У нас вы можете посмотреть бесплатно Lysyl Oxidase activity is required for ordered collagen fibrillogenesis by tendon cells или скачать в максимальном доступном качестве, видео которое было загружено на ютуб. Для загрузки выберите вариант из формы ниже:
Если кнопки скачивания не
загрузились
НАЖМИТЕ ЗДЕСЬ или обновите страницу
Если возникают проблемы со скачиванием видео, пожалуйста напишите в поддержку по адресу внизу
страницы.
Спасибо за использование сервиса ClipSaver.ru
Lysyl Oxidase activity is required for ordered collagen fibrillogenesis by tendon cells. Andreas Herchenhan et al (2015), The Journal of Biological Chemistry http://dx.doi.org/10.1074/jbc.M115.64... Lysyl oxidases (LOXs) are a family of copper- dependent oxido-deaminases that can modify the side-chain of lysyl residues in collagen and elastin, thereby leading to the spontaneous formation of non-reducible aldehyde-derived inter-polypeptide chain cross-links. The consequences of LOX inhibition in producing lathyrism are well documented but the consequences on collagen fibril formation are less clear. Here we used β-aminoproprionitrile (BAPN) to inhibit LOX in tendon-like constructs (prepared from human tenocytes), which are an experimental model of cell- mediated collagen fibril formation. The improvement in structure and strength seen with time in control constructs was absent in constructs treated with BAPN. As expected, BAPN inhibited the formation of aldimine- derived cross-links in collagen and the constructs were mechanically weak. However, an unexpected finding was that BAPN- treatment led to structurally abnormal collagen fibrils with irregular profiles and widely dispersed diameters. Of special interest, the abnormal fibril profiles resembled those seen in some Ehlers-Danlos Syndrome (EDS) phenotypes. Importantly, the total collagen content developed normally, and there was no difference in COL1A1 gene expression. Collagen type V , decorin, fibromodulin and tenascin-X proteins were unaffected by the cross-link inhibition, suggesting that LOX regulates fibrillogenesis independently of these molecules. Collectively, the data show the importance of LOX on the mechanical development of early collagenous tissues, and that LOX is essential for correct collagen fibril shape formation. Good channel: / dlium Subscribe, like and comment. Good website: https://www.dlium.com Bookmark, subscribe and comment.