Long-term risk of adverse cardiovascular outcomes associated with cutaneous lupus erythematosus: a nationwide cohort study

Clinical Rheumatology - Autoimmune diseases, including systemic lupus erythematosus, have been associated with a substantial risk of cardiovascular morbidity and mortality. However, data on the...     

Coated silver nanoparticles: synthesis,cytotoxicity, and optical properties

Coated silver nanoparticles (AgNPs) have recently become a topic of interest due to the fact that they have several applications such as in electronic, antimicrobial, industrial, optical, and medical fields as biosensors and drug delivery systems. However, the use of AgNPs in medical fields remains somewhat limited due to their probable cytotoxic effect. Researchers have succeeded in reducing the toxicity of silver particles by coating them with different substances. Generally, the coating of AgNPs leads to change in their properties depending on the type of the coating material as well as the layer thickness. This review covers the state-of-the-art technologies behind (a) the synthesis of coated AgNPs including coating methods and coating materials, (b) the cytotoxicity of coated AgNPs and (c) the optical properties of coated AgNPs.

Coated silver nanoparticles (AgNPs) have recently become a topic of interest due to the fact that they have several applications such as in electronic, antimicrobial, industrial, optical, and medical fields as biosensors and drug delivery systems.     

The Trypanosoma brucei sphingolipid synthase, an essential enzyme and drug target

Sphingolipids are important components of eukaryotic membranes, particularly the plasma membrane, and are involved in a diverse array of signal transduction processes. In the Eukaryota the biosynthetic pathway for the formation of these lipid species is largely conserved. However, in contrast to mammals which produce sphingomyelin (SM), several pathogenic fungi and protozoa synthesize inositol phosphorylceramide (IPC) as the primary phosphosphingolipid. This process is catalyzed by the enzyme IPC synthase, a recognized target for anti-fungals encoded by the AUR1 gene in yeast. Recently, functional orthologues of the AUR1p have been identified in a group of insect vector-borne pathogenic protozoa, the Kinetoplastida, which are responsible for a range of so-called neglected diseases. Of these the Trypanosoma brucei species are the causative agents of human African trypanosomiasis in many of the most under-developed regions of Africa. The available treatments for these diseases are limited, of decreasing efficacy, and often demonstrate severe side-effects. Against this background the T. brucei sphingolipid synthase, an orthologue of the yeast AUR1p, may represent a promising target for novel anti-protozoals. Our studies identify an isoform of this protein as a novel bi-functional enzyme capable of catalyzing the synthesis of both IPC and SM, both known to be present in the parasite. Furthermore, the synthase is essential for parasite growth and can be inhibited by a known anti-fungal at low nanomolar levels in vitro. Most notably this drug demonstrates trypanocidal activity against cultured bloodstream form parasites. Thus, the T. brucei sphingolipid synthase represents a valid and promising drug target.     

Genes for glycosylphosphatidylinositol toxin biosynthesis in Plasmodium falciparum

About 2.5 million people die of Plasmodium falciparum malaria every year. Fatalities are associated with systemic and organ-specific inflammation initiated by a parasite toxin. Recent studies show that glycosylphosphatidylinositol (GPI) functions as the dominant parasite toxin in the context of infection. GPIs also serve as membrane anchors for several of the most important surface antigens of parasite invasive stages. GPI anchoring is a complex posttranslational modification produced through the coordinated action of a multicomponent biosynthetic pathway. Here we present eight new genes of P. falciparum selected for encoding homologs of proteins essential for GPI synthesis: PIG-A, PIG-B, PIG-M, PIG-O, GPI1, GPI8, GAA-1, and DPM1. We describe the experimentally verified mRNA and predicted amino acid sequences and in situ localization of the gene products to the parasite endoplasmic reticulum. Moreover, we show preliminary evidence for the PIG-L and PIG-C genes. The biosynthetic pathway of the malaria parasite GPI offers potential targets for drug development and may be useful for studying parasite cell biology and the molecular basis for the pathophysiology of parasitic diseases.     

High-level expression of the Toxoplasma gondii STT3 gene is required for suppression of the yeast STT3 gene mutation

N-linked glycosylation is the most frequent modification of secretory proteins. The central reaction of this process in eukaryotic cells is catalyzed by the hetero-oligomeric protein complex oligosaccharyltransferase (OST). The gene STT3 gene encodes a protein, which is the most conserved among the components of the OST. In this report, we describe the isolation and functional characterization of a STT3 homologue from Toxoplasma gondii. The topology of the TgStt3p is similar to that of the yeast Stt3p with 47% identity. We demonstrate that high level expression of the homologues gene is required to completely suppress the defect caused by a stt3 mutation in yeast, suggesting that homologous Stt3 proteins can serve analogous functions in distantly related eukaryotic cells regardless of their degree of conservation.     

Advances in nanotechnology and antibacterial properties of biodegradable food packaging materials

A large number of non-biodegradable and non-renewable materials are produced daily for application as food packaging materials. These waste materials have a greatly negative effect on our health and the ecosystem. The idea of a bio-based economy is steadily gaining attention from the scientific, societal, and financial communities, so there are several areas in which the intended approaches can be improved for this reason. Therefore, creating biopolymer-based materials from natural sources, including polysaccharides and proteins, is a good alternative to non-renewable fossil resources. In the current review paper, we plan to summarize the major recent findings in food biodegradable packaging materials that include nanotechnology either directly or indirectly. Several natural nano-materials applied in food packaging applications such as polymers, polysaccharides, and protein-based nano-materials have been included in order to make special biopolymer hosts for nanocomposites. Finally, this review will highlight the antibacterial properties of commonly used nanoparticles or nanomaterials.

Herein, we aim to summarize the major recent findings in food biodegradable packaging materials that include nanotechnology either directly or indirectly.     

The GPI1 homologue from Plasmodium falciparum complements a Saccharomyces cerevisiae GPI1 anchoring mutant

Glycosylphosphatidylinositol (GPI) represents an important anchoring molecule for cell surface proteins. The first step in its synthesis is the transfer of N-acetylglucosamine (GlcNAc) from UDP-N-acetylglucosamine to phosphatidylinositol (PI). This chemically simple step is genetically complex because three or four genes are required in both yeast (GPI1, GPI2 and GPI3) and mammals (GPI1, PIG A, PIG H and PIG C), respectively. Here, we report cloning of a Plasmodium falciparum (P. falciparum) homologue of GPI1 (PfGPI1). Analysis showed that P. falciparum Gpi1p is somewhat more similar to the yeast proteins than human Gpi1p, showing 26 and 20% amino acid sequence identity with the Saccharomyces cerevisiae and Homo sapiens proteins, respectively. Multiple sequence alignment demonstrates also that the C-terminal half GPI1 proteins is much better conserved than the N-terminal half. The P. falciparum Gpi1p has a calculated molecular weight of 65 kDa and a predicted potential tyrosine phosphorylation site. The potential tyrosine phosphorylation site seems to occur in all other known Gpi1 proteins. Like the other GPI1 proteins, the predictive software revealed the absence of targeting signals such as organelle transit peptides, DNA binding sites, or N-terminal secretory signals. Hydrophobicity plots revealed multiple hydrophobic regions that could function as transmembrane segments. The cloned P. falciparum GPI1 gene complemented a gpi1 yeast mutant.