High impact information on Cldn2

• In glutaraldehyde-fixed samples, claudin-1-induced strands were largely associated with the protoplasmic (P) face as mostly continuous structures, whereas claudin-2-induced strands were discontinuous at the P face with complementary grooves at the extracellular (E) face which were occupied by chains of particles [1].
• Cingulin regulates claudin-2 expression and cell proliferation through the small GTPase RhoA [2].
• U0126 treatment also induced claudin-2 expression and decreased TER in a high resistance mouse cortical collecting duct cell line (94D) [3].
• Transfection of constitutively active mitogen-activated protein kinase/extracellular signal-regulated kinase kinase into MDCK strain II cells also inhibited claudin-2 expression and increased TER [3].
• In order to characterize the contribution of claudin-2 to barrier and permeability properties of the tight junction in detail, we studied two strains of Madin-Darby canine kidney cells (MDCK-C7 and MDCK-C11) with different tight junctional permeabilities [4].

Anatomical context of Cldn2

• Thus, presence of junctional claudin-2 causes the formation of cation-selective channels sufficient to transform a 'tight' tight junction into a leaky one [4].
• Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells [4].
• Conversely, in LLC-PK1 cells, claudin-2 and -15 increased the permeability for Na+, whereas claudin-4 and -11 were without effect [5].
• In primary cultures of rat hepatocytes, IL-1beta caused the disappearance of connexin32, which was reciprocal to the induction and localization of claudin-2 to cell membranes [6].
• Claudin-2 mRNA and protein were found throughout the proximal tubule and in the contiguous early segment of the thin descending limb of long-looped nephrons [7].

Associations of Cldn2 with chemical compounds

• Claudin-2 is selectively expressed in proximal nephron in mouse kidney [7].
• In Raf-1-transfected cells treated with PD98059 and SB203580, but not LY294002, expression and localization of claudin-2, but not occludin, recovered, together with barrier function, measured as the TER value [8].

Other interactions of Cldn2

• Claudin-1, claudin-2 and claudin-11 are present in tight junctions of choroid plexus epithelium of the mouse [9].
• The changes of connexin32 and claudin-2 may be controlled at the transcriptional level via NF-kappaB, HNF-1alpha, and CDX2 [6].
• In Raf-1-transfected cells expression of occludin and claudin-2 was markedly down-regulated at the protein and mRNA levels and the TER value was decreased, while the permeability was increased [8].
• In confocal images, the subcellular localization of claudin-2 protein coincided with that of the tight junction protein ZO-1 [7].

Analytical, diagnostic and therapeutic context of Cldn2

• Reverse transcriptase-polymerase chain reaction analysis was used to define that mRNA for claudin-2, -4, -8, -12, and -13 was expressed in mouse bladder tissue [10].
• To localize claudin-2 in the mouse kidney, we performed in situ hybridization using an isoform-specific riboprobe and immunohistochemistry using a polyclonal antibody directed against a COOH-terminal peptide [7].

References