TABLE 1.
Gene(s) | Skeletal muscle RNA expression (protein expression myocytes)* | Protein | Form | Appearance | Role | Source |
COL1A1-2 | 1: 11.0 NX (not detected) 2: 12.1 NX (low) | Collagen type I alpha 1 and 2 chains | Fibrils | Endo-, peri-, and epimysium | Forms strong parallel fibers, confers tensile strength and rigidity | Kovanen (2002) |
COL3A1 | 14.5 NX (not detected) | Collagen type III alpha 1 chain | Fibrils | Endo- and perimysium, myotendinous junction | Forms a loose meshwork of fibers, confers compliance | Kovanen (2002) |
COL4A1-6 | 1: 24.6 NX (not detected) 2: 26.3 NX (high) 3: 17.8 NX (not detected) 4: 7.5 NX (no data) 5: 4.8 NX (no data) 6: 1.0 NX (no data) | Collagen type IV alpha 1-6 chains | Helices | Basal lamina | Produces a network structure, constitutes the basis of the basal lamina | Sanes (2003) |
COL5A1-3 | 1: 5.0 NX (not detected) 2: 3.7 NX (no data) 3: 15.4 NX (medium) | Collagen type V alpha 1-3 chains | Fibrils | Endomysium | Control of collagen fibrillogenesis | Kovanen (2002) |
COL6A1-6 | 1: 20.0 NX (not detected) 2: 30.6 NX (not detected) 3: 31.8 NX (not detected) 4: no data 5: 0.2 NX (low) 6: 0.0 NX (medium) | Collagen type VI alpha 1-6 chains | Beaded filaments | Endo-, peri-, and epimysium (α6-chain) Basal lamina (α3-chain) Myotendinous junction (α5-chain) | Interacts with a large number of molecules and cell surface receptors, maintains muscle functional integrity. Mutations associated with fibrosis and Ullrich, Bethlem or Myosclerosis myopathies | Bönnemann (2011), Sabatelli et al. (2012), Cescon et al. (2015) |
COL12A1 | 21.6 NX (medium) | Collagen type XII alpha 1 chain | FACIT | Endo- and perimysium, myotendinous junction | Linkage protein between fibrillar collagens and other ECM components | Jakobsen et al. (2017) |
COL13A1 | 2.7 NX (not detected) | Collagen type XIII alpha 1 chain | MACIT | Neuromuscular junction | Regulation and formation of neuromuscular synapse. Lack associated with myasthenia | Härönen et al. (2017), Heikkinen et al. (2019) |
COL14A1 | 7.6 NX (not detected) | Collagen type XIV alpha 1 chain | FACIT | Endo- and perimysium, myotendinous junction | Linkage protein between fibrillar collagens and other ECM components. Increases following training at myotendinous junction (protection against strain injury?) | Jakobsen et al. (2017) |
COL15A1 | 12.8 NX (low to medium) | Collagen type XV alpha 1 chain | Multiplexin | Basement membrane | Stabilizes muscle cells and microvessels. Guides motor axons toward muscle targets. Deficiency increases vulnerability to exercise-induced muscle injury and leads to mild forms of myopathies | Eklund et al. (2001), Guillon et al. (2016) |
COL18A1 | 8.1 NX (not detected) | Collagen type XVIII alpha 1 chain | Multiplexin | Basement membrane | May bind growth factors. May link the basement membrane to other basement membrane glycoproteins and endomysium | Gillies and Lieber (2011), Heljasvaara et al. (2017) |
COL19A1 | 3.7 NX (low) | Collagen type XIX alpha 1 chain | FACIT | Basement membrane | Presence at early embryonic stages is relevant for the muscle tissue differentiation. Acts as a cross-bridge between fibrils and other extracellular matrix molecules | Khaleduzzaman et al. (1997), Sumiyoshi et al. (2001) |
COL22A1 | 0.5 NX (not detected) | Collagen type XXII alpha 1 chain | FACIT | Myotendinous junction | Integrates ECM and contributes to mechanical stability of the myotendinous junction. Knockdown of COL22A1 results in dystrophy-like muscle phenotype in zebrafish | Koch et al. (2004), Charvet et al. (2013) |
*RNA expression summary shows the consensus RNA-data based on normalized expression (NX) data and protein expression comprises profiles using single as well as independent antibodies directed against different, non-overlapping epitopes on the same protein from the Human Protein Atlas (http://www.proteinatlas.org, Uhlen et al., 2010). FACIT, Fibril Associated Collagen with Interrupted Triple Helices; MACIT: Membrane Associated Collagen with Interrupted Triple Helices. Multiplexin: Collagen with Multiple Triple Helix Interruptions.