Decreased collagen thermal stability as a response to the loss of structural integrity of thyroid cartilage

• Published in: Biophysics (Oxford) Vol. 53; no. 5; pp. 470 - 475
• Main Authors: Logunova, M. A., Shakhova, M. A., Andreeva, I. V., Ingatieva, N. Yu, Kamenskii, V. A., Bagratiashvili, V. N.
• Format: Journal Article
• Language: English
• Published: Dordrecht SP MAIK Nauka/Interperiodica 01-10-2008; Springer Nature B.V
• Subjects: Amino acids; Anisotropy; Biological and Medical Physics; Biophysics; Cartilage; Complex Systems Biophysics; Physics; Physics and Astronomy; Thyroid gland; collagen; thyroid cartilage tissue; thermal stability
• ISSN: 0006-3509; 1555-6654
• DOI: 10.1134/S0006350908050266

The amino acid composition, thermal behavior and birefringence properties of thyroid cartilage tissues have been studied. A collagen component in perichondrium consists of type-I and type-II collagens whose fibers form a highly ordered anisotropic structure with a birefringence of 4.75 × 10
−3
and a melting (denaturation) temperature of 65°C. The hyaline constituent, which is visualized as a quasi-anisotropic medium, contains of only type-II collagen, which does not denature in intact tissues at temperatures up to 100°C. However, in tissues whose proteoglycane subsystem is damaged by trypsin, the denaturation of collagen takes place at 60°C. In the integral perichondrium-hyaline system, the temperature of collagen denaturation in the perichondrium reaches 75°C, which indicates the immobilization of collagen in this tissue by the extracellular matrix of the hyaline constituent.