MiR-101 and miR-144 Regulate the Expression of the CFTR Chloride Channel in the Lung

The Cystic Fibrosis Transmembrane conductance Regulator (CFTR) is a chloride channel that plays a critical role in the lung by maintaining fluid homeostasis. Absence or malfunction of CFTR leads to Cystic Fibrosis, a disease characterized by chronic infection and inflammation. We recently reported that air pollutants such as cigarette smoke and cadmium negatively regulate the expression of CFTR by affecting several steps in the biogenesis of CFTR protein. MicroRNAs (miRNAs) have recently received a great deal of attention as both biomarkers and therapeutics due to their ability to regulate multiple genes. Here, we show that cigarette smoke and cadmium up-regulate the expression of two miRNAs (miR-101 and miR-144) that are predicted to target CFTR in human bronchial epithelial cells. When premature miR-101 and miR-144 were transfected in human airway epithelial cells, they directly targeted the CFTR 3′UTR and suppressed the expression of the CFTR protein. Since miR-101 was highly up-regulated by cigarette smoke in vitro, we investigated whether such increase also occurred in vivo. Mice exposed to cigarette smoke for 4 weeks demonstrated an up-regulation of miR-101 and suppression of CFTR protein in their lungs. Finally, we show that miR-101 is highly expressed in lung samples from patients with severe chronic obstructive pulmonary disease (COPD) when compared to control patients. Taken together, these results suggest that chronic cigarette smoking up-regulates miR-101 and that this miRNA could contribute to suppression of CFTR in the lungs of COPD patients.     

Reversal of digestive interactions between Pacific reef corals: Mediation by sweeper tentacles

Summary Aggressive interactions among reef corals involving direct interference through extracoelenteric digestion has previously been considered as a potential mechanism for the maintenance of high species diversity. In this report I show that induced development of sweeper tentacles can reverse initial digestive interactions. In the eastern Pacific these reversals contribute to resource monopolization by fast growing pocilloporid corals. This suggests that other mechanisms must account for the maintenance of local species diversity.     

Étude électrophorétique de l'hybride expérimental entre Papio anubis et P. cynocephalus

Hybrids between Papio anubis and P. cynocephalus occur in nature. We have studied laboratory bred hybrids, together with their backcrossed offspring. Electrophoretic experiments on the proteins, serum enzymes and erythrocytes obtained from both hybrids and parents lead to three conclusions. First, both parents and hybrids possess proteins having identical mobilities; this case is the most frequent in the 23 loci studied. Second, individual polymorphism caused by, for example, carbonic anhydrase I or transferrin in one or both parents results in the appearance of a codominant phenotype in the hybrid, when the parental components are distinguishable. Third, when other enzymes such as albumin, alkaline phosphatase, haemoglobin and the serum esterases have particular electrophoretic mobilities in the parents, then the hybrid is again codominant; a particularly interesting case among the esterases is that of pseudocholinesterase, where the paternal component is partially repressed in the hybrid. The hybrid than exhibits the phenomenon of allelic repression of at least one gene, which confirms the taxonomic position of species of the two forms of Papio studied.     

The p24 family and selective transport processes at the ER—Golgi interface

The secretory pathway is of vital importance for eukaryotic cells and has a pivotal role in the synthesis, sorting, processing and secretion of a large variety of bioactive molecules involved in intercellular communication. One of the key processes in the secretory pathway concerns the transport of cargo proteins from the ER (endoplasmic reticulum) to the Golgi. Type‐I transmembrane proteins of ～24 kDa are abundantly present in the membranes of the early secretory pathway, and bind the COPI and COPII coat complexes that cover vesicles travelling between the membranes. These p24 proteins are thought to play an important role in the selective transport processes at the ER—Golgi interface, although their exact functioning is still obscure. One model proposes that p24 proteins couple cargo selection in the lumen with vesicle coat recruitment in the cytosol. Alternatively, p24 proteins may furnish subcompartments of the secretory pathway with the correct subsets of machinery proteins. Here we review the current knowledge of the p24 proteins and the various roles proposed for the p24 family members.