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Connective tissue research2006; 47(2); 85-91; doi: 10.1080/03008200600584124

Thrombospondin-4 and cartilage oligomeric matrix protein form heterooligomers in equine tendon.

Abstract: Injuries of the equine superficial digital flexor tendon are common in racing horses. Knowledge of the tendon matrix composition is crucial to understand physiological and pathological processes in the tendon. The aim of this study was to analyze TSP-4 expressed in equine tendon. Equine tendons were extracted with 10 mM EDTA-containing buffer and TSP-4 purified with ion-exchange chromatography followed by heparin affinity chromatography. The purified TSP-4 was analyzed by one- and two-dimensional SDS-PAGE, immunoblotting, and MALDI-TOF mass spectrometry. Purified TSP-4 gave bands reacting with a TSP-4 specific antiserum, but also with an antiserum to COMP, when submitted to SDS-PAGE under nonreducing conditions. Two-dimensional SDS-PAGE (nonreducing followed by reducing conditions) and immunoprecipitation as well as MALDI-TOF mass spectrometry analysis showed that TSP-4 and COMP are both present in equine tendon and cannot be separated under nonreducing conditions despite significant differences in subunit size. This suggests that they are connected via disulfide bridges into heterooligomers.
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Publication Date: 2006-06-07 PubMed ID: 16754514DOI: 10.1080/03008200600584124Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research exploits a better understanding of the composition of matrix in equine (horse) tendons, particularly focusing on the presence of Thrombospondin-4 (TSP-4). The findings suggest that TSP-4 and a matrix protein named cartilage oligomeric matrix protein (COMP) form complex molecules called heterooligomers within the tendon.

Research Overview

  • This study focuses on analyzing Thrombospondin-4 (TSP-4) present in equine tendon with the aid of biochemical and biophysical procedures. Tendon injuries in horses, particularly racing ones, are common hence, understanding the composition of the tendon may provide insight into these injuries.
  • Equine tendons were used for the study and TSP-4 was extracted using ion-exchange chromatography and heparin affinity chromatography.

Research Methods

  • The extracted TSP-4 was studied using one- and two-dimensional SDS-PAGE, a method used for protein separation, and through immunoblotting, which is an analytical technique used to detect specific proteins.
  • In addition, another form of mass spectrometry named Matrix Assisted Laser Desorption/Ionization – Time of Flight (MALDI-TOF) was used for further protein analysis.
  • During the analysis, reactions were observed with TSP-4 specific antiserum as well as an antiserum that recognizes COMP, another protein found in equine tendon.

Major Findings

  • The key finding of this research is that TSP-4 and COMP were seen together within the equine tendon and could not be separated under certain conditions. Given the notable differences in their size, it was understood that these two proteins must be linked via disulfide bridges into complex units known as heterooligomers.
  • This discovery provides new insights into the protein composition of equine tendons, which may have significant implications in better understanding horse tendon injuries as well as contributing towards better prevention and treatment strategies.

Cite This Article

APA
Södersten F, Ekman S, Schmitz M, Paulsson M, Zaucke F. (2006). Thrombospondin-4 and cartilage oligomeric matrix protein form heterooligomers in equine tendon. Connect Tissue Res, 47(2), 85-91. https://doi.org/10.1080/03008200600584124

Publication

Connective tissue research
ISSN: 0300-8207
NlmUniqueID: 0365263
Country: England
Language: English
Volume: 47
Issue: 2
Pages: 85-91

Researcher Affiliations

Södersten, Fredrik
  • Department B.V.F., Division of Pathology, Swedish Agricultural University, Uppsala, Sweden. frank.sodersten@bvf.slu.se
Ekman, Stina
    Schmitz, Markus
      Paulsson, Mats
        Zaucke, Frank

          MeSH Terms

          • Amino Acid Sequence
          • Animals
          • Cartilage / metabolism
          • Cell Adhesion Molecules / metabolism
          • Chromatography, Affinity
          • Chromatography, Ion Exchange
          • Electrophoresis, Polyacrylamide Gel
          • Extracellular Matrix Proteins / metabolism
          • Glycoproteins / metabolism
          • Horses
          • Matrilin Proteins
          • Molecular Sequence Data
          • Peptide Fragments / metabolism
          • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
          • Tendons / metabolism
          • Thrombospondins / metabolism

          Citations

          This article has been cited 25 times.
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