Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability.

By C. M. Itallie, C. Rahner, James M. Anderson. Journal of Clinical Investigation, 2001

613 citations recorded by the source corpus.

Subfields: Molecular Biology, Neurology

View Paper: https://www.semanticscholar.org/paper/026780bceeed84bcd343639b6de8ace070ad96f0

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. J. Turner
2. C. Niessen
3. A. Buckley
4. R. Lynch
5. E. Schneeberger
6. C. V. Van Itallie
7. Gerd Krause
8. A. Prat

In Neurology

1. J. Turner
2. C. Niessen
3. A. Buckley
4. R. Lynch
5. E. Schneeberger
6. C. V. Van Itallie
7. A. Prat
8. James M. Anderson

Citations in the corpus

• The tight junction: a multifunctional complex. (2004, methodology): “The perturbing effect of overexpressing modified TJ proteins (32, 33, 96, 146) was minimized by using retroviral infection (165), a strategy that leads to highly efficient insertion of a relatively low copy number of the transgene per cell.”
• Tight junctions/adherens junctions: basic structure and function. (2007, background): “More importantly, experimentally manipulating the type of claudin expression directly affected paracellular ion and/or size selectivity (Van Itallie et al ., 2001; Nitta et al ., 2003).”
• Tight Junction Pore and Leak Pathways: A Dynamic Duo (2011, background): “Evidence in favor of sealing includes the reduction in paracellular ion conductance when claudin-4 is overexpressed in MDCK cell monolayers (55) as well as the loss of barrier function induced by Clostridium perfringens enterotoxin, which binds to claudins 3 and 4 and induces their removal from the ”
• Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells (2002, background): “However, the first direct demonstration of the ability of a claudin to influence paracellular ion selectivity was contributed by Van Itallie et al. for claudin-4 (Van Itallie et al., 2001).”
• Structure and function of claudins. (2008, background): “Inner ear [57] – Extension in ECL2 [7] – Stomach, lung [61] 19 – Kidney, retina [102], – Reduces paracellular cation permeability in MDCK-II, increases TER [48] – Familial hypomagnesaemia with hypercalciuria and nephrocalcinosis, visual impairments; hypomagnesaemia mutations in TMD1, 2 and ECL1 (Q57”
• Physiology and function of the tight junction. (2009, background): “The ability to increase TER can be based on limiting permeability for just cations (claudin-4 [Van Itallie et al. 2001]) or both cations and anions (claudin-7 [Alexandre et al. 2005]).”
• The blood-brain barrier. (2015, background): “The strength of the junctions varies greatly depending on the tissue in which they are found, and work in cell culture suggests that they have a size-selective permeability to uncharged molecules of up to 4 nm, and then low permeability to larger molecules (Van Itallie and Anderson 2006; Van Itallie”
• Cell Biology of Tight Junction Barrier Regulation and Mucosal Disease (2018, background): “…whereas claudins can form strands, it may be the strands themselves that are responsible for the barrier (Lingaraju et al. 2015), or, alternatively, that the sealing claudins enhance the barrier by regulating pore-forming claudins (Van Itallie et al. 2001; Angelow et al. 2007; Turner et al. 2014).”
• Tight junctions and cell polarity. (2006, background): “These protein complexes not only guide tight junction formation but also play an important role in the establishment and maintenance of apico-basal polarity.”