anti-Tricellulin (MARVELD2) Antikörper

Mouse (Murine) Tricellulin (MARVELD2) Interaktionspartner

1. Findings suggest that both tricellular tight junctions proteins TRIC and LSR have crucial roles for the differentiated cochlear cell survival.

2. Tricellulin is a specific redox sensor and sealing element at 3-cell contacts and may compensate as a redox mediator for occludin loss at 2-cell contacts in vivo and in vitro.

3. GFP-tagged angulin-1/LSR, in which serine 288 was substituted by alanine, was observed to be dispersed to bicellular junctions, indicating that phosphorylation of Ser288 is crucial for the exclusive localization of angulin-1/LSR and tricellulin at tTJs.

4. localization of angulin-1/LSR and tricellulin at tricellular contacts of brain and retinal endothelial cells in vivo

5. Loss of tricellulin prevented the coalition of the strands of the bicellular junction with the central element of the tricellular junction in the inner ear epithelia.

6. The findings show the heterogeneity of the molecular organization of tTJs in terms of the content of LSR, ILDR1 or ILDR2, and suggest that ILDR1-mediated recruitment of tricellulin to TCs is required for hearing.

7. The tricellulin may be a component to maintain the integrity for PNS myelin function and morphology.

8. marvelD3, occludin, and tricellulin define the tight junction-associated MARVEL protein family

9. In this study, we identify tricellulin, the first integral membrane protein that is concentrated at the vertically oriented TJ strands of tricellular contacts.

10. In the inner ear, tricellulin is concentrated at the tricellular tight-junctions in cochlear and vestibular epithelia, including the structurally complex and extensive junctions between supporting and hair cells.

11. Knockdown of occludin caused mislocalization of tricellulin to bTJs, implying that occludin supports tricellular localization of tricellulin by excluding tricellulin from bicellular tight junctions.

Human Tricellulin (MARVELD2) Interaktionspartner

1. ELISA revealed that Crohn's Disease twins demonstrated significantly lower levels of tight junction protein tricellulin compared with external controls.

2. this study shows that tricellulin is regulated via interleukin-13-receptor alpha2, affects macromolecule uptake, and is decreased in ulcerative colitis

3. Our results provide new insights into the function of tricellulin, and its nuclear localization may become a new prognostic factor for pancreatic cancers.

4. GSK3beta may inhibit VRK2 catalytic activity by disrupting its flexibility. The inhibition of VRK2 catalytic activity by GSK3beta may also inhibit VRK2-induced degradation of TRiC, which could suppress polyQ-expanded Htt aggregation.

5. Tricellulin-dependent macromolecule passage was comparably regulated in leaky and tight epithelia, but relative and absolute ion permeabilities of the tricellular tight junction (tTJ) were different.

6. Data show that the E3 ubiquitin ligase Itch forms a complex with tricellulin and thereby enhances its ubiquitination.

7. we demonstrated that PLG functions as a molecular bridge between tricellulin and streptococcal surface enolase (SEN). The wild type strain efficiently translocated across the epithelial monolayer, accompanied by cleavage of transmembrane junctional proteins.

8. The expressions of MARVELD2, CLDN1 and CLDN3 mRNA were significantly lower in cholesteatoma tissue and may be involved in epithelium permeability.

9. High tricellulin expression is associated with hepatocellular carcinoma.

10. MARVELD2 variants are responsible for about 1.5 % (95 % CI 0.8-2.6) of non-syndromic hearing loss in our cohort of 800 Pakistani families. The c.1331+2T>C allele is recurrent.

11. The findings show the heterogeneity of the molecular organization of tTJs in terms of the content of LSR, ILDR1 or ILDR2, and suggest that ILDR1-mediated recruitment of tricellulin to TCs is required for hearing.

12. This study reveals the presence and subcellular distribution of tricellulin in brain endothelial cells.

13. The dynamic behavior of tricellulin during the destruction and formation of tight junctions (TJ) under various extracellular calcium conditions seems to be closely associated with the barrier and fence functions of TJs.

14. DFNB49 is an important cause of non-syndromic deafness in Czech Roma patients but not in the general Czech population.

15. the tricellulin expression profile in normal and neoplastic human pancreas

16. tricellulin and its role in tight junction formation and maintenance

17. tricellulin is markedly reduced at all stages of tumor development. In situ hybridization analysis showed no correlation between HPV infection and altered expression of the tight junction proteins.

18. the expression of tricellulin both in microglia and in the stomach immune cells point to a possible role of this new tight junctions protein in the immune system.

19. JNK may be involved in the regulation of tricellular tight junctions including TRIC expression and the barrier function in pancreatic duct epithelial cells.

20. marvelD3, occludin, and tricellulin define the tight junction-associated MARVEL protein family