes, from embryonic development to cancer metastasis. Hence, integrin inhibitors are valuable research tools which may have promising therapeutic uses. Here, we focus on the four collagen-binding integrins α1β1, α2β1, α10β1 and α11β1. TC-I-15 is a small molecule inhibitor of α2β1 that inhibits platelet adhesion to collagen and thrombus deposition, and obtustatin is an α1β1-specific disintegrin that inhibits angiogenesis. Both inhibitors were applied in cellular adhesion studies, using synthetic collagen peptide coatings with selective affinity for the different collagen-binding integrins and testing the adhesion of C2C12 cells transfected with each. Obtustatin was found to be specific for α1β1, as described, whereas TC-I-15 is shown to be non-specific, since it inhibits both α1β1 and α11β1 as well as α2β1. TC-I-15 was 100-fold more potent against α2β1 binding to a lower-affinity collagen peptide, suggestive of a competitive mechanism. These results caution against the use of integrin inhibitors in a therapeutic or research setting without testing for cross-reactivity.
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