Figure 1 shows two examples of collagen organization that can be differentiated by the normalized variance of colinearity.
Bone and teeth, for example, consist of collagen and other proteins in conjunction with inorganic calcium phosphate in the form of hydroxyapatite (HA).
Development of such an AF substrate can involve (A) ion channel alterations resulting in shortening and/or enhanced dispersion of atrial refractoriness and (B) heterogeneities in conduction due to interstitial alterations like, for example, accumulation of collagen fibres, inflammatory infiltration or amyloidosis.
It is somewhat surprising that no examples of collagen-binding (i.e. αA-domain-containing) integrins have been found in protostomes since basement membrane and fibrillar collagens are essential components of some of the most primitive invertebrates such as the cnidarian, Hydra vulgaris [ 10, 11].
Figure 2 is an example of BM collagen type IV staining.
For example, in a mouse model of collagen-induced arthritis, treatment of mice with sRAGE significantly reduced synovial inflammation, as well as cartilage and bone destruction [ 5].
For example, the organization of collagen fibrils is largely responsible for transparency and refraction of cornea, lens and vitreous body, and collagens present in the sclera are largely responsible for the structural strength of the eye.
Most of the skin products that have been reported use a natural, synthetic, or hybrid hydrogel as a scaffold (Priya et al. 2008; Currie et al. 2001; Bakakrishnan et al. 2005; Boucard et al. 2007; Powell and Boyce 2009), for example the use of collagen matrix encapsulated with fibroblasts and seeded with keratinocytes (Yang et al. 2000).
For example, the expression of collagen IV and laminin 1 are reciprocally stimulated in both NHK and fibroblasts [48] [49].
By example, parallel bundles of collagen fibrils are found in connective tissues [2] and laminins assemble basement membrane structures [3].
