Mutual health insurance in Rwanda: evidence on access to care and financial risk protection.

OBJECTIVE: Rwanda has expanded mutual health insurance considerably in recent years, which has a great potential for making health services more accessible. In this paper, we examine the effect of mutual health insurance (MHI) on utilization of health services and financial risk protection. METHODS: We used data from a nationally representative survey from 2005-2006. We analysed this data through summary statistics as well as regression models. FINDINGS: Our statistical modelling shows that MHI coverage is associated with significantly increased utilization of health services. Indeed, individuals in households that had MHI coverage used health services twice as much when they were ill as those in households that had no insurance coverage. Additionally, MHI is also associated with a higher degree of financial risk protection and the incidence of catastrophic health expenditure was almost four times less than in households with no coverage. Nonetheless, the limitations of the MHI coverage also become apparent. CONCLUSION: These promising results indicate that MHI has had a strong positive impact on access to health care and can continue to improve health of Rwandans even more if its limitations are addressed further.

Molecular characterization of a specific thiamine triphosphatase widely expressed in mammalian tissues.

Thiamine triphosphate (ThTP) is found at low concentrations in most animal tissues, and recent data suggest that it may act as a phosphate donor for the phosphorylation of some proteins. In the mammalian brain, ThTP synthesis is rapid, but its steady-state concentration remains low, presumably because of rapid hydrolysis. In this report we purified a soluble thiamine triphosphatase (ThTPase; EC ) from calf brain. The bovine ThTPase is a 24-kDa monomer, hydrolyzing ThTP with virtually absolute specificity. Partial sequence data obtained from the purified bovine enzyme by tandem mass spectrometry were used to search the GenBank data base. A significant identity was found with only one human sequence, the hypothetical 230-amino acid protein MGC2652. The coding regions from human and bovine brain mRNA were amplified by reverse transcription-PCR, cloned in Escherichia coli, and sequenced. The human open reading frame was expressed in E. coli as a GST fusion protein. Transformed bacteria had a high isopropyl-beta-d-thiogalactopyranoside-inducible ThTPase activity. The recombinant ThTPase had properties similar to those of human brain ThTPase, and it was specific for ThTP. The mRNA was expressed in most human tissues but at relatively low levels. This is the first report of a molecular characterization of a specific ThTPase.