Abstract
Collagen is the primary structural protein of the human body and the main component of connective tissue. In the form of elongated fibrils, collagen is mostly found in fibrous tissues such as tendon, ligament, and skin. We have already demonstrated that pathologic changes of human collagen structures could be monitored by differential scanning calorimetry (DSC), besides the classical histological methods. The aim of the study was to find whether there is a consistent increase or decrease of the thermal parameters, if we compare the changes of calorimetric enthalpy and denaturation temperature of (1) group: degenerative with (2) group: inflamed collagen structures. The degenerative samples were collected from ruptured Quadriceps, Achilles, patellar and anterior cruciate ligament, and degenerated joint capsule of the shoulder. The inflamed tissue samples were collected from palmar aponeurosis in Dupuytren disease, transverse carpal ligament in carpal tunnel syndrome (CTS), and transverse ligament of the first dorsal compartment in De Quervain disease. The thermal denaturation of human samples was monitored by a SETARAM Micro DSC-II calorimeter. All the experiments were performed between 0 and 100 °C. The heating rate was 0.3 K min−1. DSC scans clearly demonstrated significant differences between the two groups, proving that the thermal stability of the degenerative and inflamed pathologic collagens is significantly different. In cases of degenerative samples, the enthalpy decreased, while the melting temperature showed an increase. On the contrary, inflamed samples demonstrated a significant increase in the enthalpy and the melting temperature decreased. Our results indicate that DSC may be a clinically relevant method in the diagnosis of different collagen diseases.
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Acknowledgements
The SETARAM Micro DSC-II was purchased with a grant (CO-272) from the Hungarian Scientific Research Fund (Dénes Lőrinczy).
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Nöt, L.G., Naumov, I., Vámhidy, L. et al. Comparison of thermal characteristics of degenerated and inflamed human collagen structures with differential scanning calorimetry. J Therm Anal Calorim 113, 273–279 (2013). https://doi.org/10.1007/s10973-012-2846-9
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DOI: https://doi.org/10.1007/s10973-012-2846-9