Cited by 246Open Access
Cleveland Clinic
Publishes on Protease and Inhibitor Mechanisms, Retinal Diseases and Treatments, Protein Hydrolysis and Bioactive Peptides. 16 papers and 897 citations.
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Counterfeit and substandard antimalarial drugs can cause death and contribute to the growing malaria drug resistance problem, particularly in Southeast Asia. Since 2003 in Cambodia the quality of antimalarial drugs both in the public and private health sector is regularly monitored in sentinel sites. We surveyed 34% of all 498 known facilities and drug outlets in four provinces. We collected 451 drug samples; 79% of these were not registered at the Cambodia Department of Drugs and Food (DDF). Twenty-seven percent of the samples failed the thin layer chromatography and disintegration tests; all of them were unregistered products. Immediate action against counterfeit drugs was taken by the National Malaria Control Program (NMCP) and the DDF. They communicated with the Provincial Health Department about the presence of counterfeit antimalarial drugs through alert letters, a manual, annual malaria conferencing and other training occasions. Television campaigns to alert the population about counterfeit drugs were conducted. Moreover, the NMCP has been promoting the use of good quality antimalarial drugs of a blister co-packaged combination of artesunate and mefloquine in public and private sectors. Appropriate strategies need to be developed and implemented by relevant government agencies and stakeholders to strengthen drug quality assurance and control systems in the country.
PURPOSE: We wished to establish which matrix metalloproteinases (MMPs) and metalloproteinase inhibitors (TIMPs) were present in human interphotoreceptor matrix (IPM) and vitreous. METHODS: IPM and vitreous were obtained from postmortem human eyebank eyes. Western immunoblots were probed with antibodies against human MMPs and TIMPs. Assays specific for elastase activity were also performed. RESULTS: Immunoblot analysis indicated the presence of MMP-1 (interstitial collagenase), MMP-2 and MMP-9 (gelatinases A and B), MMP-3 (stromelysin-1) and TIMP-1, -2 and -3 in both IPM and vitreous. MMP-7 (matrilysin) and MMP-12 (metalloelastase) were not found in either IPM or vitreous. CONCLUSIONS: This is the first demonstration of the MMPs and TIMPs in human IPM and of the TIMPs in human vitreous. While these enzymes are most likely involved in normal turnover within the extracellular matrices that surround the neural retina, they may also play a role in a number of retinal diseases, particularly proliferative diabetic retinopathy and age-related macular degeneration.