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A proton pump is an integral membrane protein pump that builds up a proton gradient across a biological membrane. Proton pumps catalyze the following reaction: :H+[on one side of a biological membrane] + energy H+[on the other side of the membrane] Mechanisms are based on energy-induced conformational changes of the protein structure or on the Q cycle. During evolution, proton pumps have arisen independently on multiple occasions. Thus, not only throughout nature but also within single cells, different proton pumps that are evolutionarily unrelated can be found. Proton pumps are divided into different major classes of pumps that use different sources of energy, have different polypeptide compositions and evolutionary origins. Function Transport of the positively charged proton is typically electrogenic, i.e. it generates an electric field across the membrane also called the membrane potential. Proton transport becomes electrogenic if not neutralized electrically by tr

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Regulation of the V-ATPase along the endocytic pathway occurs through reversible subunit association and membrane localization

Françoise Gisou van der Goot Grunberg

The lumen of endosomal organelles becomes increasingly acidic when going from the cell surface to lysosomes. Luminal pH thereby regulates important processes such as the release of internalized ligands from their receptor or the activation of lysosomal enzymes. The main player in endosomal acidification is the vacuolar ATPase (V-ATPase), a multi-subunit transmembrane complex that pumps protons from the cytoplasm to the lumen of organelles, or to the outside of the cell. The active V-ATPase is composed of two multi-subunit domains, the transmembrane V(0) and the cytoplasmic V(1). Here we found that the ratio of membrane associated V(1)/Vo varies along the endocytic pathway, the relative abundance of V(1) being higher on late endosomes than on early endosomes, providing an explanation for the higher acidity of late endosomes. We also found that all membrane-bound V-ATPase subunits were associated with detergent resistant membranes (DRM) isolated from late endosomes, raising the possibility that association with lipid-raft like domains also plays a role in regulating the activity of the proton pump. In support of this, we found that treatment of cells with U18666A, a drug that leads to the accumulation of cholesterol in late endosomes, affected acidification of late endosome. Altogether our findings indicate that the activity of the vATPase in the endocytic pathway is regulated both by reversible association/dissociation and the interaction with specific lipid environments.

Public Library of Science2008

Magnetization Transfer (MT) Segmentation of foot peripheral nerves at 3 T

Giulio Gambarota, Cristina Granziera

The ability of tracking peripheral nerves in foot could be of great benefit for a number of investigations, which include traumas, diabetes and infections. Previous approaches to nerve tracking have employed diffusion tensor imaging (DTI, [1, 2]), which is a well established method of fiber tracking in the central nervous system. In the peripheral nervous system (PNS), however, one limitation of DTI is the low signal-to-noise ratio (SNR) due to short T2 of water protons in nerve [3-5]. Furthermore, in imaging of foot nerves, the low SNR is exacerbated by the need of the high spatial-resolution required to visualize the nerves. Here, we propose a novel approach to nerve visualization, which exploits the difference in magnetization transfer ratio (MTR) between muscle and foot nerves.

2010

2006

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