Liraglutide Impacts Iron Homeostasis in a Murine Model of Hereditary Hemochromatosis.

Classic hereditary hemochromatosis (HH) is an autosomal recessive iron-overload disorder resulting from loss-of-function mutations of the HFE gene. Patients with HH exhibit excessive hepatic iron accumulation that predisposes these patients to liver disease, including the risk for developing liver cancer. Chronic iron overload also poses a risk for the development of metabolic disorders such as obesity, type 2 diabetes, and insulin resistance.

Peroxisome protein import recapitulated in egg extracts.

Peroxisomes import their luminal proteins from the cytosol. Most substrates contain a C-terminal Ser-Lys-Leu (SKL) sequence that is recognized by the receptor Pex5. Pex5 binds to peroxisomes via a docking complex containing Pex14, and recycles back into the cytosol following its mono-ubiquitination at a conserved Cys residue.

Structures of the double-ring AAA ATPase Pex1-Pex6 involved in peroxisome biogenesis.

The Pex1 and Pex6 proteins are members of the AAA family of ATPases and are involved in peroxisome biogenesis. Recently, cryo-electron microscopy structures of the Pex1-Pex6 complex in different nucleotide states have been determined. This Structural Snapshot describes the structural features of the complex and their implications for its function, as well as questions that still await answers.

Unique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy.

Members of the AAA family of ATPases assemble into hexameric double rings and perform vital functions, yet their molecular mechanisms remain poorly understood. Here, we report structures of the Pex1/Pex6 complex; mutations in these proteins frequently cause peroxisomal diseases. The structures were determined in the presence of different nucleotides by cryo-electron microscopy.

Dual fluorescence and electrochemical detection of the organophosphorus pesticides--ethion, malathion and fenthion.

Organophosphorus (OP) based pesticides are known powerful inhibitors of cholinesterases, thus the toxicity of this class of compounds causes serious environmental and human health concerns. We report that benzodipyrido[3,2-a:2',3'-c]phenazine (BDPPZ) and 3,6-dimethylbenzodipyrido-[3,2-a:2',3'-c]phenazine (DM-BDPPZ) provide independent fluorescent and electrochemical signal transductions in the presence of the organophosphorus (OP) pesticides; fenthion, malathion and ethion. The presence of the methyl groups at the 3 and 6 positions in DM-BDPPZ was found to significantly influence the sensor performance.