Freedom in Exile: Rastafarian Responses to Cultural Disassociation

From the outset the Rastafarian movement, which originated in the 1930s in Jamaica, was concerned with the central question of place. In its advocacy of Africa as the true home of all peoples of African descent and especially for the ex-slave population of the Americas, it tapped into a powerful Jamaican tradition of redemption and repatriation, of liberation from the of "mental slavery" which had bound blacks since the advent of colonial interests in the Americas. It also provided a means by which the culturally disassociated could rediscover an identity and sense of worth, taken from them by the process of enslavement. Since the origins of the Rastafarian movement, however, the conception of both Africa, usually referred to as Ethiopia, and Jamaica has undergone considerable modification, reflecting not only the changing social and economic situation of the Rastas in Jamaica, but the spread of the movement beyond its land of origin, into the Jamaican diaspora in Europe and America, where it has attracted not only Jamaicans and their descendants, but others of African descent (African-Americans, for example)

Characterization of the Plasmodium falciparum M17 leucyl aminopeptidase. A protease involved in amino acid regulation with potential for antimalarial drug development

Amino acids generated from the catabolism of hemoglobin by intra-erythrocytic malaria parasites are not only essential for protein synthesis but also function in maintaining an osmotically stable environment, and creating a gradient by which amino acids that are rare or not present in hemoglobin are drawn into the parasite from host serum. We have proposed that a Plasmodium falciparum M17 leucyl aminopeptidase (PfLAP) generates and regulates the internal pool of free amino acids and therefore represents a target for novel antimalarial drugs. This enzyme has been expressed in insect cells as a functional 320-kDa homo-hexamer that is optimally active at neutral or alkaline pH, is dependent on metal ions for activity, and exhibits a substrate preference for N-terminally exposed hydrophobic amino acids, particularly leucine. PfLAP is produced by all stages in the intra-erythrocytic developmental cycle of malaria but was most highly expressed by trophozoites, a stage at which hemoglobin degradation and parasite protein synthesis are elevated. The enzyme was located by immunohistochemical methods and by transfecting malaria cells with a PfLAP-green fluorescent protein construct, to the cytosolic compartment of the cell at all developmental stages, including segregated merozoites. Amino acid dipeptide analogs, such as bestatin and its derivatives, are potent inhibitors of the protease and also block the growth of P. falciparum malaria parasites in culture. This study provides a biochemical basis for the antimalarial activity of aminopeptidase inhibitors. Availability of functionally active recombinant PfLAP, coupled with a simple enzymatic readout, will aid medicinal chemistry and/or high throughput approaches for the future design/discovery of new antimalarial drugs