Endothelial Claudin

Morita, Kazumasa; Sasaki, Hiroyuki; Furuse, Mikio; Tsukita, Shöichiro

doi:10.1083/jcb.147.1.185

Cited by 747 publications

(271 citation statements)

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“…Expression of claudin proteins in primary tissues has been demonstrated for claudin-1, -2, -3, -4, and -8 in kidney and liver tissues (11,62). Claudin-5 has been demonstrated to be a component of tight junctions in endothelial cells (63), and claudin-11 expression has been demonstrated in tight junctions of sertoli cells and brain myelin sheets (61,63). Furthermore, the kidney epithelial cell line MDCK preferably expresses claudin-1 and claudin-4 but little claudin-2 and claudin-3 (64), whereas the human intestinal epithelial cell line T-84 is able to express both claudin-1 and claudin-2 in tight junctional complexes (10).…”

Section: Il-15 Regulates the Expression And Membrane Association Of Tmentioning

confidence: 99%

Interleukin-2 Receptor β Subunit-dependent and -independent Regulation of Intestinal Epithelial Tight Junctions

Nishiyama¹,

Sakaguchi²,

Kinugasa³

et al. 2001

Journal of Biological Chemistry

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Section: Il-15 Regulates the Expression And Membrane Association Of Tmentioning

confidence: 99%

Interleukin-2 Receptor β Subunit-dependent and -independent Regulation of Intestinal Epithelial Tight Junctions

Nishiyama¹,

Sakaguchi²,

Kinugasa³

et al. 2001

Journal of Biological Chemistry

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“…Although all endothelial cells share some common properties, they are heterogeneous with respect to their structure, protein expression, surface phenotype and secreted molecules depending on their tissue of origin and position in the vascular tree. [1][2][3] Brain endothelial cells which form the blood brain barrier (BBB) are coupled by continuous tight junctions of extremely low permeability to hydrophilic substances, which are more like those of epithelial barriers. In contrast endothelial cells in non-neural tissues have discontinuous tight junctions.…”

Section: Introductionmentioning

confidence: 99%

Action of Transcription Factors in the Control of Transferrin Receptor Expression in Human Brain Endothelium

Holloway

Sade

Romero

et al. 2007

Journal of Molecular Biology

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SummaryBrain endothelium has a distinctive phenotype, including high expression of transferrin receptor, pglycoprotein, claudin-5 and occludin. Dermal endothelium expresses lower levels of the transferrin receptor and it is absent from lung endothelium. All three endothelia were screened for transcription factors that bind the transferrin receptor promoter and show different patterns of binding between the endothelia. The transcription factor YY1 has distinct DNA-binding activities in brain endothelium and non-brain endothelium. The target-sites on the transferrin receptor promotor for YY1 lie in close proximity to those of the transcription initiation complex containing TFIID, so the two transcription factors potentially compete or interfere. Notably, the DNA-binding activity of TFIID was the converse of YY1, in different endothelia. YY1 knockdown reduced transferrin receptor expression in brain endothelium, but not in dermal endothelium implying that YY1 is involved in tissue-specific regulation of the transferrin receptor. Moreover a distinct YY1 variant is present in brain endothelium and it associates with Sp3. A model is presented, in which expression from the transferrin receptor gene in endothelium requires the activity of both TFIID and Sp3, but whether the gene is transcribed in different endothelia, is related to the balance between activating and suppressive forms of YY1.

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“…5 and 17). Claudins with molecular masses of Ϸ23 kDa comprise a multigene family consisting of more than 20 members (11,(17)(18)(19)(20)(21). Claudins also bear four transmembrane domains, but do not show any sequence similarity to occludin.…”

mentioning

confidence: 99%

Dynamic behavior of paired claudin strands within apposing plasma membranes

Sasaki

Matsui

Furuse

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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174

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The tight junction (TJ) strand is a linear proteinaceous polymer spanning plasma membranes, and each TJ strand associates laterally with another TJ strand in the apposing membranes of adjacent cells to form ''paired'' TJ strands. Claudins have been identified as the major constituents of TJ strands, and when exogenously expressed in L fibroblasts, they polymerize into paired strands, which are morphologically similar to paired TJ strands in epithelia. Here, we show that a fusion protein of GFP with claudin-1 can also form similar paired strands in L fibroblasts, allowing us to directly observe individual paired claudin strands in live cells in real time. These paired strands showed more dynamic behavior than expected; they were occasionally broken and annealed, and dynamically associated with each other in both an end-to-side and side-to-side manner. Through this behavior of individual paired claudin strands, the network of strands was reorganized dynamically. Furthermore, fluorescence recovery after photobleaching analyses revealed that claudin molecules were not mobile within paired strands. Although these observations are not necessarily representative of TJ strands per se in epithelial cells, they provide important information on the structural and kinetic properties of TJ strands in situ with significant implications for barrier function of TJs. T he tight junction (TJ) is one mode of cell-to-cell adhesion in epithelial and endothelial cells. TJs seal the cells to create a primary barrier to the diffusion of solutes across the cellular sheet, and also function as a boundary between the apical and basolateral membrane domains to produce their polarization (1-5). On ultrathin section electron microscopy, TJs appear as a series of discrete sites of apparent fusion, involving the outer leaflets of the plasma membranes of adjacent cells (6). On freeze-fracture electron microscopy, TJs appear as a set of continuous, anastomosing intramembranous particle strands (TJ strands; ref. 7). These observations led to our current understanding of the three-dimensional structure of TJs; each TJ strand associates laterally with another TJ strand in apposing membranes of adjacent cells to form ''paired'' TJ strands, where the intercellular space is completely obliterated (reviewed in ref. 5).To date, three distinct types of integral membrane proteins have been shown to be localized at TJs; occludin (8, 9), junctional adhesion molecule (10), and claudins (11). Occludin, an Ϸ65-kDa integral membrane protein with four transmembrane domains, was identified as the first component of TJ strands. However, several studies including gene knockout analyses revealed that TJ strands can be formed without occludin (12-15). JAM with a single transmembrane domain was recently shown to associate laterally with TJ strands, but not to constitute the strands per se (16). In contrast, claudin is now believed to be a major constituent of TJ strands (reviewed in refs. 5 and 17). Claudins with molecular masses of Ϸ23 kDa comprise a multigene family...

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Endothelial Claudin

Cited by 747 publications

References 56 publications

Interleukin-2 Receptor β Subunit-dependent and -independent Regulation of Intestinal Epithelial Tight Junctions

Interleukin-2 Receptor β Subunit-dependent and -independent Regulation of Intestinal Epithelial Tight Junctions

Action of Transcription Factors in the Control of Transferrin Receptor Expression in Human Brain Endothelium

Dynamic behavior of paired claudin strands within apposing plasma membranes

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