Comparison of the effectiveness of 4 anti-inflammatory drops in relieving photophobia after pupil dilation.

PURPOSE: To compare the relative effectiveness of diclofenac, flurbiprofen, ketorolac, and prednisolone acetate in relieving photophobia after pupil dilation for fundus examination. SETTING: Eye, Ear, Nose, and Throat Hospital, New Orleans, Louisiana, USA. METHODS: This prospective, blind, placebo-controlled study comprised 105 patients randomly assigned to 1 of 10 treatment groups. Five minutes after instillation of dilating drops, each patient received drops of different test medications in the right and left eyes. Light sensitivity and pupil measurement tests were performed over 2 hours after the pharmacological mydriasis. After photostimulation, patients were asked to rate their photosensitivity on numerical and analog scales and to indicate a filter value required to alleviate right-induced discomfort. Test results were analyzed to detect differences among the pain levels associated with each treatment. RESULTS: There were no significant differences between the placebo and any active treatment drug at any time during the study. CONCLUSION: These findings suggest that mediators other than prostaglandins may have a role in photosensitivity or that increased postmydriatic photosensitivity is a result of higher light levels entering the eye through the dilated pupil.

Topical carbonic anhydrase inhibitors.

Dorzolamide, a topically active carbonic anhydrase inhibitor, is an effective new glaucoma medication that creates a decrease in intraocular pressure similar to that produced by beta-blockers. When beta-blockers are contraindicated, dorzolamide may be used as a first-line therapy. It has excellent additivity with other topical ocular hypotensive medications, including beta-blockers and pilocarpine. Systemic side effects are minimal, particularly compared with those of oral carbonic anhydrase inhibitors. However, local side effects, including corneal edema in patients with borderline endothelial function, may occur. Decreased visual acuity and allergic reactions, which occur frequently, may curtail the use of dorzolamide in some patients.

Inhibition of tumor implantation at sites of trauma by plasminogen activators.

The authors report on the influence of plasminogen activators (PA) on implantation of TA3Ha mammary tumor cells in the healing hepatic wounds of syngeneic strain A mice. Intravenously injected TA3Ha cells, although they rarely metastasize to the liver, formed tumors in the hepatic wounds of a significant percent (42%, P less than 0.0001) of mice. The frequency of tumor formation declined as the interval between surgery and tumor cell inoculation was increased. Furthermore, preexposure of cells to fibrinogen, fibronectin, laminin, or peptides containing the arginine-glycine-aspartic acid-serine residues dramatically reduced the frequency of tumor formation in the hepatic wounds. These results indicate that TA3Ha cells interact with fibrinogen-related proteins in the wound to aid their attachment and growth. Because these proteins are susceptible to digestion by plasmin, PA were used in this study to examine whether administration of these drugs to the mice would modulate tumor formation in the liver wounds. Among the PA tested, human plasmin B-chain-streptokinase complex (B-SK) and recombinant tissue plasminogen activator (t-PA) inhibited tumor implantation in a dose-related manner. Administration of 900 units (U) of B-SK or 3300 U of t-PA per mouse reduced the frequency of tumor formation from 42% to 0% (P = 0.02) and 11% (P = 0.02), respectively. The B-SK was complexed with p-nitrophenyl-p-guanidinobenzoate; it did not activate the plasminogen or inhibit tumor formation in the hepatic wounds. Although urokinase activated the plasminogen, it did not inhibit tumor implantation in the hepatic wound. Heparin, an anticoagulant that prevents conversion of fibrinogen to fibrin without being fibrinolytic, had no influence on tumor formation in the hepatic wounds. The PA can generate plasmin that digests the cell attachment proteins in wounds and consequently inhibits tumor cell attachment.