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Articular Cartilage Pathology and Therapies
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
Not surprisingly, many of the candidate genes identified are those of the articular cartilage extracellular matrix. Candidate genes identified through familial studies are matrix genes such as COL2A1, COL1A1, cartilage oligomeric matrix protein (COMP), aggrecan (ACAN), matrilin 3 (MATN3), and asporin (ASPN) (Bleasel et al. 1999; Meulenbelt et al. 1999; Mustafa et al. 2000; Stefansson et al. 2003; Kizawa et al. 2005). However, more distantly associated genes involved in the development and maintenance of the joint have also been implicated (Sandell 2012).
Skin proteomics – analysis of the extracellular matrix in health and disease
Published in Expert Review of Proteomics, 2020
Jörn Dengjel, Leena Bruckner-Tuderman, Alexander Nyström
MS-based proteomics have been used since the early 2000s as an analytic tool for studying wound healing [159]. Despite the obvious necessity for wound healing of a timely and well-coordinated deposition and arrangement of the ECM, few studies have directly by means of proteomics interrogated the ECM in physiological and pathophysiological wounds. The insights toward specific changes in the ECM that have come from general proteomic analyses of diseased skin are scarce and often limited to the description of altered abundance in individual proteins. Collagen VI was shown to be increased in human scleroderma skin [160] and the SLRP asporin in human keloids. In one of the few studies with a more direct focus on the ECM in normal and pathologically healing skin Eming et al. compared wound exudates from healing leg wounds and chronic venous leg ulcers [161]. Healing wounds showed an increased abundance of collagen I, collagen III, perlecan, COMP, lumican, and fibulin. Contrastingly, exudates from chronic wounds contained more transitional ECM proteins, fibronectin, and vitronectin. Chronic ulcers also contained a unique abundance of olfactomedin-4, an ECM protein with reported immunosuppressive activities [161,162]. In addition, chronic wounds showed an imbalance in proteolytic activities due to the dysregulated balance of proteases and protease inhibitors [161].
Class I small leucine-rich proteoglycans (SLRPs) colocalise with the Aβ2M amyloid deposits: implications for the roles of SLRP core proteins in the pathogenesis of dialysis-related amyloidosis
Published in Amyloid, 2019
Itaru Yamaguchi, Yasuo Kokubo, Taro Yamashita, Mitsuharu Ueda, Tadakazu Okoshi, Akihiko Matsumine, Yukio Ando, Hironobu Naiki
In the proteomic analysis, 68 molecules including β2-m were detected in all tissues and 100 molecules were detected in 3 of 4 tissues. SLRPs, such as decorin, biglycan, lumican, fibromodulin, mimecan and prolargin were detected in all tissues, and asporin was detected in 3 of 4 tissues. Immunohistochemically, class I SLRPs of decorin, biglycan and asporin were strongly stained in a diffuse or mosaic pattern. These SLRPs-positive areas almost overlapped with Congo-red positive amyloid deposits. Class II SLRPs of lumican and fibromodulin exhibited weak staining intensity at the periphery of Congo-red positive amyloid deposits. Prolargin was weakly stained only in one case. Class III SLRPs of mimecan exhibited weak staining intensity in a diffuse or mosaic pattern.