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Autologous Stem Cell Transplantation in Relapsing Polychondritis
Published in Richard K. Burt, Alberto M. Marmont, Stem Cell Therapy for Autoimmune Disease, 2019
Falk Hiepe, Andreas Thiel, Oliver Rosen, Gero Massenkeil, Gerd-Rüdiger Burmester, Andreas Radbruch, Renate Arnold
Although the etiology and pathogenesis of relapsing polychondritis are still unknown, several findings suggest that both humoral and cell-mediated immune responses are involved. Cartilage contains large quantities of type II collagen. Serum autoantibodies to native collagen II as well as to collagen IX and XI were found during acute attacks.2-5 Granular deposits of immunoglobulins and complement were detected at the chondrofibrous junction of affected cartilage by immunofluorescence.6,7 A predominance of HLA-DR positive cells and significant quantities of CD4+ T lymphocytes in cellular infiltrates were found by immunohistology. Susceptibility to relapsing polychondritis is significantly associated with HLA-DR4, and the extent of organ involvement is negatively associated with HLA-DR6.8,9 Experimental immunization of rats with type II collagen can induce auricular chondritis and arthritis. As in humans, the murine lesions were characterized by severe chondritis, positive immunofluorescence reactions to IgG and C3, and circulating IgG that reacted with native type II collagen.10,11
Structure and Function of Cartilage
Published in Kyriacos A. Athanasiou, Eric M. Darling, Grayson D. DuRaine, Jerry C. Hu, A. Hari Reddi, Articular Cartilage, 2017
Kyriacos A. Athanasiou, Eric M. Darling, Grayson D. DuRaine, Jerry C. Hu, A. Hari Reddi
Type II collagen is the predominant collagen type (∼90%) in articular cartilage, comprising more than half the dry weight of the tissue (Deshmukh and Nimni 1973) and complexes with type IX and XI collagens. Type II collagen forms an extracellular framework to resist both imparted tensile forces from articulation and the swelling pressures due to proteoglycans. This collagen serves as a marker for articular cartilage differentiation because it is only localized to the hyaline and fibrous cartilages and the vitreous humor of the eye. The presence of type I collagen with type II helps to distinguish between hyaline and fibrocartilages. Except for small amounts of collagen type I in its superficial zone, collagen type I is not found in hyaline articular cartilage. Since the expression of type I collagen increases with monolayer culture-induced dedifferentiation of chondrocytes, the ratio of type I to type II cartilage is further used to track chondrocyte differentiation.
Mechanical Investigations of Biological Tissues Using Tensile Loading and Indentation
Published in Adil Al-Mayah, Biomechanics of Soft Tissues, 2018
Articular cartilage, another connective tissue, also consists of a fibrous structure. Type-II collagen is the main fibrous protein, which represents 90% of the collagen in the cartilage (Whiting and Zernicke 2008). In stretching, the mechanical response is, to some extent, similar to the ligaments and tendons; however, it does not develop the linear region in the force-deformation response as in stretching of ligaments and tendons. This behavior is related to the random distribution of collagen fibers, shown in Figure 2.13, which prevents the complete recruitment of these fibers under stretching, and also makes the indentation test the most common testing technique for this tissue.
Electrospun natural polymer and its composite nanofibrous scaffolds for nerve tissue engineering
Published in Journal of Biomaterials Science, Polymer Edition, 2020
Fangwen Zha, Wei Chen, Lifeng Zhang, Demei Yu
Type II collagen is mainly produced by chondrocytes and composed of 50–80% the dry weight of articular cartilage. It is insoluble and exhibits the mechanical integrity of connective tissue and also maintains the adhesive qualities [41–43]. Shields and co-workers fabricated three kinds of collagen type II scaffolds by electrospinning technique [44]. Three scaffolds were prepared and evaluated as uncross-linked, cross-linked and cross-linked/seeded. Among them, the uncross-linked fiber showed minimum average diameter and thickness. Mechanical properties were measured, and the results showed electrospun type II collagen nanofiber were stiffer but were not able to attain the high tensile strength of native cartilages. Differences between natural tissue and the uncross-linked scaffolds can be attributed to differing matrix constituents and a lack of hydration in the scaffolds.
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]