Tendon extracellular matrix contains pentameric thrombospondin-4 (TSP-4).


In preparations of cartilage oligomeric matrix protein (COMP) from bovine tendon two contaminating polypeptides of 120 and 135 kDa were detected. N-terminal protein sequencing of these polypeptides showed homology to the N-terminus and to an internal sequence in TSP-4, respectively. TSP-4 was further enriched by heparin affinity chromatography. Electron microscopy of this sample shows primarily five armed particles with globular domains at the periphery connected to a central assembly domain in which smaller N-terminal globular domains can be resolved tightly packed at the center of the particle. We can thereby confirm the pentameric model for TSP-4 proposed by Lawler et al. [(1995) J. Biol. Chem. 270, 2809-2814], on the basis of recombinantly expressed protein. We further show that TSP-4 is abundant in tendon.

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@article{Hauser1995TendonEM, title={Tendon extracellular matrix contains pentameric thrombospondin-4 (TSP-4).}, author={Nils Hauser and Mats Paulsson and Anandrao A. Kale and Paul E Dicesare}, journal={FEBS letters}, year={1995}, volume={368 2}, pages={307-10} }