Localisation of laminin and fibronectin during rat lens morphogenesis

Abstract

Immunofluorescence clearly localised laminin and fibronectin in the basement membranes of ocular epithelia through all stages of rat lens differentiation. Some fibronectin is also localised around the mesodermal cells associated with the epithelia. At 10 days of embryonic development, the presumptive lens ectoderm and optic vesicle are closely associated, and the "interspace" between the two tissues contains only a few mesodermal cells. Later, as the mesoderm is excluded and the lens placode invaginates to form the lens pit, there is a marked increase in the concentration of both laminin and fibronectin in the interspace. At about 13 days, the interspace widens, and there is fluorescence for both glycoproteins in the basement membranes of the optic cup and lens vesicle; as the lens capsule thickens, the fluorescence for laminin increases in the latter. The unlabelled peroxidase anti-peroxidase (PAP) method shows that 'blebs' and 'blisters' of basement membranes, particularly from the optic vesicle, appear to give rise to cords of fibronectin- and laminin-positive material. These cords extend into the interspace and are associated with flocculent and fibrillar material. Therefore, the glycoproteins probably combine with other extracellular matrix (ECM) constituents, e.g. collagen, to form a network of fibrils in the interspace. This network must provide good adhesion between the lens placode and the optic vesicle so that invagination is co-ordinated to form the lens pit and the optic cup, respectively. It is suggested that, in addition to providing good adhesion between the tissues, this laminin- and fibronectin-rich ECM may stimulate the formation of basal extensions and cytoplasmic processes, particularly from the lens placode, and therefore, initiate the ectoderm to form lens placode.