scholarly journals EMT Transcription Factors Are Involved in the Altered Cell Adhesion under Simulated Microgravity Effect or Overloading by Regulation of E-cadherin

2020 ◽  
Vol 21 (4) ◽  
pp. 1349 ◽  
Author(s):  
Shuliang Shi ◽  
Qiao Li ◽  
Qiuying Cao ◽  
Yan Diao ◽  
Yao Zhang ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Cell Adhesion ◽  
Simulated Microgravity ◽  
Time Dependent ◽  
Control Group ◽  
Adhesion Proteins ◽  
Stress Changes ◽  
Altered Cell ◽  
Microgravity Effect ◽  
E Cadherin

In order to study the effect of stress changes on cell adhesion, HUVEC, and MCF-7 cells were treated with simulated microgravity effect (SMG) and overloading (OL). Methods: Rotating Wall Vessel (2D-RWVS) bioreactor was used to create different culture conditions. In addition, the alteration of cell adhesion states, adhesion proteins, and relating factors of adhesion molecules under these two conditions were detected using cell adhesion assay, immunofluorescence, western blot, and qRT-PCR technology. Results: The results showed that the adhesion of cells decreased under SMG, while increased under OL. The expressions of integrin β1, paxillin, and E-cadherin under SMG condition were down-regulated as compared to that of the control group showing a time-dependent pattern of the decreasing. However, under OL condition, the expressions of adhesion proteins were up-regulated as compared to that of the control group, with a time-dependent pattern of increasing. EMT transcription factors Snail, twist, and ZEB1 were up-regulated under SMG while down-regulated under OL. Conclusion: Collectively our results indicated that cells could respond to stress changes to regulate the expressions of adhesion proteins and adapt their adhesion state to the altered mechanical environment. The altered cell adhesion in response to the mechanical stress may involve the changed expression of EMT-inducing factors, Snail, Twist, and ZEB1under the SMG/OL conditions.

scholarly journals Decreased expression of catenins (? and ?), p120 CTN, and E-cadherin cell adhesion proteins and E-cadherin gene promoter methylation in prostatic adenocarcinomas

Cancer ◽  
2001 ◽  
Vol 92 (11) ◽  
pp. 2786-2795 ◽  
Author(s):  
Bhaskar V. S. Kallakury ◽  
Christine E. Sheehan ◽  
Emily Winn-Deen ◽  
Julie Oliver ◽  
Hugh A. G. Fisher ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Promoter Methylation ◽  
Gene Promoter ◽  
Adhesion Proteins ◽  
Cell Adhesion Proteins ◽  
E Cadherin

The homeodomain transcription factors Cdx1 and Cdx2 induce E-cadherin adhesion activity by reducing β- and p120-catenin tyrosine phosphorylation

2007 ◽  
Vol 293 (1) ◽  
pp. G54-G65 ◽  
Author(s):  
Toshihiko Ezaki ◽  
Rong-Jun Guo ◽  
Hong Li ◽  
Albert B. Reynolds ◽  
John P. Lynch
Keyword(s):  
Transcription Factors ◽  
Cell Adhesion ◽  
Tyrosine Phosphorylation ◽  
Intestinal Cell ◽  
Specific Gene ◽  
P120 Catenin ◽  
Cdx2 Expression ◽  
E Cadherin ◽  
Cell Cell ◽  
Homeodomain Transcription Factors

The homeodomain transcription factors Cdx1 and Cdx2 are regulators of intestine-specific gene expression. They also regulate intestinal cell differentiation and proliferation; however, these effects are poorly understood. Previously, we have shown that expression of Cdx1 or Cdx2 in human Colo 205 cells induces a mature colonocyte morphology characterized by the induction of a polarized, columnar shape with apical microvilli and strong cell-cell adhesion. To elucidate the mechanism underlying this phenomenon, we investigated the adherens junction complex. Cdx1 or Cdx2 expression reduced Colo 205 cell migration and invasion in vitro, suggesting a physiologically significant change in cadherin function. However, Cdx expression did not significantly effect E-cadherin, α-, β-, or γ-catenin, or p120-catenin protein levels. Additionally, no alteration in their intracellular distribution was observed. Cdx expression did not alter the coprecipitation of β-catenin with E-cadherin; however, it did reduce p120-catenin-E-cadherin coprecipitation. Tyrosine phosphorylation of β- and p120-catenin is known to disrupt E-cadherin-mediated cell adhesion and is associated with robust p120-catenin/E-cadherin interactions. We specifically investigated β- and p120-catenin for tyrosine phosphorylation and found that it was significantly diminished by Cdx1 or Cdx2 expression. We restored β- and p120-catenin tyrosine phosphorylation in Cdx2-expressing cells by knocking down the expression of protein tyrosine phosphatase 1B and noted a significant decline in cell-cell adhesion. We conclude that Cdx expression in Colo 205 cells induces E-cadherin-dependent cell-cell adhesion by reducing β- and p120-catenin tyrosine phosphorylation. Ascertaining the mechanism for this novel Cdx effect may improve our understanding of the regulation of cell-cell adhesion in the colonic epithelium.

scholarly journals Neurobehavioral and Ultrastructural Changes Induced by Phytosynthesized Silver-Nanoparticle Toxicity in an In Vivo Rat Model

Nanomaterials ◽  
2021 ◽  
Vol 12 (1) ◽  
pp. 58
Author(s):  
Razvan Vlad Opris ◽  
Vlad Toma ◽  
Alina Mihaela Baciu ◽  
Remus Moldovan ◽  
Bogdan Dume ◽  
...  
Keyword(s):  
Brain Regions ◽  
Time Dependent ◽  
Ultrastructural Changes ◽  
Control Group ◽  
Adult Rats ◽  
Male Adult ◽  
Cornus Mas ◽  
Transmission Electron ◽  
Altered Cell

(1) Background: The study aimed to assess neurobehavioral, ultrastructural, and biochemical changes induced by silver nanoparticles synthesized with Cornus mas L. extract (AgNPs-CM) in rat brains. (2) Methods: The study included 36 male adult rats divided into three groups. Over a period of 45 days, AgNPs-CM (0.8 and 1.5 mg/kg b.w.) were administered daily by gavage to two of the groups, while the control group received the vehicle used for AgNP. After treatment, OFT and EPM tests were conducted in order to assess neurobehavioral changes. Six of the animals from each group were sacrificed immediately after completion of treatment, while the remaining six were allowed to recuperate for an additional 15 days. Transmission electron microscopy (TEM), GFAP immunohistochemistry, and evaluation of TNFα, IL-6, MDA, and CAT activity were performed on the frontal cortex and hippocampus. (3) Results: Treated animals displayed a dose- and time-dependent increase in anxiety-like behavior and severe ultrastructural changes in neurons, astrocytes, and capillaries in both brain regions. Immunohistochemistry displayed astrogliosis with altered cell morphology. TNFα, IL-6, MDA, and CAT activity were significantly altered, depending on brain region and time post exposure. (4) Conclusions: AgNPs-CM induced neurobehavioral changes and severe cell lesions that continued to escalate after cessation of exposure.

Isoform-specific function of calpains in cell adhesion disruption: studies in postlactational mammary gland and breast cancer

2016 ◽  
Vol 473 (18) ◽  
pp. 2893-2909 ◽  
Author(s):  
Lucía Rodríguez-Fernández ◽  
Iván Ferrer-Vicens ◽  
Concha García ◽  
Sara S. Oltra ◽  
Rosa Zaragozá ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Migration ◽  
Cell Adhesion ◽  
Mammary Gland ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Proximity Ligation Assay ◽  
Specific Function ◽  
Adhesion Proteins ◽  
E Cadherin

Cleavage of adhesion proteins is the first step for physiological clearance of undesired cells during postlactational regression of the mammary gland, but also for cell migration in pathological states such as breast cancer. The intracellular Ca2+-dependent proteases, calpains (CAPNs), are known to cleave adhesion proteins. The isoform-specific function of CAPN1 and CAPN2 was explored and compared in two models of cell adhesion disruption: mice mammary gland during weaning-induced involution and breast cancer cell lines according to tumor subtype classification. In both models, E-cadherin, β-catenin, p-120, and talin-1 were cleaved as assessed by western blot analysis. Both CAPNs were able to cleave adhesion proteins from lactating mammary gland in vitro. Nevertheless, CAPN2 was the only isoform found to co-localize with E-cadherin in cell junctions at the peak of lactation. CAPN2/E-cadherin in vivo interaction, analyzed by proximity ligation assay, was dramatically increased during involution. Calpain inhibitor administration prevented the cytosolic accumulation of truncated E-cadherin cleaved by CAPN2. Conversely, in breast cancer cells, CAPN2 was restricted to the nuclear compartment. The isoform-specific expression of CAPNs and CAPN activity was dependent on the breast cancer subtype. However, CAPN1 and CAPN2 knockdown cells showed that cleavage of adhesion proteins and cell migration was mediated by CAPN1, independently of the breast cancer cell line used. Data presented here suggest that the subcellular distribution of CAPN1 and CAPN2 is a major issue in target-substrate recognition; therefore, it determines the isoform-specific role of CAPNs during disruption of cell adhesion in either a physiological or a pathological context.

Expression of cell adhesion molecule E-cadherin in human arachnoid villi

1992 ◽  
Vol 77 (5) ◽  
pp. 749-756 ◽  
Author(s):  
Tetsumori Yamashima ◽  
Yasuo Tohma ◽  
Junkoh Yamashita
Keyword(s):  
Cerebrospinal Fluid ◽  
Surface Layer ◽  
Cell Adhesion ◽  
Plasma Membranes ◽  
Cell Junctions ◽  
Control Group ◽  
Content Type ◽  
Arachnoid Villi ◽  
Arachnoid Villus ◽  
E Cadherin

✓ Calcium-dependent epithelial cell adhesion molecules designated as E-cadherin (also known as uvomorulin or L-CAM) were identified in human arachnoid villi by immunoblotting and immunocytochemical analyses using a monoclonal antibody HECD-1 raised against human mammary carcinoma MCF-7 cells. Immunoblot analysis showed that HECD-1 recognizes E-cadherin with a molecular weight of 124 kD. In all arachnoid cells of an arachnoid villus, E-cadherin was detected by immunolight microscopy within the cytoplasm rather than the cellular boundaries as seen in the control group. Furthermore, the extent of expression by immunolight microscopy varied from portion to portion. The expression was usually weak in the syncytial cluster which was ultrastructurally composed of tightly juxtaposed cells characterized by few extracellular cisterns and numerous cell junctions, while it was intense in the reticular cluster and the surface layer which were ultrastructurally characterized by abundant extracellular cisterns and smaller numbers of cell junctions. The cells of the reticular cluster and the surface layer contained more free ribosomes than those of the syncytial cluster. Immunoelectron microscopy showed that E-cadherin was localized not only to the opposing plasma membranes and the cytoplasm around the free ribosomes or the rough endoplasmic reticulum but also to the extracellular cisterns. As the expression of E-cadherin was closely related to the arachnoid cells adjacent to the cerebrospinal fluid pathway, it is suggested that, instead of the cell junctions, E-cadherin may play an important role in the flexible adhesion of arachnoid cells even in the presence of the cerebrospinal fluid.

Co-downregulation of cell adhesion proteins α- and β-catenins, p120CTN, E-cadherin, and CD44 in prostatic adenocarcinomas

2001 ◽  
Vol 32 (8) ◽  
pp. 849-855 ◽  
Author(s):  
Bhaskar V.S. Kallakury ◽  
Christine E. Sheehan ◽  
Jeffrey S. Ross
Keyword(s):  
Cell Adhesion ◽  
Adhesion Proteins ◽  
Cell Adhesion Proteins ◽  
E Cadherin

622: Von Hippel-Lindau Inactivation Downregulates the Cell-Cell Adhesion Molecule E Cadherin in Renal Cancer Cells

2005 ◽  
Vol 173 (4S) ◽  
pp. 170-170
Author(s):  
Maxine G. Tran ◽  
Miguel A. Esteban ◽  
Peter D. Hill ◽  
Ashish Chandra ◽  
Tim S. O'Brien ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cancer Cells ◽  
Renal Cancer ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Von Hippel Lindau ◽  
E Cadherin ◽  
Cell Cell
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