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, Finland.
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 for each protein, 5 of each type. The amount 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 between the acrylate and the other materials, except PMMA, were significant (P < .01 to .001; PMMA P = .31). Although significantly more laminin bound to acrylate 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 also had significantly higher binding of type IV collagen than the other IOLs (P < .01 to .0001).
Conclusions: It can be hypothesized that if an IOL has more fibronectin bound to it, the IOL can also attach to the capsule better as it consists mainly of collagen. The stronger binding of fibronectin and laminin to acrylate IOLs could be an explanation for the better adhesion of the acrylate IOL to the anterior and posterior capsules and thus for the lower rate of posterior capsule opacification.