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The Functional Role of Extracellular Matrix
Published in Claudio Migliaresi, Antonella Motta, Scaffolds for Tissue Engineering, 2014
Eleonora Carletti, Matteo Stoppato, Claudio Migliaresi, Antonella Motta
In particular, collagen types I, III, IV, V, VI, XI, XII, XIV, XV, and XVIII are expressed during skeletal muscle development, while fibrillar types I and III predominate in adult endo-, peri-, and epimysium. Collagen type I is predominant in perimysial, whereas collagen type III is more distributed between endomysium and epimysium. However, it is still not well studied if collagen ratios differ in muscles with different functions. Type V collagen, another fibril-forming collagen, combines with types I and III forming, in perimysium and endomysium, a core for type I collagen fibrils. Types XII and XIV collagen are FACITs mainly found in perimysium.
Biomolecules and Tissue Properties
Published in Joseph W. Freeman, Debabrata Banerjee, Building Tissues, 2018
Joseph W. Freeman, Debabrata Banerjee
Type V collagen is a minor component in most interstitial tissues, placenta, tendon, skin, and cardiovascular tissue. It forms a matrix around cells. Type V forms associations with type I and type III collagen. Type V is in the core, type III forms the outer layer, and type I associates with the outer layer.
Extracellular collagenase isolated from Streptomyces antibioticus UFPEDA 3421: purification and biochemical characterization
Published in Preparative Biochemistry & Biotechnology, 2023
Elizianne Pereira Costa, Romero Marcos Pedrosa Brandão-Costa, Wendell Wagner Campos Albuquerque, Thiago Pajeú Nascimento, Amanda Emmanuelle Sales Conniff, Kethylen Barbara Barbosa Cardoso, Anna Gabrielly Duarte Neves, Juanize Matias da Silva Batista, Ana Lúcia Figueiredo Porto
The anticoagulant assay showed activity for the peptides obtained from type V collagen degradation (Figure 5B) with the maximum activity levels reached after 120 min of collagen hydrolysis. The clotting time was delayed by 32.4 s for the control, by 81.3 s for the native enzyme, and by 120.3 s for the enzyme added of CaCl2, what is plausible since the calcium ion was previously verified as a collagenase activator, making bacterial collagenases attain a complete catalytic activity.[64] Biomolecules with anticoagulant activity are reported as obtained from organisms such as mosquitoes, leeches, snakes, sea cucumbers, among others; however, bioactive peptides derived from collagen hydrolysis are still not well reported,[65–69] what highlights the present study.
Genetic variants within the COL5A1 gene are associated with ligament injuries in physically active populations from Australia, South Africa, and Japan
Published in European Journal of Sport Science, 2023
Javier Alvarez-Romero, Mary-Jessica N. Laguette, Kirsten Seale, Macsue Jacques, Sarah Voisin, Danielle Hiam, Julian A. Feller, Oren Tirosh, Eri Miyamoto-Mikami, Hiroshi Kumagai, Naoki Kikuchi, Nobuhiro Kamiya, Noriyuki Fuku, Malcolm Collins, Alison V. September, Nir Eynon
Collagen genes have been spotlighted as important role players in musculoskeletal injury susceptibility (Bouchard, 2015). Specifically, genetic variants within the COL5A1 3’untranslated region (UTR) are associated with both ligament and tendon injuries (Rahim, Collins, & September, 2016). The COL5A1 gene encodes the α1 chain of type V collagen, which typically forms heterofibrils with types I and III collagens and is an important regulator of fibril assembly and diameter (Gelse, Po ̈schlb, & Aigner, 2003). Motifs within the COL5A1 3’-UTR have been suggested to be involved in regulating the mRNA stability of the COL5A1 transcript (Abrahams, Laguette, Prince, & Collins, 2013; Laguette, Abrahams, Prince, & Collins, 2011). It has been proposed that these COL5A1 associated variants may alter the collagen fibril architecture and structure, thereby modifying tissue biomechanics. (Collins & Posthumus, 2011).