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Cartilage: Volume 1: Physiology and Development by Susanne Grässel, Attila Aszódi

By Susanne Grässel, Attila Aszódi

In 3 Volumes this mini ebook sequence provides present wisdom and new views on cartilage as a really good but flexible tissue. this primary quantity offers a finished evaluate at the simple composition and improvement of cartilaginous tissues by way of the outline of the main signaling pathways which keep an eye on cartilage morphogenesis and function.
This publication addresses Professors, researchers and PhD scholars who're drawn to musculoskeletal and cartilage biology.

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Additional resources for Cartilage: Volume 1: Physiology and Development

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1998). Collagen IX stabilizes these individual fibrils (Eikenberry and Bruckner 1999) and directs their organization into a fibrillar network. Deletion of the α1 (IX) chain of the heterotrimeric molecule leads to a functional knockout of the entire collagen IX protein (Fässler et al. 1994; Hagg et al. 1997). Lack of collagen IX impairs cartilage matrix integrity by subsequent loss of COMP and matrilin-3. The association of matrilin-3 with collagen fibrils is critically dependent on the presence of collagen IX and to some extent of COMP, as fibrils isolated from α1 (IX) collagen-deficient mice are almost devoid of matrilin-3 and COMP-deficient collagen fibrils exhibit a reduced matrilin-3 decoration (Budde et al.

Aspberg Vogel KG, Paulsson M, Heinegård D (1984) Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon. Biochem J 223(3):587–597 von Marschall Z, Fisher LW (2010) Decorin is processed by three isoforms of bone morphogenetic protein-1 (BMP1). Biochem Biophys Res Commun 391(3):1374–1378. 1016/j. 067 Wang Z, Weitzmann MN, Sangadala S, Hutton WC, Yoon ST (2013) Link protein N-terminal peptide binds to bone morphogenetic protein (BMP) type II receptor and drives matrix protein expression in rabbit intervertebral disc cells.

Clearly demonstrated that vertebral bodies of newborn collagen IX-deficient mice were smaller and showed an increased mineral density compared to wild-type animals (Kamper et al. 2015). At birth, the lack of collagen IX led to a disrupted cellular organization in the cartilaginous end plate and to a smaller nucleus pulposus of the IVD. Expression levels and localization of other extracellular matrix proteins were strongly altered accompanied by a softening of cartilaginous tissues. In older animals, absence of collagen IX caused earlier and more pronounced disk degeneration with annular fissures.

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