scholarly journals Suppression of cellular adhesion and the anticancer activity of Aralia elata extract

2021 ◽  
Author(s):  
Je-Hyuk LEE
Keyword(s):  
Anticancer Activity ◽  
Cellular Adhesion ◽  
Aralia Elata

Segregation of cell adhesion molecules into membrane microdomains facilitates leukocyte-endothelial interactions

1995 ◽  
Vol 53 ◽  
pp. 780-781
Author(s):  
S.L. Erlandsen
Keyword(s):  
Cell Surface ◽  
Adhesion Molecules ◽  
Colloidal Gold ◽  
High Spatial Resolution ◽  
Low Voltage ◽  
Cellular Adhesion ◽  
Membrane Microdomains ◽  
Immunogold Label ◽  
Cellular Adhesion Molecules ◽  
Electron Detection

Cells interact with their extracellular environments by means of a variety of cellular adhesion molecules (CAM) and surface ligands. In many instances, CAMs interact in a sequential temporal fashion which suggests that these adhesion molecules may occupy or be polarized to various membrane microdomains on the cell surface. Detection of CAMs can be accomplished by a variety of methods including immunofluorescent microscopy and flow cytometry, and by the use of immunocytochemical markers (i.e. colloidal gold) in electron microscopy. The development of high resolution field emission SEM in the mid 1980's and the Autrata modification of the YAG detector for backscatter electron detection at low voltage has greatly facilitated the recognition of colloidal gold probes for detection of surface CAMs. Low voltage FESEM with Bse imaging provides increased resolution of cell surface topography (~3nm at 3-4 keV) which can be observed in 3-dimensions, and simultaneously permits detection/high spatial resolution of immunogold label by atomic number contrast.

Anticancer activity of resveratrol analogs from Eugenia rigida DC

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
MA Zaki ◽  
V Samoylenko ◽  
S Khan ◽  
RM Abd slam ◽  
MH Hetta ◽  
...  
Keyword(s):  
Anticancer Activity ◽  
Resveratrol Analogs

Specific inhbitor of ERK 1/2 AEZS-131: anticancer activity in models of human cancers with and without overactivation of ERK 1/2

2014 ◽  
Vol 74 (S 01) ◽  
Author(s):  
JB Engel ◽  
S Meyer ◽  
J Dietl ◽  
B Kwok ◽  
O Ortmann ◽  
...  
Keyword(s):  
Anticancer Activity ◽  
Human Cancers

Mislocalization of Adherens Junction- Associated Proteins in a Patient with Darier Disease

2018 ◽  
Vol 2 (3) ◽  
pp. 184-201
Author(s):  
George D Glinos ◽  
Irena Pastar ◽  
Marjana Tomic-Canic ◽  
Rivka C Stone
Keyword(s):  
Adherens Junction ◽  
Cellular Adhesion ◽  
Calcium Flux ◽  
Keratinocyte Differentiation ◽  
Calcium Dependent ◽  
Endoplasmic Reticulum Calcium ◽  
Darier Disease ◽  
Associated Proteins ◽  
Attachment Proteins ◽  
E Cadherin

Darier disease (DD) is an autosomal dominant keratinizing genodermatosis that manifests clinically with red-brown pruritic papules in a seborrheic distribution often in association with palmoplantar pits and dystrophic nail changes. It is caused by mutation in ATP2A2 which encodes a sarco/endoplasmic reticulum calcium ATPase isoform 2 (SERCA2) pump that regulates calcium flux. Consequent alteration of intracellular calcium homeostasis is thought to impair trafficking of cellular adhesion proteins and to lead to aberrant keratinocyte differentiation, contributing to the characteristic histopathologic features of acantholysis and dyskeratosis in DD, though the precise mechanisms are incompletely understood. Previous studies have identified defective localization of desmosomal attachment proteins in skin biopsies and cultured keratinocytes from DD patients, but reports of effects on adherens junction proteins (including calcium-dependent E-cadherin) are conflicting. Here we describe a case of DD presenting with characteristic clinical and histologic features in which we performed immunofluorescence staining of four adherens junction-associated proteins (E-cadherin, α-catenin, β-catenin, and vinculin). In lesional (acantholytic) DD skin, we identified loss of distinctive bright membranous staining that was present at the periphery of keratinocytes throughout the epidermis in the healthy skin of a matched donor. Perilesional (non-acantholytic) portions of DD skin partially recapitulated the normal phenotype. Our findings support a role for SERCA2 dysfunction in impaired assembly of adherens junctions, which together with defective desmosomes contribute to acantholysis in DD.

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