Long-term continuous exposure to potentially inappropriate medications (PIMs) can lead to adverse events in the elderly. However, the effects of long-term exposure of the elderly to PIM and the relationship between PIM and chronic diseases remain unclear. The objective of this study was to investigate the continuous use of PIMs in a community-dwelling elderly population. A cross-sectional population-based study was conducted using community pharmacy–filed dispensing records from the Hcare system. Twenty-three community pharmacies were sampled from 2013 to 2015 to obtain records of patients above 65 years-old with continuous prescriptions. PIM were identified according to the 2015 Beers Criteria. The prevalence of patients using PIM was highest in patients with co-morbid mental disorders (40.05%), followed by neurological system disorders (28.91%). Patients who were prescribed a PIM were more than three times as likely to have a mental disorder as those (odds ratio 3.16, 95% confidence interval: 3.06–3.28) with non-chronic diseases. The most prescribed PIM agents were central nervous system drugs (53.16%), and benzodiazepines (35.15%). Patients with mental disorders had the highest rate of long-term persistent PIM exposure, with benzodiazepines being the most frequently dispensed. Drug safety concerns should be closely monitored in elderly patients with the abovementioned conditions.
For patients with moderate to severe asthma, pharmacist intervention can be a cost-effective addition to the management of patients at an outpatient clinic by improving PEFR and patient quality of life, and saving medical resources.
The type 2 transmembrane serine protease matriptase is broadly expressed in human carcinomas and hematological cancers. The proteolytic activity of matriptase is a potential target of drugs and imaging probes. We assessed the fate of active matriptase following the induction of matriptase zymogen activation. Exposing eight human carcinoma cells to pH 6.0 buffer induced robust matriptase zymogen activation followed by rapid inhibition of the nascent active matriptase by hepatocyte growth factor activator inhibitor (HAI)-1. Consequently, no enzymatically active matriptase was detected in these cells. Some active matriptase is, however, rapidly shed to the extracellular milieu by these carcinoma cells. The lack of cell-associated active matriptase and the shedding of active matriptase were also observed in two hematological cancer lines. Matriptase shedding is correlated closely with the induction of matriptase activation, suggesting that matriptase activation and shedding are kinetically coupled. The coupling allows a proportion of active matriptase to survive HAI-1 inhibition by rapid shedding from cell surface. Our study suggests that cellular free, active matriptase is scarce and might not be an effective target for in vivo imaging and drug development.
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