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Adhesion of soluble fibronectin, laminin, and collagen type IV to intraocular lens materials 1 2

1999; Lippincott Williams & Wilkins; Volume: 25; Issue: 11 Linguagem: Inglês

10.1016/s0886-3350(99)00238-2

1873-4502

Reijo J. Linnola, Malin Sund, Riikka Ylönen, Taina Pihlajaniemi,

Veterinary Equine Medical Research

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°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.