Expression of Cell Adhesion Molecules in Endometrial Tissue and Endometrioid Adenocarcinomas

2021 ◽  
Vol 6 (5) ◽  
pp. 89-94
Author(s):  
M. S. Lyndin ◽  
◽  
O. I. Kravtsova ◽  
V. V. Sikora ◽  
N. I. Hyriavenko ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Malignant Tumors ◽  
Endometrial Adenocarcinoma ◽  
Intercellular Adhesion ◽  
Endometrial Tissue ◽  
Endometrioid Adenocarcinoma ◽  
Apical Surface ◽  
Normal Endometrium ◽  
E Cadherin

Endometrioid endometrial adenocarcinomas are the most common histological variant of malignant tumors in the uterine cavity. In turn, the features of expression by neoplastic cells of intercellular adhesion molecules are a reliable prognostic factor in the progression of malignant tumors. One of the important indicators of cancer progression is E-cadherin, which determines the strength of intercellular adhesion and the ability of cells to spread. Among other adhesion molecules, considerable attention has recently been paid to the molecules of cell adhesion of carcino-embryonic antigen 1 (MCA-REA1). Therefore, the purpose of the study was to study the expression of E-cadherin and MCA-REA1 in normal endometrium and endometrioid adenocarcinomas. Materials and methods. To achieve this purpose, we performed tissue studies of 10 samples of normal endometrium and 30 samples of endometrioid endometrial adenocarcinoma (8380/3). Morphological features of neoplastic tissue were studied by hematoxylin and eosin staining. Visualization of E-cadherin and MCA-REA1 receptors was determined using the appropriate antibodies and the UltraVision Quanto Detection System HRP DAB Chromogen (Thermo scientific, USA) in similar areas of the tumor on serial sections. Results and discussion. It has been shown that endometrial tissue demonstrates different expression of MCA-REA1 and E-cadherin receptors in the normal state and in endometrioid adenocarcinomas. This indicates the absence of any functional correlation between them. Expression of MCA-REA1 was detected on the apical surface of the luminal and glandular columnar epithelium. In contrast, the endometrioid endometrial carcinoma tissues showed the pronounced heterogeneous location of MCA-REA1 in tumor cells. Moreover, due to the tumor dedifferentiation, these proteins disappear from the cell surface. On the other hand, E-cadherin is normally localized in intercellular contacts and epithelial-mesenchymal junctions. During carcinoma dedifferentiation, the intensity of E-cadherin expression decreased, which was accompanied by an increase in nuclear polymorphism of cancer cells and focal separation of cells from the total tumor mass. Conclusion. The variability of the expression patterns of MCA-REA1 and E-cadherin in the dedifferentiation of endometrioid adenocarcinoma may be an indicator of neoplastic transformation and progression of the malignant process

scholarly journals Reevaluating αE-catenin monomer and homodimer functions by characterizing E-cadherin/αE-catenin chimeras

2015 ◽  
Vol 210 (7) ◽  
pp. 1065-1074 ◽  
Author(s):  
Julie M. Bianchini ◽  
Khameeka N. Kitt ◽  
Martijn Gloerich ◽  
Sabine Pokutta ◽  
William I. Weis ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Intercellular Adhesion ◽  
Dependent Cell ◽  
In Cells ◽  
E Cadherin ◽  
Cell Cell

As part of the E-cadherin–β-catenin–αE-catenin complex (CCC), mammalian αE-catenin binds F-actin weakly in the absence of force, whereas cytosolic αE-catenin forms a homodimer that interacts more strongly with F-actin. It has been concluded that cytosolic αE-catenin homodimer is not important for intercellular adhesion because E-cadherin/αE-catenin chimeras thought to mimic the CCC are sufficient to induce cell–cell adhesion. We show that, unlike αE-catenin in the CCC, these chimeras homodimerize, bind F-actin strongly, and inhibit the Arp2/3 complex, all of which are properties of the αE-catenin homodimer. To more accurately mimic the junctional CCC, we designed a constitutively monomeric chimera, and show that E-cadherin–dependent cell adhesion is weaker in cells expressing this chimera compared with cells in which αE-catenin homodimers are present. Our results demonstrate that E-cadherin/αE-catenin chimeras used previously do not mimic αE-catenin in the native CCC, and imply that both CCC-bound monomer and cytosolic homodimer αE-catenin are required for strong cell–cell adhesion.

scholarly journals Differences in E-Cadherin and Syndecan-1 Expression in Different Types of Ameloblastomas

2018 ◽  
Vol 2018 ◽  
pp. 1-10 ◽  
Author(s):  
Ramón G. Carreón-Burciaga ◽  
Rogelio González-González ◽  
Nelly Molina-Frechero ◽  
Sandra López-Verdín ◽  
Vanesa Pereira-Prado ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Tumor Size ◽  
Cell Adhesion Molecules ◽  
Strong Association ◽  
Tumor Aggressiveness ◽  
Future Studies ◽  
Unicystic Ameloblastoma ◽  
Different Types ◽  
E Cadherin

Ameloblastomas are a group of benign, locally aggressive, recurrent tumors characterized by their slow and infiltrative growth. E-Cadherin and syndecan-1 are cell adhesion molecules related to the behavior of various tumors, including ameloblastomas. Ninety-nine ameloblastoma samples were studied; the expression of E-cadherin and syndecan-1 were evaluated by immunohistochemistry. E-Cadherin and epithelial syndecan-1 were more highly expressed in intraluminal/luminal unicystic ameloblastoma than in mural unicystic ameloblastoma and solid/multicystic ameloblastoma, whereas the stromal expression of syndecan-1 was higher in mural unicystic ameloblastoma and solid/multicystic ameloblastoma. Synchronicity was observed between E-cadherin and epithelial syndecan-1; the expression was correlated with intensity in all cases. There was a strong association between expression and tumor size and recurrence. The evaluation of the expression of E-cadherin and syndecan-1 are important for determining the potential aggressiveness of ameloblastoma variants. Future studies are required to understand how the expression of these markers is related to tumor aggressiveness.

scholarly journals Ultrastructural localization of E-cadherin cell adhesion molecule on the cytoplasmic membrane of keratinocytes in vivo and in vitro.

1994 ◽  
Vol 42 (10) ◽  
pp. 1333-1340 ◽  
Author(s):  
Y Horiguchi ◽  
F Furukawa ◽  
M Fujita ◽  
S Imamura
Keyword(s):  
Cell Adhesion ◽  
Free Surface ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Cytoplasmic Membrane ◽  
Ultrastructural Localization ◽  
In Vivo Studies ◽  
E Cadherin

We examined the ultrastructural localization of E (epithelial)-cadherin cell adhesion molecules by immunoperoxidase electron microscopy on the epithelium of mouse intestine, epidermis of human skin, and cultured human keratinocytes. The in vivo studies demonstrated that E-cadherin was present at the intermediate junction but not at the desmosome of the mouse intestinal single epithelium, and was found on the cytoplasmic membranes of keratinocytes with condensation in the intercellular space of the desmosomes, except for the basal surface of the basal cells. In vitro studies demonstrated that keratinocytes cultured in medium containing a low Ca2+ concentration (0.1 mM) lacked the tight connection through desmosomes, and that E-cadherin showed diffuse distribution and dot-like accumulation around the free surface of the cytoplasmic membrane. In culture medium containing a high concentration of Ca2+ (0.6 mM), keratinocytes formed desmosomal adhesion structures in which E-cadherin was accumulated. The free surface of the keratinocytes in this medium showed weaker distribution and a lesser amount of dot-like accumulation of E-cadherin than that in a low Ca2+ condition. These findings suggest that the distribution pattern of the E-cadherin cell adhesion molecules on the keratinocytes is different from that on the single epithelium of the intestine, and that E-cadherin on the cytoplasmic membrane of the keratinocytes shifts to the desmosomes under physiological conditions, participating in adhesion in association with other desmosomal cadherins.

Expression of a dominant negative cadherin mutant inhibits proliferation and stimulates terminal differentiation of human epidermal keratinocytes

1996 ◽  
Vol 109 (13) ◽  
pp. 3013-3023 ◽  
Author(s):  
A.J. Zhu ◽  
F.M. Watt
Keyword(s):  
Cell Adhesion ◽  
Terminal Differentiation ◽  
Intercellular Adhesion ◽  
Dominant Negative ◽  
Epidermal Keratinocytes ◽  
Dominant Negative Mutant ◽  
Beta Catenin ◽  
Human Epidermal Keratinocytes ◽  
Negative Mutant ◽  
E Cadherin

Cell adhesion molecules are not only required for maintenance of tissue integrity, but also regulate many aspects of cell behaviour, including growth and differentiation. While the regulatory functions of integrin extracellular matrix receptors in keratinocytes are well established, such functions have not been investigated for the primary receptors that mediate keratinocyte intercellular adhesion, the cadherins. To examine cadherin function in normal human epidermal keratinocytes we used a retroviral vector to introduce a dominant negative E-cadherin mutant, consisting of the extracellular domain of H-2Kd and the transmembrane and cytoplasmic domains of E-cadherin. As a control a vector containing the same construct, but with the catenin binding site destroyed, was prepared. High levels of expression of the constructs were achieved; the dominant negative mutant, but not the control, formed complexes with alpha-, beta- and gamma-catenin. In cells expressing the dominant negative mutant there was a 5-fold decrease in the level of endogenous cadherins and a 3-fold increase in the level of beta-catenin. Cell-cell adhesion and stratification were inhibited by the dominant negative mutant and desmosome formation was reduced. Expression of the mutant resulted in reduced levels of the alpha 2 beta 1 and alpha 3 beta 1 integrins and increased cell motility, providing further evidence for cross-talk between cadherins and the beta 1 integrins. In view of the widely documented loss of E-cadherin in keratinocyte tumours it was surprising that the dominant negative mutant had an inhibitory effect on keratinocyte proliferation and stimulated terminal differentiation even under conditions in which intercellular adhesion was prevented. These results establish a role for cadherins in regulating keratinocyte growth and differentiation and raise interesting questions as to the relative importance of cell adhesion-dependent and -independent mechanisms.

Human telomerase RNA as endogenous control in endometrial tissue

2005 ◽  
Vol 15 (2) ◽  
pp. 343-348
Author(s):  
M. Paul-Samojedny ◽  
A. Witek ◽  
A. Samojedny ◽  
A. Witkowska ◽  
T. Wilczok
Keyword(s):  
Reverse Transcriptase ◽  
Endometrial Hyperplasia ◽  
Expression Profiles ◽  
Quantitative Polymerase Chain Reaction ◽  
Endometrial Adenocarcinoma ◽  
Endometrial Tissue ◽  
Endogenous Control ◽  
Telomerase Rna ◽  
Normal Endometrium ◽  
Human Telomerase

Telomerase is a reverse transcriptase that adds repetitive telomere sequences to the end of chromosomes, which is thought to be essential for cellular immortality and oncogenesis. The enzyme consists of three subunits: human telomerase reverse transcriptase (hTERT), human telomerase RNA (hTR), and telomerase protein 1 (TP1). The hTERT subunit determines the activity of telomerase as an enzyme and is detected in most human tumors and regenerative cells. But many studies have revealed that hTR and TP1 are expressed constitutively. This resuts suggest that the hTR and TP1 subunits may be potentially good markers of endogenous RNA control. Endometrial dating was determined from the pathomorphology of the endometrium and classified into normal proliferative endometrium, endometrial hyperplasia (simple, complex, and atypical), and endometrial adenocarcinoma. The analysis of the expression of the hTERT, TP1, and hTR telomerase subunits was performed by a quantitative polymerase chain reaction method, based on fluorescent TaqMan methodology (ABI Prism 7 700 Sequence Detection System) capable of measuring fluorescence in real time. The aim of the study was an analysis of the expression profiles of genes encoding hTR and TP1 telomerase subunits in normal endometrium, endometrial hyperplasia, and adenocarcinoma forthe estimation of the possibility of once application in endogenous RNA control of gene analysis in the endometrium. The nonparametric Mann–Whitney U test and analysis of variance Friedman test were used to evaluate the variation in telomerase subunit mRNA level between normal endometrium, and endometrial hyperplasia and adenocarcinoma. The results confirm the hTR subunit expression as a good marker of endogenous control in quantitative analysis of gene transcription in endometrial tissue. TP1 subunit transcriptions have not been detected constitutively in our study.

scholarly journals Differential regulation of leukocyte function-associated antigen-1/ intercellular adhesion molecules-1-dependent adhesion and aggregation in HL-60 cells

Blood ◽  
1996 ◽  
Vol 87 (10) ◽  
pp. 4276-4285 ◽  
Author(s):  
K Katagiri ◽  
T Kinashi ◽  
S Irie ◽  
T Katagiri
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Transforming Growth Factor ◽  
De Novo ◽  
Active Form ◽  
Intercellular Adhesion ◽  
Cytoskeletal Proteins ◽  
Leukocyte Function ◽  
Cellular Aggregation ◽  
Intercellular Adhesion Molecules

Activation of integrin and organization of cytoskeletal proteins are highly regulated in cell adhesion and aggregation. The interaction of leukocyte function-associated antigen-1 (LFA-1) and intercellular adhesion molecules-1 (ICAM-1) mediates cell adhesion and aggregation, which facilitate leukocyte trafficking to inflamed tissues and augment effector functions. We investigated how LFA-1/ICAM-1-mediated adhesion and aggregation are regulated in HL-60 cells induced to differentiate into neutrophils by retinoic acid (RA). Uninduced HL-60 cells did not bind to ICAM-1 even with stimulation by 12–0-tetradecanoyl phorbol-13- acetate, although they express LFA-1 on the cell surface. When cultured with RA for 24 hours, HL-60 cells were able to adhere to ICAM-1 constitutively. The induction of adhesion did not accompany any change in surface density of LFA-1, indicating that the avidity of LFA-1 was increased. The change in its avidity required de novo synthesis of proteins. Although ICAM-1 was intensely expressed on RA-induced HL-60 cells, these cells did not show any cellular aggregation. The HL-60 cells transfected with the active form of Ras (Val12) exhibited LFA- 1/ICAM-1-dependent aggregation by RA stimulation without change in the avidity of LFA-1. In these Ras-transfectants, a cytoskeletal protein, paxillin, was tyrosine-phosphorylated, and the level of F-actin increased. Transforming growth factor (TGF) beta, as well as cytochalasin D, prevented both the tyrosine phosphorylation of paxillin and the aggregation without any effects on the avidity of LFA-1. Thus, an increase in the avidity of LFA-1 was not sufficient for the induction of aggregation, which required activation of Ras and reorganization of cytoskeletal proteins. These results suggest that distinct regulatory mechanisms control LFA-1/ICAM-1-dependent adhesion and aggregation in HL-60 cells differentiating into neutrophils.

Attenuated expression of epithelial cell adhesion molecules in murine polycystic kidney disease

1992 ◽  
Vol 262 (4) ◽  
pp. F679-F686 ◽  
Author(s):  
M. V. Rocco ◽  
E. G. Neilson ◽  
J. R. Hoyer ◽  
F. N. Ziyadeh
Keyword(s):  
Cell Adhesion ◽  
Growth Factors ◽  
Kidney Disease ◽  
Adhesion Molecules ◽  
Polycystic Kidney Disease ◽  
Cell Adhesion Molecules ◽  
Structural Proteins ◽  
Polycystic Kidney ◽  
Cystic Kidneys ◽  
E Cadherin

Polycystic kidney disease is an inherited disorder of parenchymal structure that leads to renal failure. Cysts begin as focal dilations in proximal tubules and collecting ducts, giving rise to cyst walls lined by a phenotypically disturbed epithelium that expresses dysfunctional transport and matrix proteins. We used an mRNA search protocol to probe efficiently for tissue-specific disturbances that might underlie the formation of cysts. This search assessed the relative abundance of transcripts encoding a variety of growth factors (transforming growth factor-beta 1, interleukin-6, tumor necrosis factor, and endothelin-1), structural proteins (collagen IV, nidogen, fibronectin, and laminins A and B1), and cell adhesion molecules (CAMs; E-cadherin, N-CAM, laminin receptor, and fibronectin receptor) in the cystic kidneys of cpk/cpk mice and uncovered a previously unrecognized early reduction in mRNA encoding N-CAM (54%) and E-cadherin (56%) (n = 5; P less than 0.001). Levels of transcripts for growth factors, structural proteins, and for fibronectin and laminin receptors in normal and cystic kidneys were generally similar. The reduction in transcripts for N-CAM and E-cadherin in kidneys from cystic mice was not observed in autologous liver. The immunofluorescent staining of cystic kidneys confirmed that the decrease in N-CAM and E-cadherin was generally confined to regions abundant in developing cystic epithelium. The presence of both N-CAM and E-cadherin appears to guide the sequential differentiation and polarization of normal renal epithelium, and their attenuated expression in the kidney of cpk/cpk mice may be a material factor contributing to the pathogenesis of cyst formation.

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