Research and Markets: Barriers and Channels Formed by Tight Junction Proteins I - Annals of the New York Academy of Sciences

DUBLIN--()--Research and Markets (http://www.researchandmarkets.com/research/swmt9p/barriers_and_chann) has announced the addition of John Wiley and Sons Ltd's new book "Barriers and Channels Formed by Tight Junction Proteins I. Annals of the New York Academy of Sciences" to their offering.

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

Key Topics Covered:

Perspectives on tight junction research

Charge-selective claudin channels

Claudin-derived peptides are internalized via specific endocytosis pathways

A phosphorylation hotspot within the occludin C-terminal domain

Determinants contributing to claudin ion channel formation

Lipolysis-stimulated lipoprotein receptor: a novel membrane protein of tricellular tight junctions

Overexpression of claudin-5 but not claudin-3 induces formation of trans-interaction-dependent multilamellar bodies

Association between segments of zonula occludens proteins: live-cell FRET and mass spectrometric analysis

Dynamic properties of the tight junction barrier

Regulation of tight junctions in human normal pancreatic duct epithelial cells and cancer cells

The role for protein tyrosine phosphatase nonreceptor type 2 in regulating autophagosome formation

Caveolin binds independently to claudin-2 and occludin

Regulation of epithelial barrier function by the inflammatory bowel disease candidate gene, PTPN2

Intracellular mediators of JAM-A-dependent epithelial barrier function

Cingulin, paracingulin, and PLEKHA7: signaling and cytoskeletal adaptors at the apical junctional complex

ZO-2, a tight junction scaffold protein involved in the regulation of cell proliferation and apoptosis

From TER to trans- and paracellular resistance: lessons from impedance spectroscopy

Diverse types of junctions containing tight junction proteins in stratified mammalian epithelia

Barriers and more: functions of tight junction proteins in the skin

Roles for claudins in alveolar epithelial barrier function

Claudins and alveolar epithelial barrier function in the lung

Relevance of endothelial junctions in leukocyte extravasation and vascular permeability

Involvement of claudins in zebrafish brain ventricle morphogenesis

Modulation of tight junction proteins in the perineurium for regional pain control

Author:

Edited by Michael Fromm (Charité, Campus Benjamin Franklin, Berlin, Germany) and Jörg-Dieter Schulzke Charité, Campus Benjamin Franklin, Berlin, Germany)

For more information visit http://www.researchandmarkets.com/research/swmt9p/barriers_and_chann

Source: John Wiley and Sons Ltd

Contacts

Research and Markets
Laura Wood, Senior Manager.
press@researchandmarkets.com
U.S. Fax: 646-607-1907
Fax (outside U.S.): +353-1-481-1716
Sector: Proteomics

Contacts

Research and Markets
Laura Wood, Senior Manager.
press@researchandmarkets.com
U.S. Fax: 646-607-1907
Fax (outside U.S.): +353-1-481-1716
Sector: Proteomics