Collagens and collagen-related matrix components in the human and mouse eye

The three-dimensional structure of the eye plays an important role in providing a correct optical environment for vision. Much of this function is dependent on the unique structural features of ocular connective tissue, especially of the collagen types and their supramolecular structures. 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. Phylogenetically, most of the collagens are highly conserved between different species, which suggests that collagens also share similar functions in mice and men. Despite considerable differences between the mouse and the human eye, particularly in the proportion of the different tissue components, the difficulty of performing systematic histologic and molecular studies on the human eye has made mouse an appealing alternative to studies addressing the role of individual genes and their mutations in ocular diseases. From a genetic standpoint, the mouse has major advantages over other experimental animals as its genome is better known than that of other species and it can be manipulated by the modern techniques of genetic engineering. Furthermore, it is easy, quick and relatively cheap to produce large quantities of mice for systematic studies. Thus, transgenic techniques have made it possible to study consequences of specific mutations in genes coding for structural components of ocular connective tissues in mice. As these changes in mice have been shown to resemble those in human diseases, mouse models are likely to provide efficient tools for pathogenetic studies on human disorders affecting the extracellular matrix. This review is aimed to clarify the role of collagenous components in the mouse and human eye with a closer look at the new findings of the collagens in the cartilage and the eye, the so-called "cartilage collagens".