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, 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.

Abnormal adherence junctions in the heart and reduced angiogenesis in transgenic mice overexpressing mutant type XIII collagen.

Type XIII collagen is a type II transmembrane protein found at sites of cell adhesion. Transgenic mouse lines were generated by microinjection of a DNA construct directing the synthesis of truncated alpha1(XIII) chains. Shortened alpha 1(XIII) chains were synthesized by fibroblasts from mutant mice, and the lack of intracellular accumulation in immunofluorescent staining of tissues suggested that the mutant molecules were expressed on the cell surface. Transgene expression led to fetal lethality in offspring from heterozygous mating with two distinct phenotypes. The early phenotype fetuses were aborted by day 10.5 of development due to a lack of fusion of the chorionic and allantoic membranes. The late phenotype fetuses were aborted by day 13.5 of development and displayed a weak heartbeat, defects of the adherence junctions in the heart with detachment of myofilaments and abnormal staining for the adherence junction component cadherin. Decreased microvessel formation was observed in certain regions of the fetus and the placenta. These results indicate that type XIII collagen has an important role in certain adhesive interactions that are necessary for normal development.