Membrane lipid defects are responsible for the generation of reactive oxygen species in peripheral blood mononuclear cells from vitiligo patients.

The pathogenesis of vitiligo, an acquired depigmenting disease of the skin, involves oxidative stress. Based on that, the generation of reactive oxygen species (ROS) by the mitochondria may be relevant in the pathogenesis of vitiligo. Here, we evaluate the biochemical and functional alterations involved in the defective activity that has been previously described both in melanocytes and peripheral blood mononuclear cells (PBMC) from vitiligo patients.

Membrane lipid alterations as a possible basis for melanocyte degeneration in vitiligo.

The occurrence of oxidative stress has been proposed as a pathogenetic mechanism for melanocyte degeneration in vitiligo. In order to evaluate this possible correlation we focused on the lipid component of cell membranes. We observed in vitiligo melanocytes, through FACS methods, an increased median fluorescence intensity of rhodamine 123 and C11-BODIPY581/591 indicating a spontaneous higher production of reactive oxygen species (ROS) and membrane lipoperoxidation, associated with an altered pattern of cardiolipin (CL) distribution, defined on the basis of the fluorescence pattern after staining with 10-nonyl acridine orange.

Set regulation in asexual and sexual Plasmodium parasites reveals a novel mechanism of stage-specific expression.

Transmission of the malaria parasite depends on specialized gamete precursors (gametocytes) that develop in the bloodstream of a vertebrate host. Gametocyte/gamete differentiation requires controlled patterns of gene expression and regulation not only of stage and gender-specific genes but also of genes associated with DNA replication and mitosis. Once taken up by mosquito, male gametocytes undergo three mitotic cycles within few minutes to produce eight motile gametes.

A gene-family encoding small exported proteins is conserved across Plasmodium genus.

A gene-family, named sep, encoding small exported proteins conserved across Plasmodium species has been identified. SEP proteins (13-16 kDa) contain a predicted signal peptide at the NH(2)-terminus, an internal hydrophobic region and a polymorphic, low-complexity region at the carboxy-terminus. One member of the Plasmodium berghei family, Pbsep1, encodes an integral membrane protein expressed along the entire erythrocytic cycle.