Learn More
A tight junction-enriched membrane fraction has been used as immunogen to generate a monoclonal antiserum specific for this intercellular junction. Hybridomas were screened for their ability to both react on an immunoblot and localize to the junctional complex region on frozen sections of unfixed mouse liver. A stable hybridoma line has been isolated that(More)
ZO-1, originally identified by mAb techniques, is the first protein shown to be specifically associated with the tight junction. Here we describe and compare the physical characteristics of ZO-1 from mouse liver and the Madin-Darby canine kidney (MDCK) epithelial cell line. The ZO-1 polypeptide has an apparent size of 225 kD in mouse tissues and 210 kD in(More)
The relationship of tight junction permeability to junction structure and composition was examined using two strains of Madin-Darby canine kidney (MDCK) cells (I and II) which differ greater than 30-fold in transepithelial resistance. This parameter is largely determined by paracellular, and hence junctional, permeability under most conditions. When these(More)
We previously identified and characterized ZO-1 as a peripheral membrane protein specifically associated with the cytoplasmic surface of tight junctions. Here we describe the identification of partial cDNA sequences encoding rat and human ZO-1 and their use to study the assembly of tight junctions in the Caco-2 human intestinal epithelial cell line. A rat(More)
The relative localization of ZO-1 and cingulin, the only two known components of the tight junction, was compared in Madin-Darby canine kidney (MDCK) cells, chicken small intestine, rat kidney distal convoluted tubule, and a hepatoma cell line. Immunoblot analysis demonstrated that cingulin and ZO-1 are immunologically unrelated and that, in the colon,(More)
A bile canaliculus-derived preparation containing junctional complexes has been obtained from mouse livers using subcellular fractionation techniques. The junctional complexes include structurally intact zonulae occludentes (ZOs). Extraction of this preparation with the anionic detergent sodium deoxycholate (DOC) left junctional ribbons, the(More)
The complete cDNA sequence for canine ZO-2, a tight junction-specific protein, is presented. A single open reading frame encodes a polypeptide of 1,174 amino acids with a predicted molecular mass of 132,085 daltons. As noted previously (), ZO-2 is a member of the membrane-associated guanylate kinase-containing (MAGUK) protein family, a family which includes(More)
The tight junction, or zonula occludens (ZO), forms a semi-permeable barrier in the paracellular pathway in most vertebrate epithelia. The ZO is the apical-most member of a series of intercellular junctions, collectively known as the junctional complex, found at the interface of the apical and lateral cell surface. This structure not only restricts movement(More)
The design of targeted oral liposomes is anticipated to improve the systemic delivery of poorly absorbed agents, such as proteins and peptides. A poly(ethylene oxide) (PEO)-folic acid (FA) derivative was prepared and evaluated for improving liposome transport across a model gastrointestinal cell line (Caco-2). FA-PEO-cholesterol (Chol) derivatives were(More)
A comparison was made of the phosphate content of the tight-junction-specific protein ZO-1 in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance, a parameter reflective of tight-junctional permeability. Analysis revealed that the ZO-1 from the low-resistance strain contained approximately twice as much phosphate as(More)