Decreased collagen thermal stability as a response to the loss of structural integrity of thyroid cartilage |
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| Authors: | M A Logunova M A Shakhova I V Andreeva N Yu Ingatieva V A Kamenskii V N Bagratiashvili |
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| Institution: | (1) Chemical Department, Lomonosov Moscow State University, Moscow, 119899, Russia;(2) Semashko Regional Clinical Hospital, ul. Rodionova 190, Nizhni Novgorod, 603126, Russia;(3) Institute of Laser and Information Technologies, Russian Academy of Sciences, ul. Pionerskaya 2, Troitsk, 142092, Russia;(4) Institute of Applied Physics, Russian Academy of Sciences, ul. Ulyanova 46, Nizhni Novgorod, 603950, Russia |
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| Abstract: | 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. |
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| Keywords: | collagen thermal stability thyroid cartilage tissue |
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