Let the cell move: Influence of collagen on cell movement.


Cell movement is essential for organisms, and it relies on functions and coordination among cell organelles and cytoskeleton fibers. It reflects the status of cells, without the ability to move, cells could not grow, divide, or expand to areas. Scientists working in Cancer Research, Wound Healing, or Drug Discovery constantly need cell migration experiments enable characterization of conditions and substances effecting physiological processes and functions of cells, so in vitro cell culture technique are constantly improved to optimize cell condition and behavior. 

Extracellular matrix (ECM) proteins such as collagens and elastin used in vitro culture had been reported in many cases to improve cell behaviors. Fibrillar collagen is the most ECM constituent maintaining the structure of most interstitial tissues andorgans.
Collagen also works as signal ligands promoting cell movement via receptors on cell membrane such as integrins1, discoidin domain receptors DDR1 and 2, OSCAR, GPVI, G6b-B, and LAIR-1 of the leukocyte receptor complex (LRC) and mannose family receptor uPARAP/Endo180.2 It has been subsequently observed that collagen substrates alter the morphology, migration, and adhesion of cells and, in some cases, differentiation since 1956.3

Cell migration that collagen and integrin trigger is essential for several cell types.
Four different integrin heterodimers (α1β1, α2β1, α10β1, and α11β1) have been demonstrated to bind collagen for cell migration. The expression of α1 and α2 chains are increased upon VEGF secretion in response to injury and are required for lymphangiogenesis in vivo.4
Genetic inactivation of integrin collagen signaling results in the dysfunction of growth plate chondrocytes.5 α11β1 integrin is expressed in a subset of mesenchymal tissues and modulates PDGF dependent chemotaxis on collagen matrixes.6, 7

In addition, uPARAP/Endo180 was shown to aid in the initial adhesion of fibroblasts to collagen and to accelerate the migration of these cells on a fibrillar collagen matrix.8, 9, 10, 11 [38, 39, 41, 42]
In bone, this receptor is highly expressed on osteoblasts and osteocytes at sites of endochondral and intramembranous ossification during development.8 [38]

Thus, collagen is crucial for cell since it bind multiple receptor families and induce a variety of cellular effects. TOOLS launches collagen products of premium quality in industry for cell culture use. All TOOLS Collagen I products are in quality of > 95% purity by SDS-PAGE and ultra-low endotoxin level (≤ 1.0 EU/ml by LAL assay).
TOOLS Collagen I is supplied in lyophilized format and solution of 3-4 mg/mL respectively, which offers the flexibility to dilute to lower concentrations for various applications.
TOOLS Collagen I is proofed to promote cell adhesion, growth, differentiation, and migration and ideal for establishing 3D and 2.5D culture that mimics extracellular environment.

To see more details about TOOLS collagen I product and scaffold-based 3D culture kit

  1. Hood JD, Cheresh DA. Role of integrins in cell invasion and migration. Nat Rev Cancer. 2002 Feb;2(2):91-100.
  2. Boraschi-Diaz I, Wang J, Mort JS and Komarova SV (2017) Collagen Type I as a Ligand for Receptor-Mediated Signaling. Front. Phys. 5:12.
  3. Erhmann and Gey in 1956 (48) were the first to systematically compare growth of many cell strains and tissue explants on collagen substrates with growth on glass. They reported that collagen gels in many cases improved cell growth. Subsequently, it has been observed that collagen substrates alter the morphology (43, 235), migration (181), and adhesion (97, 113, 159) of cells and, in some cases, differentiation (124, 184).
  4. Hong YK, Lange-Asschenfeldt B, Velasco P. et al. VEGF-A promotes tissue repair- associated lymphatic vessel formation via VEGFR-2 and the alpha1beta1 and alpha2beta1 integrins. FASEB J. 2004;18(10):1111–1113.
  5. Bengtsson T, Aszodi A, Nicolae C. et al. Loss of alpha10beta1 integrin expression leads to moderate dysfunction of growth plate chondrocytes. J Cell Sci. 2005;118(Pt 5):929–936
  6. Popova SN, Rodriguez-Sanchez B, Liden A. et al. The mesenchymal alpha11beta1 integrin attenuates PDGF-BB-stimulated chemotaxis of embryonic fibroblasts on collagens. Dev Biol. 2004;270(2):427–442.
  7. Tiger CF, Fougerousse F, Grundstrom G. et al. alpha11beta1 integrin is a receptor for interstitial collagens involved in cell migration and collagen reorganization on mesenchymal nonmuscle cells. Dev Biol. 2001;237(1):116–129.
  8. Engelholm LH, List K, Netzel-Arnett S, Cukierman E, Mitola DJ, Aaronson H, et al. uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion. J Cell Biol. (2003) 160:1009–15.
  9. Jürgensen HJ, Madsen DH, Ingvarsen S, Melander MC, Gårdsvoll H, Patthy L, et al. A novel functional role of collagen glycosylation: interaction with the endocytic collagen receptor uparap/ENDO180. J Biol Chem. (2011)
  10. Madsen DH, Engelholm LH, Ingvarsen S, Hillig T, Wagenaar-Miller RA, Kjøller L, et al. Extracellular collagenases and the endocytic receptor, urokinase plasminogen activator receptor-associated protein/Endo180, cooperate in
    fibroblast-mediated collagen degradation. J. Biol Chem. (2007) 282:27037–45.
  11. Engelholm LH, Melander MC, Hald A, Persson M, Madsen DH, Jürgensen HJ, et al. Targeting a novel bone degradation pathway in primary bone cancer by inactivation of the collagen receptor uPARAP/Endo180. J Pathol. (2016) 238:120–33.
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