By Markus J. Seibel, Simon P. Robins, John P. Bilezikian
This up to date variation is a finished treatise that spans the entire variety of easy biochemistry of bone and cartilage parts to the medical evaluate of sickness markers in bone and joint problems. With contributions from over seventy five overseas specialists, this most up-to-date version is critical examining for these taken with skeletal examine in addition to for rheumatologists, endocrinologists, scientific biochemists, and different medical disciplines partaking within the administration of sufferers with bone and cartilage ailments. *Part I presents an up to date account of present wisdom of the constitution, biosynthesis and molecular biology of the key tissue elements *Part II covers the organizational constitution and mobile metabolism of bone and cartilage *Part III bargains with the software of elements particular to bone and cartilage as biomarkers of health and wellbeing and affliction
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Additional resources for Dynamics of Bone and Cartilage Metabolism, Second Edition: Principles and Clinical Applications
Also type V/XI hybrid molecules containing α1(V) and α2(XI) collagen chains were described in articular cartilage [4, 115], in bone , and in vitreous humor . Immunohistochemical identification of type V collagen in tissue sections with antibodies requires demasking of the epitopes with acid or enzymes [118, 119], indicating a dense packing of type V collagen within the type I/V collagen heterofibrils . IV. CARTILAGE COLLAGENS The backbone of all cartilaginous tissues of the vertebrate body is a heterofibril containing type II collagen as the predominant collagen type, into which type XI collagen is incorporated.
Similarly to COL5A2, its promoter is GC-rich with two potential Sp1binding sites [167, 364]. A chondrocyte-specific enhancer element in the murine Col11a2 gene which binds Sox9 and resembles the Col2a1 enhancer confers cartilage-specific expression . B. Type VI Collagen Genes The genes of the three type VI collagen subunits are composed of more than 60 small exons that are multiples of nine bp similar to those of the fibril-forming collagens. Of these, 19 exons in the range between 27–90 bp code for the triple helical part of chicken and human α1(VI) and α2(VI) [216, 366, 367].
Interestingly, the human COL6A1 gene is not always coregulated with COL6A2 or COL6A3. Only α3(VI) expression, but not α1(VI) nor α2(VI), are up-regulated by TGFβ  or down-regulated by IFNγ  . C. Type X Collagen Genes Unlike genes coding for fibril-forming collagens or type VI collagen chains, the genes for type X collagen contain only three exons that are fairly conserved in all CHAPTER 1 Structure, Biosynthesis and Gene Regulation of Collagens in Cartilage and Bone four species investigated: chicken , mouse [381–383], bovine , and human [385, 386].