Barriers and Channels Formed by Tight Junction Proteins I

Specificaties
Paperback, 252 blz. | Engels
John Wiley & Sons | e druk, 2012
ISBN13: 9781573318730
Rubricering
John Wiley & Sons e druk, 2012 9781573318730
Verwachte levertijd ongeveer 16 werkdagen

Samenvatting

Tight junctions between epithelial and endothelial cells form selective barriers and paracellular channels and regulate paracellular transport of solutes, immune cells, and drugs. More specifically, tight junctions consist of proteins that laterally interconnect neighboring cells of epithelia and endothelia. Certain proteins seal the tight junction, so that a nearly impermeable barrier develops, whereas others form channels that allow for permeation between the cells. Recent investigations have focused on tight junction proteins, belonging to the claudin family (claudins–1 to –27 in humans) and the newly defined group of TAMP (three proteins: occludin, Marvel–D2, and tricellulin).  Barriers and Channels Formed by Tight Junction Proteins I showcases work in this area clustered around three major themes: the molecular properties of tight junctions, for example, the role of the claudin family of proteins and the formation of ion and charge–selective channels; the regulation of tight junction and barrier functions via genetic mechanisms and scaffold protein mediation; and the functional role of the tight junction in various tissues, such as the skin, lungs, endothelia, and nervous system

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Specificaties

ISBN13:9781573318730
Taal:Engels
Bindwijze:paperback
Aantal pagina's:252

Inhoudsopgave

<p>1. Perspectives on tight junction research<br /> J&ouml;rg–Dieter Schulzke, Dorothee G&uuml;nzel, Lena J. John, and Michael Fromm</p>
<p>Molecular properties of the tight junction</p>
<p>20. Charge–selective claudin channel<br /> Susanne M. Krug, Dorothee G&uuml;nzel, Marcel P. Conrad, In–Fah M. Lee, Salah Amasheh, Michael Fromm, and Alan S. L. Yu</p>
<p>29. Claudin–derived peptides are internalized via specific endocytosis pathways<br /> Denise Zwanziger, Christian Staat, Anuska V. Andjelkovic, and Ingolf E. Blasig</p>
<p>38. A phosphorylation hotspot within the occluding C–terminal domain<br /> Max J. D&ouml;rfel and Otmar Huber</p>
<p>45. Determinants contributing to claudin ion channel formation<br /> Anna Veshnyakova, Susanne M. Krug, Sebastian L. Mueller, J&ouml;rg Piontek, Jonas Protze, Michael Fromm, and Gerd Krause</p>
<p>54. Lipolysis–stimulted lipoprotein receptor: a novel membrane protein of tricellular tight junctions<br /> Mikio Furuse, Yukako Oda, Tomohito–Higashi, Noriko Iwamoto, and Sayuri Masuda</p>
<p>59. Overexpression of claudin–5 but not claudin–3 induces formation of trans–interaction–dependent multilamellar bodies<br /> Jan Rossa, Dorothea Lorenz, Martina Ringling, Anna Veshnyakova, and Joerg Piontek</p>
<p>67. Association between segments of zonula occludens proteins: live–cell FRET and mass spectrometric analysis<br /> Christine Rueckert, Victor Castro, Corinna Gagell, Sebastian Dabrowski, Michael Sch&uuml;mann, Eberhard Krause, Ingolf E. Blasig, and Reiner F. Haseloff</p>
<p>77. Dynamic properties of the tight junction barrier<br /> Christopher R. Weber</p>
<p>Regulation of the tight junction and barrier function</p>
<p>85. Regulation of tight junctions in human normal pancreatic duct epithelial cells and cancer cells<br /> Takashi Kojima and Norimasa Sawada</p>
<p>93. The role for protein tyrosine phosphatase nonreceptor type 2 in regulating autophagosome formation<br /> Michael Scharl and Gerhard Rogler</p>
<p>103. Caveolin binds independently to claudin–2 and occluding<br /> Christina M. Van Itallie and James M. Anderson</p>
<p>108. Regulation of epithelial barrier function by the inflammatory bowel disease candidate gene, PTPN2<br /> Declan F. McCole</p>
<p>115. Intracellular mediators of JAM–A–dependent epithelial barrier function<br /> Ana C. Monteiro and Charles A. Parkos</p>
<p>125. Cingulin, paracingulin, and PLEKHA7: signaling and cytoskeletal adaptors at the apical junctional complex<br /> Sandra Citi, Pamela Pulimeno, and Serge Paschoud</p>
<p>133. ZO–2, a tight junction scaffold protein involved in the regulation of cell proliferation and apoptosis<br /> Lorenza Gonzalez–Mariscal, Pablo Bautista, Susana Lechuga, and Miguel Quiros</p>
<p>142. From TER to trans– and paracellular resistance: lessons from impedance spectroscopy<br /> Dorothee G&uuml;nzel, Silke S. Zakrzewski, Thomas Schmid, Maria Pangalos, John Wiedenhoeft, Corinna Blasse, Christopher Ozboda, and Susanne M. Krug</p>
<p>Tight junctions in skin, lung, endothelia, and nervous tissues</p>
<p>152. Diverse type of junctions containing tight junction proteins in stratified mammalian epithelia<br /> Werner W. Franke and Ulrich–Frank Pape</p>
<p>158. Barriers and more: functions of tight junction proteins in the skin<br /> Nina Kirschner and Johanna M. Brandner</p>
<p>167. Roles for claudins in alveolar epithelial barrier function<br /> Christian E. Overgaard, Leslie A. Mitchell, and Michael Koval</p>
<p>175. Claudins and alveolar epithelial barrier function in the lung<br /> &nbsp;James A. Frank</p>
<p>184. Relevance of endothelial junctions in leukocyte extravasation and vascular permeability<br /> Dietmar Vestweber</p>
<p>193. Involvement of claudins in zebrafish brain ventricle morphogenesis<br /> Jingjing Zhang, Martin Liss, Hartwig Wolburg, Ingolf E. Blasig, and Salim Abdelilah–Seyfried</p>
<p>199. Modulation of tight junction proteins in the perineurium for regional pain control<br /> D. Hackel, A. Brack, M. Fromm, and K. L. Rittner</p>

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        Barriers and Channels Formed by Tight Junction Proteins I