By Francis H. Glorieux MD PhD, John M Pettifor, Harald Juppner
Pediatric Bone is the 1st ebook to be released to deal solely with the biology and ailments of bone as they have an effect on little ones. swift advances were made in our figuring out of the mechanisms and elements controlling the expansion and improvement of bone, and those are mentioned intimately during this booklet. extra, many of the illnesses of bone that are atypical to youngsters are highlighted and mentioned within the gentle of our present wisdom in regards to the causation, scientific symptoms and therapy. The booklet is aimed to supply these clinicians drawn to kid's ailments and uncomplicated scientists with a finished source protecting a number of the features of bone health and wellbeing and illness in kids Key beneficial properties* offers solely with bone improvement and illnesses of kids and every bankruptcy written via an * absolutely referenced supplying an appendix of frequently tough to discover info at the research of pediatric bone affliction and reference values* Covers either the body structure of bone and mineral homeostasis in childrens and illnesses in a single e-book* encompasses a CD-ROM of pictures
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Extra info for Pediatric Bone, Second Edition: Biology & Diseases
In woven bone, the collagen fibrils are generally randomly distributed. Lamellar bone contains collagen fibrils that are arranged in parallel layers or sheets running in different directions. Bone osteons have a lamellar structure in which the lamellae are arranged in concentric cylinders. Type V Collagen Type V collagen was first identified in human placenta and dermis, but later studies showed that it is widely expressed in type I collagen-containing tissues including bone [96,97]. The type V collagen molecules exist as heterotrimers a1(V)2a2(V) a1(V) a2(V) a3(V) and as homotrimers a1(V)3 [98,99].
An alternative molecular packing model is the fivestranded Smith microfibril . The microfibril, with a diameter of approximately 4 nm, is the minimum filamentous structure that possesses an axial D repeat. Although their existence is still debated, evidence indicates that they do exist . Three-dimensional image reconstructions of 25-nm diameter collagen fibrils show evidence of a 4-nm repeat in transverse section, which might correspond to ordered arrays of microfibrils, particularly at the level of gapeoverlap junctions.
The mature protein is composed of a central region containing leucine-rich repeats with up to four keratan sulfate chains flanked by disulfide-bonded terminal domains. The amino-terminal domain contains 10 tryosine residues that are partially sulfated . The keratan sulfate chains are attached by N-glycosidic linkages from Nacetylglucosamine to asparagine residues in the central domain of the molecule . In contrast to other SLRPs, fibromodulin does not contain glycosaminoglycan chains in the amino-terminal domain and does not contain chondroitin/dermatan sulfate in any domain.