Adhesion of soluble fibronectin, laminin, and collagen type IV to intraocular lens materials

Purpose: To evaluate soluble fibronectin, laminin, and collagen IV adhesion to poly(methyl methacrylate) (PMMA), heparin-surface-modified (HSM) PMMA, silicone, acrylate, and hydrogel intraocular lenses (IOLs). Setting: Department of Medical Biochemistry, University of Oulu, Oulu, Finl and. Methods: Seventy-five IOLs were incubated for 24 hours at 37 degrees C With radioactive iodine labeled soluble fibronectin, laminin, or collagen type IV. Twenty-five IOLs were analyzed far each protein, 5 of each type. The am ount of absorbed protein was measured with a gamma counter and expressed as counts per minute (cpm). Results: Fibronectin bound best to the acrylate IOL; the differences betwee n the acrylate and the other materials, except PMMA, were significant (P < .01 to .001; PMMA P = .31). Although significantly more laminin bound to ac rylate than to PMMA, HSM PMMA, or silicone (P < .05 to .001), hydrogel had the highest overall binding of this protein (P < .001 to .0001). Hydrogel a lso had significantly higher binding of type IV collagen than the other IOL s (P < .01 to .0001). Conclusions: It can be hypothesized that if an IOL has more fibronectin bou nd to it, the IOL can also attach to the capsule better as it consists main ly of collagen. The stranger binding of fibronectin and laminin to acrylate IOLs could be an explanation for the better adhesion of the acrylate IOL t o the anterior and posterior capsules and thus for the lower rate of poster ior capsule opacification. J Cataract Refract Surg 1999; 25:1486-1491 (C) 1 999 ASCRS and ESCRS.