Aberrant retinal tight junction and adherens junction protein expression in an animal model of autosomal recessive Retinitis pigmentosa: The Rho(−/−) mouse

2006 ◽  
Vol 83 (3) ◽  
pp. 484-492 ◽  
Author(s):  
M. Campbell ◽  
M. Humphries ◽  
A. Kennan ◽  
P. Kenna ◽  
P. Humphries ◽  
...  
Keyword(s):  
Animal Model ◽  
Retinitis Pigmentosa ◽  
Protein Expression ◽  
Tight Junction ◽  
Autosomal Recessive ◽  
Adherens Junction ◽  
Adherens Junction Protein ◽  
Junction Protein

scholarly journals Stress‐induced Effects on Endometriosis and Tight Junction Protein Expression are Counteracted by VSL#3 Administration in an Animal Model

2019 ◽  
Vol 33 (S1) ◽  
Author(s):  
Adriana C Hernandez Santini ◽  
Myrella L Cruz ◽  
Gerardo A Arroyo ◽  
Raquel M Rivera‐Mendez ◽  
Gladys Chompre ◽  
...  
Keyword(s):  
Animal Model ◽  
Protein Expression ◽  
Tight Junction ◽  
Tight Junction Protein ◽  
Tight Junction Protein Expression ◽  
Junction Protein

116. Contribution of claudin-11 to the inter-Sertoli cell tight junction, in vitro

2005 ◽  
Vol 17 (9) ◽  
pp. 72
Author(s):  
M. J. McCabe ◽  
P. G. Stanton
Keyword(s):  
Tight Junction ◽  
Mrna Expression ◽  
Sertoli Cell ◽  
Adhesion Molecule ◽  
Sertoli Cells ◽  
Adherens Junction ◽  
Adherens Junction Protein ◽  
Junction Protein

The inter-Sertoli cell tight junction (TJ) forms the blood testis barrier (BTB) between Sertoli cells and is composed of three major transmembrane proteins: claudin-11, occludin and junctional adhesion molecule. Formation of the BTB occurs during puberty associating with an increase in circulating gonadotrophins. Claudin-11 and occludin are hormonally regulated in vitro although their importance to the function of the TJ is unknown. The aim of this study was to investigate the contribution of claudin-11 to the inter-Sertoli cell TJ in vitro by blocking gene expression using RNA interference. Two claudin-11-specific siRNA fragments were designed for this purpose. Sertoli cells in primary culture formed stable TJs within 5 days as measured by transepithelial electrical resistance (TER). The addition of siRNA for 2 days resulted in a significant (P < 0.01) 55% (mean, SD, n = 4 cultures) decrease in TER along with a major reduction in claudin-11 localisation to the TJ as assessed by immunocytochemistry. The specificity of the siRNA was shown by the presence of extensive immunostaining of occludin and of the adherens junction protein β-catenin in the same treatments. Similarly, claudin-11 mRNA expression significantly (P < 0.01) decreased by 71% (mean, SD, n = 3 cultures) in response to both claudin-11 siRNA fragments. Occludin mRNA expression was not affected. It is concluded that claudin-11 contributes at least 55% to the function of the rat Sertoli cell TJ in vitro. It is hypothesised that the remaining 45% of TJ function can be attributed to other integral proteins, such as occludin and junctional adhesion molecule. It is expected that claudin-11 and other TJ proteins play a pivotal role in the function of the BTB in vivo with potential implications in fertility and contraception.

scholarly journals The Tight Junction Protein Occludin and the Adherens Junction Protein α-Catenin Share a Common Interaction Mechanism with ZO-1

2004 ◽  
Vol 280 (5) ◽  
pp. 3747-3756 ◽  
Author(s):  
Sebastian L. Müller ◽  
Michael Portwich ◽  
Anke Schmidt ◽  
Darkhan I. Utepbergenov ◽  
Otmar Huber ◽  
...  
Keyword(s):  
Tight Junction ◽  
Interaction Mechanism ◽  
Adherens Junction ◽  
Tight Junction Protein ◽  
Adherens Junction Protein ◽  
Junction Protein

scholarly journals Mechanisms involved in AMPK-mediated deposition of tight junction components to the plasma membrane

2020 ◽  
Vol 318 (3) ◽  
pp. C486-C501
Author(s):  
Jingshing Wu ◽  
Pascal Rowart ◽  
Francois Jouret ◽  
Brandon M. Gassaway ◽  
Vanathy Rajendran ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Tight Junction ◽  
Adherens Junction ◽  
Bound State ◽  
Ampk Activation ◽  
Zonula Occludens ◽  
Adherens Junction Protein ◽  
Junction Protein ◽  
Associated Proteins ◽  
Amp Activated Protein Kinase

AMP-activated protein kinase (AMPK) activation promotes early stages of epithelial junction assembly. AMPK activation in MDCK renal epithelial cells facilitates localization of the junction-associated proteins aPKCζ and Par3 to the plasma membrane and promotes conversion of Cdc42, a key regulator of epithelial polarization and junction assembly, to its active GTP bound state. Furthermore, Par3 is an important regulator of AMPK-mediated aPKCζ localization. Both aPKCζ and Par3 serve as intermediates in AMPK-mediated junction assembly, with inhibition of aPKCζ activity or Par3 knockdown disrupting AMPK’s ability to facilitate zonula occludens (ZO-1) localization. AMPK phosphorylates the adherens junction protein afadin and regulates its interaction with the tight-junction protein zonula occludens-1. Afadin is phosphorylated at two critical sites, S228 (residing within an aPKCζ consensus site) and S1102 (residing within an AMPK consensus site), that are differentially regulated during junction assembly and that exert different effects on the process. Expression of phospho-defective mutants (S228A and S1102A) perturbed ZO-1 localization to the plasma membrane during AMPK-induced junction assembly. Expression of S228A increased the ZO-1/afadin interaction, while S1102A reduced this interaction during extracellular calcium-induced junction assembly. Inhibition of aPKCζ activity also increased the ZO-1/afadin interaction. Taken together, these data suggest that aPKCζ phosphorylation of afadin terminates the ZO-1/afadin interaction and thus permits the later stages of junction assembly.

Regulation of adherens junction protein expression in growth-activated 3T3 cells and in regenerating liver

1992 ◽  
Vol 202 (2) ◽  
pp. 477-486 ◽  
Author(s):  
Ursula Glück ◽  
JoséLuis Rodríguez Fernández ◽  
Roumen Pankov ◽  
Avri Ben-Ze'ev
Keyword(s):  
Protein Expression ◽  
Adherens Junction ◽  
Regenerating Liver ◽  
3T3 Cells ◽  
Adherens Junction Protein ◽  
Junction Protein
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