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The Extracellular Matrix as a Substrate for Stem Cell Growth and Development and Tissue Repair
Published in Richard K. Burt, Alberto M. Marmont, Stem Cell Therapy for Autoimmune Disease, 2019
Stephen F. Badylak, Mervin C. Yoder
Collagen types other than type I collagen exist in the ECM of virtually every tissue and organ, albeit in much lower quantities. These alternative collagen types each provide distinct mechanical and physical properties to the ECM and contribute to the population of ligands that interact with the resident cell populations. By way of example, Type III collagen exists within selected submucosal ECMs, such as the submucosal ECM of the urinary bladder; a location in which less rigid structure is required for appropriate function than is required in a tendinous or ligamentous location. Type IV collagen is present within the basement membrane of all vascular structures and is an important ligand for endothelial cells. Type VI collagen functions as a “connector” of glycosaminoglycan and functional proteins to larger structural proteins such as type I collagen, thus helping to provide a gel like consistency to the ECM. Type VII collagen is an essential component of the anchoring fibrils of keratinocytes to the underlying basement membrane of the epidermis. Each of these collagen types is of course the result of specific gene expression patterns as cells differentiate and tissues and organs develop and spatially organize.
Age-specific response of skeletal muscle extracellular matrix to acute resistance exercise: A pilot study
Published in European Journal of Sport Science, 2019
Barbara Wessner, Michael Liebensteiner, Werner Nachbauer, Robert Csapo
In contrast to COL1A1, COL7A1 gene expression was decreased 6 h after the resistance exercise bout. This effect was detected by the PCR array and confirmed on individual samples, whereby a higher relative 1-RM was associated with a higher reduction in COL7A1 mRNA levels. Collagen type VII is a major structural component of anchoring fibrils, found immediately beneath the lamina densa of many epithelia (Nystrom et al., 2013). Genetic mutations in the COL7A1 gene and the resulting alterations in the morphology and numbers of anchoring fibrils are responsible for various dystrophic forms of epidermolysis bullosa (Kuttner et al., 2013). The loss of collagen VII in dermal fibroblasts has a global impact on the cellular microenvironment and is associated with proteome alterations such as a decrease in basement membrane components and an increase in dermal matrix proteins, TGF-β and metalloproteases (Kuttner et al., 2013). Interestingly, COL7A1 expression in skin increases with age (Glass et al., 2013). Besides the generally high expression of COL7A1 in skin tissue, low amounts of mRNA have also been detected in skeletal muscle tissue (Uhlen et al., 2015). Our results indicate that COL7A1 may be involved in the resistance exercise-induced remodelling of the muscular extracellular matrix, but further studies are required to elucidate the underlying mechanisms.