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Neurogenetics
Published in John W. Scadding, Nicholas A. Losseff, Clinical Neurology, 2011
Sonia Gandhi, Sarah Tabrizi, Nicholas Wood
Bethlem myopathy is an autosomal dominant disorder with onset at any age. It is characterized by a proximal myopathy and joint contractures, which clinically overlaps with the EMDM phenotype. It is caused by mutations in one of three different genes for collagen type 6: COL6A1, COL6A2 or COL6A3.
Chondrocyte protein co-synthesis network analysis links ECM mechanosensing to metabolic adaptation in osteoarthritis
Published in Expert Review of Proteomics, 2021
Aspasia Destouni, Konstantinos C. Tsolis, Anastassios Economou, Ioanna Papathanasiou, Charalampos Balis, Evanthia Mourmoura, Aspasia Tsezou
Reconstruction of the chondrocyte proteome network also recapitulates the interactions between COL6A1 and COL6A3 alpha chains (MEyellow) with COL6A2 (MEgreenyellow) to compose collagen type VI, a major component of the chondrocyte pericellular matrix (PCM) and were also depleted in OA hypertrophic compared to healthy chondrocytes (Figure 3a) [34,64]. Importantly, in Col6a1 -/- mice, PCM module is decreased compared to WT mice and loses its mechanical properties leading to increased chondrocyte swelling in response to osmotic stress in an age-dependent manner [65]. Similarly, significant loss of PCM stiffness in OA compared to normal chondrons has been detected across the surface, middle and deep zones [66].
A potential dermal substitute using decellularized dermis extracellular matrix derived bio-ink
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2019
Joo-Yun Won, Mi-Hee Lee, Mi-Jeong Kim, Kyung-Hyun Min, Geunseon Ahn, Ji-Seok Han, Songwan Jin, Won-Soo Yun, Jin-Hyung Shim
In addition, to check residual proteins in dECM, SDS PAGE was carried out for LC/MS. Next, after gel slicing, an antibody microarray was used to study the growth factors. The result of LC/MS showed the presence of 51 proteins. Moreover, an identical set of 13 residual proteins in both the normal and skin dECM were found, all from the ECM. These proteins included COL1A1, COL1A2, COL3A1, COL5A2, COL6A2, COL6A3, asporin, dermatopontin, decorin and keratin. The Gene Ontology (GO) analysis of the analysed proteins revealed that the nucleus and cell membrane were detected in normal skin, whereas only the extracellular region and cytoplasm were found in dECM (Figure 2(a)).
Understanding collagen interactions and their targeted regulation by novel drugs
Published in Expert Opinion on Drug Discovery, 2021
Marialucia Gallorini, Simone Carradori
As for the group of collagens of basement membranes and collagen-like membrane, it is composed of types IV, VI, VII, VIII, X, XIII, XV, XVII, XVIII, XXIII, and of collagen-like membrane proteins such as macrophage receptor with collagenous structure (MARCO) and macrophage scavenger receptors [34,35]. Basement membranes (BMs) are fragile and pliable sheets of ECMs that act often as inner surfaces and/or partitions in organisms. Among others, the core structural component of BMs is composed by collagen IV. Additionally, collagens VI, VII, VIII, XV, XVII and XVIII are found at the interface BMs/stroma [36]. Alteration at the gene and protein level of these collagens have been related to rare multi-systemic diseases but also with other major common pathologies including stroke. Milder Bethlem myopathy and severe Ullrich congenital muscular dystrophy (UCMD) are caused by COL6A1/COL6A2/COL6A3 mutations but COL6 mutations can also affect the skin and tendon. The pathogenic molecular mechanisms seem to involve an alteration in the mitochondrial autophagic flux and a defect in the ATP synthesis. Having identified BM-associated collagen mutations, in particular collagen type 6, in several disorders lays the grounds for the identification of treatments eventually effective across distinct disorders [35]. Type X collagen is produced by hypertrophic chondrocytes and it has been related to mineralization, endochondral ossification and angiogenesis [37]. Homologous collagens type XIII, XXIII and XXV are a subgroup of type II transmembrane proteins within the collagen superfamily. It has been reported that collagen XIII could have a crucial role in musculoskeletal tissues, microvessels and inflammation, being localized at the cell focal contacts, and having many interactions with BMs and other ECM proteins involved in cell-cell interactions [38].