New PDF release: Cartilage: Volume 1: Physiology and Development

By Susanne Grässel, Attila Aszódi

ISBN-10: 3319295667

ISBN-13: 9783319295664

ISBN-10: 3319295683

ISBN-13: 9783319295688

In 3 Volumes this mini e-book sequence provides present wisdom and new views on cartilage as a really expert but flexible tissue. this primary quantity offers a entire evaluation at the simple composition and improvement of cartilaginous tissues through the outline of the main signaling pathways which control cartilage morphogenesis and function.
This ebook addresses Professors, researchers and PhD scholars who're attracted to musculoskeletal and cartilage biology.

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Additional resources for Cartilage: Volume 1: Physiology and Development

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M301169200 Liu H, McKenna LA, Dean MF (2000) An N-terminal peptide from link protein can stimulate biosynthesis of collagen by human articular cartilage. Arch Biochem Biophys 378(1):116–122. 1758 Lorenzo P, Aspberg A, Önnerfjord P, Bayliss MT, Neame PJ, Heinegård D (2001) Identification and characterization of asporin. a novel member of the leucine-rich repeat protein family closely related to decorin and biglycan. J Biol Chem 276(15):12201–12211 Luehders K, Sasai N, Davaapil H, Kurosawa-Yoshida M, Hiura H, Brah T, Ohnuma S (2015) The small leucine-rich repeat secreted protein Asporin induces eyes in Xenopus embryos through the IGF signalling pathway.

A comparative proteomic analysis of costal cartilage from newborn Col9a1-deficient mice revealed 15 ECM proteins as differentially expressed to rib cartilage from WT controls (Brachvogel et al. 2013). Collagen IX deficiency is associated with dramatically reduced COMP and matrilin-3, consistent with known interactions. Matrilin-1, 2 Collagens in Hyaline Cartilage 33 matrilin-4, epiphycan, and thrombospondin-4 levels were reduced in collagen IX null cartilage, providing the first in vivo evidence for these proteins to belong to the collagen IX interactome.

Binding to integrins avß3/ß5 is crucial for the function of PIIBNP, the main reason why cartilage is protected from the deleterious action of the propeptide as chondrocytes do not express these integrin subunits. These results suggest that PIIBNP may function to maintain the avascularity of cartilage and protect it from tumor cell invasion. In studies with the Col2a1+ex2 mice, it was shown that procollagen IIA was repressed in adult articular cartilage tissue (McAlinden 2014). Inhibition of Col2a1 alternative splicing is apparently well tolerated in these mice during cartilage development, and procollagen IIA appears to compensate quite well for the absence of procollagen IIB.

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


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