ArticleMolecular biology of the cell1994
Cell-type specific adhesive interactions of skeletal myoblasts with thrombospondin-1.
Article in Molecular biology of the cell, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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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
35 citing papers in PubMed, 82 citations in OpenAlex.
- THBS1 as a Key Regulator of Myoblasts: Validation of Its Inhibitory Roles in Skeletal Muscle Development.Genes · 2026Article
- DExD-Box Helicase 21 Enhances Myometrial Contractions Through Thrombospondin-1-Mediated Increase in Cell Adhesion.Journal of cellular and molecular medicine · 2024Article
- Thrombospondins: Conserved mediators and modulators of metazoan extracellular matrix.International journal of experimental pathology · 2024Review
- Involvement of phosphatidylserine receptors in the skeletal muscle regeneration: therapeutic implications.Journal of cachexia, sarcopenia and muscle · 2022Review
- Thrombospondin-4 in tissue remodeling.Matrix biology : journal of the International Society for Matrix Biology · 2019Review
- Tenascin-C: Form versus function.Cell adhesion & migration · 2015Review
- Control of organization and function of muscle and tendon by thrombospondin-4.Matrix biology : journal of the International Society for Matrix Biology · 2014Article
- Heparan sulfate modification of the transmembrane receptor CD47 is necessary for inhibition of T cell receptor signaling by thrombospondin-1.The Journal of biological chemistry · 2011Article
- CD47 knockout mice exhibit improved recovery from spinal cord injury.Neurobiology of disease · 2011Article
- Review
- Cartilage oligomeric matrix protein promotes cell attachment via two independent mechanisms involving CD47 and alphaVbeta3 integrin.Molecular and cellular biochemistry · 2010Article
- The interaction of Thrombospondins with extracellular matrix proteins.Journal of cell communication and signaling · 2009Article
- The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation.Molecular & cellular proteomics : MCP · 2009Article
- Chemical synthesis and biotinylation of the thrombospondin domain TSR2.Protein science : a publication of the Protein Society · 2009Article
- Phosphatidylserine-positive erythrocytes bind to immobilized and soluble thrombospondin-1 via its heparin-binding domain.Translational research : the journal of laboratory and clinical medicine · 2008Article
- Article
- Function-blocking antithrombospondin-1 monoclonal antibodies.Journal of thrombosis and haemostasis : JTH · 2006Article
- Biophysical characterization of the signature domains of thrombospondin-4 and thrombospondin-2.The Journal of biological chemistry · 2005Article
- Article
- Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats.The EMBO journal · 2004Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Thrombospondin-1 (TSP-1) is an extracellular matrix glycoprotein that may play important roles in the morphogenesis and repair of skeletal muscle. To begin to explore the role of thrombospondin-1 in this tissue, we have examined the interactions of three rodent skeletal muscle cell lines, C2C12, G8, and H9c2, with platelet TSP-1. The cells secrete thrombospondin and incorporate it into the cell layer in a distribution distinct from that of fibronectin. Myoblasts attach and spread on fibronectin- or thrombospondin-coated substrates with similar time and concentration dependencies. Whereas cells adherent on fibronectin organize actin stress fibers, cells adherent on TSP-1 display prominent membrane ruffles and lamellae that contain radial actin microspikes. Attachment to thrombospondin-1 or the 140-kDa tryptic fragment is mediated by interactions with the type 1 repeats and the carboxy-terminal globular domain. Attachment is not inhibited by heparin, GRGDSP peptide, or VTCG peptide but is inhibited by chondroitin sulphate A. Integrins of the beta 1 or alpha V subgroups do not appear to be involved in myoblast attachment to TSP-1; instead, this process depends in part on cell surface chondroitin sulphate proteoglycans. Whereas the central 70-kDa chymotryptic fragment of TSP-1 does not support myoblast attachment, the carboxy-terminal domain of TSP-1 expressed as a fusion protein in the bacterial expression vector, pGEX, supported myoblast attachment to 30% the level of intact TSP-1. Thrombospondin-4 (TSP-4) is also present in skeletal muscle and a fusion protein containing the carboxy-terminal domain of TSP-4 also supported myoblast adhesion, although this protein was less active on a molar basis than the TSP-1 fusion protein. Thus, the carboxyterminal domain of TSP-1 appears to contain a primary attachment site for myoblasts, and this activity is present in a second member of the thrombospondin family.
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