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 furthe...

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Bibliographic Details
Published in:FEBS letters 1995-07, Vol.368 (2), p.307-310
Main Authors: Hauser, Nik, Paulsson, Mats, Kale, Ashay A., DiCesare, Paul E.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Bovine tendon
Cartilage oligomeric matrix protein (COMP)
Cattle
Chromatography, Liquid
Extracellular matrix
Extracellular Matrix - chemistry
Extracellular Matrix Proteins
Glycoproteins - chemistry
Glycoproteins - isolation & purification
Glycoproteins - ultrastructure
Heparin - metabolism
Matrilin Proteins
Molecular Sequence Data
Molecular Weight
Protein Structure, Tertiary
Sequence Analysis
Tendons - chemistry
Thrombospondin
Thrombospondins
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00675-Y