Document Detail

Barriers built on claudins.
MedLine Citation:
PMID:  15159449     Owner:  NLM     Status:  MEDLINE    
The fundamental functions of epithelia and endothelia in multicellular organisms are to separate compositionally distinct compartments and regulate the exchange of small solutes and other substances between them. Tight junctions (TJs) between adjacent cells constitute the barrier to the passage of ions and molecules through the paracellular pathway and function as a 'fence' within the plasma membrane to create and maintain apical and basolateral membrane domains. How TJs achieve this is only beginning to be understood. Recently identified components of TJs include the claudins, a family of four-transmembrane-span proteins that are prime candidates for molecules that function in TJ permeability. Their identification and characterization have provided new insight into the diversity of different TJs and heterogeneity of barrier functions in different epithelia and endothelia.
Kursad Turksen; Tammy-Claire Troy
Related Documents :
16945359 - Membranes are not just rafts.
17661499 - Remodeling of ordered membrane domains by gpi-anchored intestinal alkaline phosphatase.
7957179 - Characterization, quantification and subcellular localization of inositol-containing sp...
20013029 - Use of lipid rafting for the analysis of human basophil activation by flow cytometry.
11720999 - Flexibility of the cytoplasmic domain of the anion exchange protein, band 3, in human e...
9971769 - Human immunodeficiency virus type 1 protease triggers a myristoyl switch that modulates...
6654909 - A chemical procedure for determining the sidedness of the nh2 terminus in a membrane pr...
15662509 - Measuring the solubilities of ionic liquids in water using ion-selective electrodes.
19446029 - An rrna-based analysis for evaluating the effect of heat stress on the rumen microbial ...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Journal of cell science     Volume:  117     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2004 May 
Date Detail:
Created Date:  2004-05-25     Completed Date:  2004-12-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  2435-47     Citation Subset:  IM    
Ottawa Health Research Institute, Ontario K1Y 4E9, Canada.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Motifs
Amino Acid Sequence
Biological Transport
Cell Membrane / chemistry*
Cell Membrane Permeability
Cell Polarity
Conserved Sequence
Evolution, Molecular
Gene Expression
Membrane Proteins / chemistry*,  genetics,  metabolism*
Models, Biological
Molecular Sequence Data
Molecular Weight
Protein Structure, Tertiary
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Tight Junctions*
Tissue Distribution
Reg. No./Substance:
0/Membrane Proteins
Erratum In:
J Cell Sci. 2004 Aug 15;117(Pt 18):4341

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Serofendic acid, a sulfur-containing diterpenoid derived from fetal calf serum, attenuates reactive ...
Next Document:  Mechanosensitive ion channels: molecules of mechanotransduction.