Estimating the global costs of vitamin A capsule supplementation: a review of the literature

BACKGROUND: Vitamin A supplementation reduces child mortality. It is estimated that 500 million vitamin A capsules are distributed annually. Policy recommendations have assumed that the supplementation programs offer a proven technology at a relatively low cost of around US$0.10 per capsule. OBJECTIVES: To review data on costs of vitamin A supplementation to analyze the key factors that determine program costs, and to attempt to model these costs as a function of per capita income figures. METHODS: Using data from detailed cost studies in seven countries, this study generated comparable cost categories for analysis, and then used the correlation between national incomes and wage rates to postulate a simple model where costs of vitamin A supplementation are regressed on per capita incomes. RESULTS: Costs vary substantially by country and depend principally on the cost of labor, which is highly correlated with per capita income. Two other factors driving costs are whether the program is implemented in conjunction with other health programs, such as National Immunization Days (which lowers costs), and coverage in rural areas (which increases costs). Labor accounts for 70% of total costs, both for paid staff and for volunteers, while the capsules account for less than 5%. Marketing, training, and administration account for the remaining 25%. CONCLUSIONS: Total costs are lowest (roughly US$0.50 per capsule) in Africa, where wages and incomes are lowest, US$1 in developing countries in Asia, and US$1.50 in Latin America. Overall, this study derives a much higher global estimate of costs of around US$1 per capsule.     

University productivity rankings: A psychologist by any other name.

Refuted W. M. Cox and V. Catt's (see record 1978-21651-001) findings on productivity ratings of graduate psychology programs based on publication in American Psychological journals. Records from the University of Wisconsin—Madison (UW) for authors whose departmental affiliations were not specified in the various journals were examined. Instead of 8.6%, 40% of the articles associated with UW came from nonpsychology departments. (PsycINFO Database Record (c) 2010 APA, all rights reserved)     

Tissue Sampling and Homogenization with NIRL Enables Spatially Resolved Cell Layer Specific Proteomic Analysis of the Murine Intestine

For investigating the molecular physiology and pathophysiology in organs, the most exact data should be obtained; if not, organ-specific cell lines are analyzed, or the whole organ is homogenized, followed by the analysis of its biomolecules. However, if the morphological organization of the organ can be addressed, then, in the best case, the composition of molecules in single cells of the target organ can be analyzed. Laser capture microdissection (LCM) is a technique which enables the selection of specific cells of a tissue for further analysis of their molecules. However, LCM is a time-consuming two-dimensional technique, and optimal results are only obtained if the tissue is fixed, e.g., by formalin. Especially for proteome analysis, formalin fixation reduced the number of identifiable proteins, and this is an additional drawback. Recently, it was demonstrated that sampling of fresh-frozen (non-fixed) tissue with an infrared-laser is giving higher yields with respect to the absolute protein amount and number of identifiable proteins than conventional mechanical homogenization of tissues. In this study, the applicability of the infrared laser tissue sampling for the proteome analysis of different cell layers of murine intestine was investigated, using LC–MS/MS-based differential quantitative bottom-up proteomics. By laser ablation, eight consecutive layers of colon tissue were obtained and analyzed. However, a clear distinguishability of protein profiles between ascending, descending, and transversal colon was made, and we identified the different intestinal-cell-layer proteins, which are cell-specific, as confirmed by data from the Human Protein Atlas. Thus, for the first time, sampling directly from intact fresh-frozen tissue with three-dimensional resolution is giving access to the different proteomes of different cell layers of colon tissue.