scholarly journals The Protective Effect of Hamamelis virginiana Stem and Leaf Extract on Fine Dust-Induced Damage on Human Keratinocytes

Cosmetics ◽  
2021 ◽  
Vol 8 (4) ◽  
pp. 119
Author(s):  
Jiyoung Choi ◽  
Dongki Yang ◽  
Mi Yeon Moon ◽  
Gi Yeon Han ◽  
Moon Sik Chang ◽  
...  
Keyword(s):  
Particulate Matter ◽  
Tight Junction ◽  
Leaf Extract ◽  
Inflammatory Marker ◽  
Human Keratinocytes ◽  
Skin Care ◽  
Witch Hazel ◽  
Junction Protein ◽  
Skin Care Products

Witch hazel extracts have been used for decades as cosmetic ingredients in skin care products. Our present study aims to evaluate its potential in anti-pollution products using a previously reported in vitro model. Calcium is a universal second messenger, and we used human respiratory and skin cells to detect changes in intracellular Ca2+ concentrations upon particulate matter contact. Both an increase in pro-inflammatory markers and a decrease in tight junction proteins were confirmed, as previously reported. Witch hazel stem and leaf extract showed significant attenuation of Ca2+ response upon the challenge; it displayed systematic regulations of the signal generator, PAR-2; a pro-inflammatory marker, NF-κB; and a tight junction protein, Occludin. We identified hexagalloylglucose from the extract and concluded that it is a major component regulating protection from particulate matter. Based on these results, witch hazel extract containing hexagalloylglucose is an active ingredient in anti-pollution skin care products.

scholarly journals ZO-3, a Novel Member of the MAGUK Protein Family Found at the Tight Junction, Interacts with ZO-1 and Occludin

1998 ◽  
Vol 141 (1) ◽  
pp. 199-208 ◽  
Author(s):  
Julie Haskins ◽  
Lijie Gu ◽  
Erika S. Wittchen ◽  
Jennifer Hibbard ◽  
Bruce R. Stevenson
Keyword(s):  
Amino Acid ◽  
Tight Junction ◽  
Molecular Mass ◽  
Mdck Cells ◽  
Cdna Libraries ◽  
Pdz Domains ◽  
Large Tumor ◽  
Junction Protein ◽  
Discs Large

A 130-kD protein that coimmunoprecipitates with the tight junction protein ZO-1 was bulk purified from Madin-Darby canine kidney (MDCK) cells and subjected to partial endopeptidase digestion and amino acid sequencing. A resulting 19–amino acid sequence provided the basis for screening canine cDNA libraries. Five overlapping clones contained a single open reading frame of 2,694 bp coding for a protein of 898 amino acids with a predicted molecular mass of 98,414 daltons. Sequence analysis showed that this protein contains three PSD-95/SAP90, discs-large, ZO-1 (PDZ) domains, a src homology (SH3) domain, and a region similar to guanylate kinase, making it homologous to ZO-1, ZO-2, the discs large tumor suppressor gene product of Drosophila, and other members of the MAGUK family of proteins. Like ZO-1 and ZO-2, the novel protein contains a COOH-terminal acidic domain and a basic region between the first and second PDZ domains. Unlike ZO-1 and ZO-2, this protein displays a proline-rich region between PDZ2 and PDZ3 and apparently contains no alternatively spliced domain. MDCK cells stably transfected with an epitope-tagged construct expressed the exogenous polypeptide at an apparent molecular mass of ∼130 kD. Moreover, this protein colocalized with ZO-1 at tight junctions by immunofluorescence and immunoelectron microscopy. In vitro affinity analyses demonstrated that recombinant 130-kD protein directly interacts with ZO-1 and the cytoplasmic domain of occludin, but not with ZO-2. We propose that this protein be named ZO-3.

scholarly journals Papain Degrades Tight Junction Proteins of Human Keratinocytes In Vitro and Sensitizes C57BL/6 Mice via the Skin Independent of its Enzymatic Activity or TLR4 Activation

2015 ◽  
Vol 135 (7) ◽  
pp. 1790-1800 ◽  
Author(s):  
Caroline Stremnitzer ◽  
Krisztina Manzano-Szalai ◽  
Anna Willensdorfer ◽  
Philipp Starkl ◽  
Mario Pieper ◽  
...  
Keyword(s):  
Tight Junction ◽  
Enzymatic Activity ◽  
Human Keratinocytes ◽  
Tight Junction Proteins ◽  
Tlr4 Activation ◽  
Junction Proteins

scholarly journals Layilin is critical for mediating hyaluronan 35 kDa-induced intestinal epithelial tight junction protein ZO-1 in vitro and in vivo

2018 ◽  
Vol 66 ◽  
pp. 93-109 ◽  
Author(s):  
Yeojung Kim ◽  
Gail A. West ◽  
Greeshma Ray ◽  
Sean P. Kessler ◽  
Aaron C. Petrey ◽  
...  
Keyword(s):  
Tight Junction ◽  
Tight Junction Protein ◽  
Intestinal Epithelial ◽  
Junction Protein ◽  
Epithelial Tight Junction

scholarly journals The Heat-Shock Protein Apg-2 Binds to the Tight Junction Protein ZO-1 and Regulates Transcriptional Activity of ZONAB

2006 ◽  
Vol 17 (3) ◽  
pp. 1322-1330 ◽  
Author(s):  
Anna Tsapara ◽  
Karl Matter ◽  
Maria S. Balda
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Tight Junction ◽  
Intracellular Signaling ◽  
Transcriptional Activity ◽  
Adaptor Protein ◽  
Sh3 Domain ◽  
Nucleic Acid Binding ◽  
Junction Protein

The tight junction adaptor protein ZO-1 regulates intracellular signaling and cell proliferation. Its Src homology 3 (SH3) domain is required for the regulation of proliferation and binds to the Y-box transcription factor ZO-1-associated nucleic acid binding protein (ZONAB). Binding of ZO-1 to ZONAB results in cytoplasmic sequestration and hence inhibition of ZONAB's transcriptional activity. Here, we identify a new binding partner of the SH3 domain that modulates ZO-1–ZONAB signaling. Expression screening of a cDNA library with a fusion protein containing the SH3 domain yielded a cDNA coding for Apg-2, a member of the heat-shock protein 110 (Hsp 110) subfamily of Hsp70 heat-shock proteins, which is overexpressed in carcinomas. Regulated depletion of Apg-2 in Madin-Darby canine kidney cells inhibits G1/S phase progression. Apg-2 coimmunoprecipitates with ZO-1 and partially localizes to intercellular junctions. Junctional recruitment and coimmunoprecipitation with ZO-1 are stimulated by heat shock. Apg-2 competes with ZONAB for binding to the SH3 domain in vitro and regulates ZONAB's transcriptional activity in reporter gene assays. Our data hence support a model in which Apg-2 regulates ZONAB function by competing for binding to the SH3 domain of ZO-1 and suggest that Apg-2 functions as a regulator of ZO-1–ZONAB signaling in epithelial cells in response to cellular stress.

Abstract 166: Matrix Metalloproteinase-9 Mediates Post-hypoxic Vascular Pruning Of Cerebral Blood Vessels By Degrading Laminin And Claudin-5

2014 ◽  
Vol 115 (suppl_1) ◽  
Author(s):  
Amin Boroujerdi ◽  
Jennifer V Welser-Alves ◽  
Richard Milner
Keyword(s):  
Matrix Metalloproteinase ◽  
Tight Junction ◽  
Blood Vessels ◽  
Matrix Metalloproteinase 9 ◽  
Vascular Density ◽  
Cerebral Blood Vessels ◽  
Wild Type ◽  
Junction Protein ◽  
Metalloproteinase 9

Objective: Vascular remodeling involves a highly coordinated break-down and build-up of the vascular basal lamina and inter-endothelial tight junction proteins. The goal of this study was to examine the role of matrix metalloproteinase-9 (MMP-9) in remodeling of cerebral blood vessels, both in hypoxia-induced angiogenesis and in the vascular pruning that accompanies the switch from hypoxia back to normoxia. Approach and Results: In a chronic mild hypoxia model of cerebrovascular remodeling, gel zymography revealed that MMP-9 levels were increased, both in the hypoxic angiogenic response and in the post-hypoxic pruning response. Compared to wild-type mice, MMP-9 KO mice showed no alteration in hypoxic-induced angiogenesis, but did show marked delay in post-hypoxic vascular pruning. In wild-type mice, vascular pruning was associated with fragmentation of vascular laminin and the tight junction protein claudin-5, while this process was markedly attenuated in MMP-9 KO mice. In vitro experiments showed that hypoxia stimulated MMP-9 expression in brain endothelial cells (BECs) but not pericytes. While immunofluorescent and flow cytometry analyses showed that hypoxia led to reduced expression of laminin and claudin-5 in wild-type BECs, this decrease was absent in MMP-9 KO BECs. Conclusions: These results show that while MMP-9 is not essential for hypoxic-induced cerebral angiogenesis, it plays an important role in post-hypoxic vascular pruning by degrading laminin and claudin-5. Our data support the concept that MMP-9 inhibition might provide therapeutic benefit in the treatment of ischemic stroke, by preventing post-hypoxic vascular pruning, thereby optimizing vascular density and integrity.

scholarly journals Particulate matter air pollution disrupts endothelial cell barrier via calpain-mediated tight junction protein degradation

2012 ◽  
Vol 9 (1) ◽  
pp. 35 ◽  
Author(s):  
Ting Wang ◽  
Lichun Wang ◽  
Liliana Moreno-Vinasco ◽  
Gabriel D Lang ◽  
Jessica H Siegler ◽  
...  
Keyword(s):  
Air Pollution ◽  
Particulate Matter ◽  
Endothelial Cell ◽  
Tight Junction ◽  
Protein Degradation ◽  
Tight Junction Protein ◽  
Junction Protein

scholarly journals Diesel exhaust particles modulate the tight junction protein occludin in lung cells in vitro

2009 ◽  
Vol 6 (1) ◽  
pp. 26 ◽  
Author(s):  
Andrea D Lehmann ◽  
Fabian Blank ◽  
Oliver Baum ◽  
Peter Gehr ◽  
Barbara M Rothen-Rutishauser
Keyword(s):  
Tight Junction ◽  
Diesel Exhaust ◽  
Diesel Exhaust Particles ◽  
Tight Junction Protein ◽  
Lung Cells ◽  
Junction Protein ◽  
Exhaust Particles

scholarly journals Spatio-temporal expression pattern and role of the tight junction protein MarvelD3 in pancreas development and function

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Charlotte Heymans ◽  
Ophélie Delcorte ◽  
Catherine Spourquet ◽  
Mylah Villacorte-Tabelin ◽  
Sébastien Dupasquier ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Tight Junction ◽  
Expression Pattern ◽  
Pancreatic Tissue ◽  
Cell Polarization ◽  
Tight Junction Protein ◽  
Jnk Pathway ◽  
Genetic Ablation ◽  
Junction Protein

AbstractTight junction complexes are involved in the establishment and maintenance of cell polarity and the regulation of signalling pathways, controlling biological processes such as cell differentiation and cell proliferation. MarvelD3 is a tight junction protein expressed in adult epithelial and endothelial cells. In Xenopus laevis, MarvelD3 morphants present differentiation defects of several ectodermal derivatives. In vitro experiments further revealed that MarvelD3 couples tight junctions to the MEKK1-JNK pathway to regulate cell behaviour and survival. In this work, we found that MarvelD3 is expressed from early developmental stages in the exocrine and endocrine compartments of the pancreas, as well as in endothelial cells of this organ. We thoroughly characterized MarvelD3 expression pattern in developing pancreas and evaluated its function by genetic ablation. Surprisingly, inactivation of MarvelD3 in mice did not alter development and differentiation of the pancreatic tissue. Moreover, tight junction formation and organization, cell polarization, and activity of the JNK-pathway were not impacted by the deletion of MarvelD3.

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