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Biomolecules and Tissue Properties
Published in Joseph W. Freeman, Debabrata Banerjee, Building Tissues, 2018
Joseph W. Freeman, Debabrata Banerjee
Another disease, Ehlers-Danlos syndrome (EDS), is a group of rare genetic disorders caused by a defect in collagen synthesis, varying from mild to life-threatening. EDS is caused by the partial cleavage of the N-propeptide. This allows the N-propeptide to become incorporated within the body of the fibrils. N-propeptides are in a bent-back conformation that is within the overlap region. There can be intact N-propeptides on fibril surfaces in type VII EDS, which alters fibrilogenesis and fiber packing. Common symptoms of EDS include unstable, flexible joints with a tendency to dislocate, ligaments which are overly stretchable, and elastic, fragile, soft skin that easily forms welts and scars. EDS can also affect bones and cause fragile blood vessels and organs.
What do musicians think caused their musculoskeletal symptoms?
Published in International Journal of Occupational Safety and Ergonomics, 2022
Jessica Stanhope, Dino Pisaniello, Philip Weinstein
Various musculoskeletal conditions were reported by 28 (13.1%) musicians as the cause of their MSSs. The specific musculoskeletal conditions reported included arthritis, bursitis, tendinitis, plantar fasciitis, nerve pain, fractures, scoliosis, osteopenia/osteoporosis, Ehlers–Danlos syndrome, flat arches, ‘issues with hip alignment’, hypermobility and fibromyalgia, as well as ‘spinal damage caused by thoracic kyphosis’, ‘deformation of the temporomandibular joint’, ‘congenital hole in the spine’ and ‘jammed lower neck/ribs’. In addition, 12 (5.6%) participants referred to previous injuries.
Exploration of type II and III collagen binding interactions with short peptide-phenyl pyrazole conjugates via docking, molecular dynamics and laboratory experiments
Published in Soft Materials, 2023
Lucy R. Hart, Charlotta G. Lebedenko, Beatriz G. Goncalves, Mia I. Rico, Dominic J. Lambo, Diego S. Perez, Ipsita A. Banerjee
Of particular interest in tissue growth is the role of collagen, as it is the most abundant protein in the human body and plays a critical role.[6] Depending upon the type of tissue, the nature of collagen varies. Thus far, it has been reported that 28 different types of collagen exist and the distribution of various types of collagen depends upon the tissue type and location in the body.[7] While Type I collagen accounts for over 90% of collagen in the body, and has been studied in depth, comparatively lesser studies have focused on other types of collagen, and particularly their interactions with scaffolds. Interestingly, it has been reported that Type IV collagen is the primary constituent of basement membrane, particularly in skin tissue.[8] While all collagens share the triple-helix motif, Type IV collagen lacks a glycine in every third amino acid residue which leads to its relatively kinked structure. Type III collagen, on the other hand, makes up a significant part of connective tissue including in skin, lung, and the vascular endothelial systems. An interesting aspect of Type III collagen is the occurrence of cystine knots at the C-terminal, which is necessary for its stabilization.[9] In the articular cartilage of joints, type III collagen is present in different amounts as a part of the collagen fibrillar complex, cross-linked with collagen Type II.[10] Furthermore, Type III collagen is mostly formed in mature articular cartilage, and plays a critical role in wound healing and chondrocyte behavioral changes upon tissue damage by aiding in binding interactions with the collagen network. Additionally, Type III collagen aids in the fibrillogenesis of Type I collagen and in cardiovascular development,[11] and its mutation or abnormality leads to Type IV Ehlers–Danlos syndrome.[12] Type II collagen is a major constituent of cartilage, intervertebral discs, and the vitreous humor of the eye. It is essential for the proper development of bone and teeth.[13] It has been reported that Type II collagen has three identical α1-polypeptide chains, with significant triple-helical regions and relatively short, non-helical regions that do not contain the typical Gly-Pro-Hyp repeats that are generally found in the triple-helices of collagen.[14] Furthermore, proteoglycans bind to Type II collagen fibrils and stabilize its structure.[15] More importantly, Type II collagen is the main constituent of articular cartilage in mammals[16] and reduces articular chondrocyte hypertrophy and osteoarthritis.[17]