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Keybot 11 Résultats  www.bio-pro.de  Page 7
  Biotechnologie / Life S...  
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Weitere Forschungen ergaben: Irre C hat eine Schwester, das Protein Kirre. Beide sitzen in der Membran von Axonendigungen, ragen in den extrazellulären Raum hinein und können definierte Proteine auf der Oberfläche von anderen Zellen binden.
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More than ten years ago, Fischbach and his team discovered the gene irregular Chiasm C (irreC) in one of the fly mutants. irreC is necessary for the correct projection of visual fibres in the optic chiasm. Defective irreC genes lead to malformations in the optic area in the fly brain, which are referred to as outer and inner optic chiasms. The axons, originating from the eye, take in this case a long detour before eventually finding their final destination in deeper brain areas. Further research has shown that the protein Irre C has a sister, the protein Kirre. These two proteins are located in the membrane of axon endings and extend into the extracellular space where they bind to defined proteins on the surface of other cells. "That is how the growing axons recognise their target cells," explained Fischbach. The researchers also found protein partners on the membranes of the target cells, which are bound by IrreC and Kirre. The entire functional unit was subsequently named "irre cell recognition module" (IRM). All these molecules are members of the immunoglobulin family, and are similar to the antibodies of the immune system that are found in humans. And this is a long way from being the only similarity between flies and humans.
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Insgesamt drei Gruppen von Molekülen sorgen für die Polarität – egal ob im Darm, in der Lunge oder in einem anderen Organ. Da gibt es erstens die sogenannten Adhäsionsmoleküle, die durch die Membran ragen und die Nachbarzellen miteinander verschweißen.
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There are three groups of molecules that control the polarity of cells; these groups are found in the intestines, the lungs and all other organs. The first group consists of adhesion molecules that protrude the membrane and tightly fuse neighbouring cells with each other. These molecules anchor the cells in the tissue and enable cell-cell contacts. The second group, which are signalling molecules, are found inside the cells. These signalling molecules translate information from the tissue into a cell response. These molecules trigger cells to form structures at their “head” that are different from those at their “foot”. The two groups are linked by scaffold proteins that also establish links with the cytoskeleton. The cytoskeleton determines the morphology of the cells and also enables targeted cell movements in the tissue, something that is important for patrolling immune cells. Loosli and his team have taken on the task of gaining deeper insights into the network that consists of different molecular players. “Cell polarity is already of great importance in the early development of an organism,” said the biologist. “Cell polarity defects lead to the malformation of organs.”
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Es handelt sich dabei um die Moleküle der Neph-Nephrin Proteinfamilie, die von den Podozyten gebildet werden und in deren Zellmembran verankert sind. Sie ragen in den extrazellulären Raum hinaus und verbinden sich mit ähnlichen Proteinen aus benachbarten Podozyten.
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“What is the role of the slit diaphragm and the podocytes in terms of filtration?” asks Huber. “Are they purely mechanical filters?” Huber’s team have been studying the central proteins that form the slit diaphragm for a number of years. These proteins are molecules of the Neph-Nephrin protein family produced by the podocytes that are anchored in the cell membrane of the podocytes. The Neph-Nephrin proteins extend into the extracellular space and bind similar proteins originating from neighbouring podocytes, thus forming the protein layer which the scientists refer to as slit diaphragm. The slit diaphragm is an extremely vital zone. The experiments carried out by Huber’s team have shown that the proteins that form the slit diaphragm detect a broad range of environmental stimuli and transfer this information into the podocytes. In a collaborative project with Marty Chalfie, who received the Nobel Prize in Chemistry in 2008, Huber’s team was able to show that the slit diaphragm is a mechanical sensor, which constantly measures the filtration rate and reports back to the interior of the podocytes.
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Die fettlöslichen Bereiche können sich an Schmutzpartikel oder andere fettige Substanzen anlagern und um sie eine Schicht bilden. Die wasserlöslichen Bereiche ragen dann nach außen und sind in einem wässrigen Medium lösbar.
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Surfactants are molecules with a water-soluble and a fat-soluble domain. The fat-soluble domains can attach to dirt particles or other fatty substances and form a layer around them. The water-soluble domains extend to the outside and dissolve in aqueous solutions. This is how surfactants help remove dirt from clothes or food residue from plates. Surfactants are the major constituents of washing agents, soap or household detergents. "Industry requires a large amount of these substances," said Dr. Rudolf Hausmann from the Department of Technical Biology led by Prof. Christoph Syldatk at the Institute of Bio- and Food Technology at the Karlsruhe Institute of Technology (KIT). "At present, the majority of surfactants is produced from mineral oil, but the need for biologically degradable surfactants made from renewable materials has been growing over the last few years.
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Man sieht es zum Beispiel in der einschichtigen Wand des Lungenepithels: Zellen haben eine obere (apikale) Seite, an der Haarstrukturen ins Lungenlumen ragen, und eine untere (basale) Seite, an der solche Härchen fehlen.
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The single-layer wall of the lung epithelium shows that cells have a top (apical) side where hairy structures reach into the lung lumen, and a bottom (basal) side that lacks such hairy structures. The majority of epithelia have this kind of apico-basal asymmetry, including the renal channels (tubuli) in which each cell has a sensory cilium that projects into the lumen. These tubuli are rather like sensors that control the composition of urine. Using this model system, Prof. Dr. Matias Simons from the Center for Biological Systems Analysis (ZBSA) at the University of Freiburg discovered another type of cellular asymmetry around 10 years ago. What he discovered was planar cell polarity (PCP) pathways that polarize cells in the tissue plane and equip cells with a defined orientation (left/right axis). Between 2002 and 2005, Simons investigated the causes of polycystic kidney diseases in which the epithelial cells of renal tubuli are unable to divide on their correct axis, which results in the formation of epithelial cysts. It was known that such defects were associated with defective PCP signalling involved in early embryonic development. In cooperation with colleagues in Prof. Dr. Gert Walz’ laboratory at the Freiburg University Medical Centre, Simons found that mutated Inversin genes led to the development of polycystic kidneys. “We also found that the Inversin gene was a determinant of planar cell polarity,” said Simons.
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Rund dreißig Prozent aller Proteine in einer Zelle stehen mit einer Biomembran in Verbindung – einige durchqueren die Lipiddoppelschicht, manchmal sogar mehrfach, andere sind an Membranen gebunden und ragen in den extra- oder intrazellulären Raum hinein.
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Around thirty per cent of all cellular proteins are in some way or other associated with a biomembrane – some proteins cross the lipid bilayer once and some even several times while others are bound to membranes and protrude into the extra- or intracellular space. The pharmaceutical industry has long known that cellular membranes are important drug targets. Aspirin acts on a specific membrane-associated protein, thereby preventing the transmission of pain signals, to cite just one example. Researchers are currently particularly interested in the structure-function relationship of membrane proteins and membrane-active peptides. Their targets include ion channels, signal receptors, peptide antibiotics as well as cell penetrating peptides that are used to shuttle drugs across the cell membrane. “In all these cases, we are not only interested in the three-dimensional structure of these molecules; we are also interested in how these molecules interact with each other,” said Prof. Dr. Anne S. Ulrich from the Institute of Biological Interfaces 2 (IBG-2) at the Karlsruhe Institute of Technology (KIT). “We are looking at the molecules when they bind to membranes; we specifically manipulate the molecular contact areas and try to deduce their mechanisms of action from this information.”
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Es sind die Membranproteine aus der Familie der Cadherine, die wie ein Klettverschluss die Nachbarzellen in der Epithelschicht zusammenhalten. Sie sitzen in der Membran und ragen in den extrazellulären Raum hinaus, wo sie nach dem Schlüssel-Schloss-Prinzip mit den Cadherinen der Gegenseite einrasten.
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The epithelium is a layer of cells that are bound so tightly to each other that nothing is able to pass through them. This is important in the intestines, for example, where substances that may pass through the intestinal wall into the blood need to be differentiated from those that must not. Membrane proteins of the cadherin family bind neighbouring cells of the epithelial layer together in a zip-like fashion. They are anchored in the cell membrane and extend into the extracellular space where they fit into the cadherins located in the membrane of neighbouring cells in the same way as a key fits into a lock. The adhesion of cells is crucial during embryonic development. Cells located in what is referred to as the cranial neural crest must remain together. Other cells, however, need to detach at the right point in time and migrate, for example in order to form what later become the eyes. “Researchers have long thought that cadherins have only one role, namely to promote the adhesion between cells,” said Dr. Almut Köhler from the Department of Cell and Developmental Biology at the Institute of Zoology of the Karlsruhe Institute of Technology (KIT).
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Man sieht es zum Beispiel in der einschichtigen Wand des Lungenepithels: Zellen haben eine obere (apikale) Seite, an der Haarstrukturen ins Lungenlumen ragen, und eine untere (basale) Seite, an der solche Härchen fehlen.
Comparer pages textesComparer pages HTMMontrer URL avec texte sourceMontrer URL avec langue cibleDéfinir bio-pro.de comme domaine prioritaire
The single-layer wall of the lung epithelium shows that cells have a top (apical) side where hairy structures reach into the lung lumen, and a bottom (basal) side that lacks such hairy structures. The majority of epithelia have this kind of apico-basal asymmetry, including the renal channels (tubuli) in which each cell has a sensory cilium that projects into the lumen. These tubuli are rather like sensors that control the composition of urine. Using this model system, Prof. Dr. Matias Simons from the Center for Biological Systems Analysis (ZBSA) at the University of Freiburg discovered another type of cellular asymmetry around 10 years ago. What he discovered was planar cell polarity (PCP) pathways that polarize cells in the tissue plane and equip cells with a defined orientation (left/right axis). Between 2002 and 2005, Simons investigated the causes of polycystic kidney diseases in which the epithelial cells of renal tubuli are unable to divide on their correct axis, which results in the formation of epithelial cysts. It was known that such defects were associated with defective PCP signalling involved in early embryonic development. In cooperation with colleagues in Prof. Dr. Gert Walz’ laboratory at the Freiburg University Medical Centre, Simons found that mutated Inversin genes led to the development of polycystic kidneys. “We also found that the Inversin gene was a determinant of planar cell polarity,” said Simons.