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Academic literature on the topic 'Cadherins'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 January 2023

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Journal articles on the topic "Cadherins"

1

Klingelhofer, J., R. B. Troyanovsky, O. Y. Laur, and S. Troyanovsky. "Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions." Journal of Cell Science 113, no. 16 (August 15, 2000): 2829–36. http://dx.doi.org/10.1242/jcs.113.16.2829.

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Classic cadherins are transmembrane receptors involved in cell type-specific calcium-dependent intercellular adhesion. The specificity of adhesion is mediated by homophilic interactions between cadherins extending from opposing cell surfaces. In addition, classic cadherins can self-associate forming lateral dimers. Whereas it is widely excepted that lateral dimerization of cadherins is critical for adhesion, details of this process are not known. Yet, no evidence for physical association between different classic cadherins in cells expressing complex cadherin patterns has been reported. To study lateral and adhesive intercadherin interactions, we examined interactions between two classic cadherins, E- and P-cadherins, in epithelial A-431 cells co-producing both proteins. We showed that these cells exhibited heterocomplexes consisting of laterally assembled E- and P-cadherins. These complexes were formed by a mechanism involving Trp(156) of E-cadherin. Removal of calcium ions from the culture medium triggered a novel Trp(156)-independent type of lateral E-cadherin-P-cadherin association. Notably, an antiparallel (adhesive) mode of interaction between these cadherins was negligible. The specificity of adhesive interaction was localized to the amino-terminal (EC1) domain of both cadherins. Thus, EC1 domain of classic cadherins exposes two determinants responsible for nonspecific lateral and cadherin type-specific adhesive dimerization.

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SHIMOYAMA, Yutaka, Gozoh TSUJIMOTO, Masaki KITAJIMA, and Michiya NATORI. "Identification of three human type-II classic cadherins and frequent heterophilic interactions between different subclasses of type-II classic cadherins." Biochemical Journal 349, no. 1 (June 26, 2000): 159–67. http://dx.doi.org/10.1042/bj3490159.

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We identified three novel human type-II classic cadherins, cadherin-7, -9 and -10, by cDNA cloning and sequencing, and confirmed that they interact with catenins and function in cell-cell adhesion as do other classic cadherins. Cell-cell binding activities of the eight human type-II classic cadherins, including the three new molecules, were evaluated by long-term cell-aggregation experiments using mouse L fibroblast clones transfected with the individual cadherins. The experiments indicated that all the type-II cadherins appeared to possess similar binding strength, which was virtually equivalent to that of E-cadherin. We next examined the binding specificities of the type-II cadherins using the mixed cell-aggregation assay. Although all of the type-II cadherins exhibited binding specificities distinct from that of E-cadherin, heterophilic interactions ranging from incomplete to complete were frequently observed among them. The combinations of cadherin-6 and -9, cadherin-7 and -14, cadherin-8 and -11, and cadherin-9 and -10 interacted in a complete manner, and in particular cadherin-7 and -14, and cadherin-8 and -11 showed an indistinguishable binding specificity against other cadherin subclasses, at least in this assay system. Although these data were obtained from an in vitro study, they should be useful for understanding cadherin-mediated mechanisms of development, morphogenesis and cell-cell interactions in vivo.

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Suzuki, S. T. "Protocadherins and diversity of the cadherin superfamily." Journal of Cell Science 109, no. 11 (November 1, 1996): 2609–11. http://dx.doi.org/10.1242/jcs.109.11.2609.

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Recent cadherin studies have revealed that many cadherins and cadherin-related proteins are expressed in various tissues of different multicellular organisms. These proteins are characterized by the multiple repeats of the cadherin motif in their extracellular domains. The members of the cadherin superfamily are divided into two groups: classical cadherin type and protocadherin type. The current cadherins appear to have evolved from a protocadherin type. Recent studies have proved the cell adhesion role of classical cadherins in embryogenesis. In contrast, the biological role of protocadherins is elusive. Circumstantial evidence, however, suggests that protocadherins are involved in a variety of cell-cell interactions. Since protocadherins, and many other new cadherins as well, have unique properties, studies of these cadherins may provide insight into the structure and biological role of the cadherin superfamily.

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Yanagisawa, Masahiro, and Panos Z. Anastasiadis. "p120 catenin is essential for mesenchymal cadherin–mediated regulation of cell motility and invasiveness." Journal of Cell Biology 174, no. 7 (September 18, 2006): 1087–96. http://dx.doi.org/10.1083/jcb.200605022.

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During epithelial tumor progression, the loss of E-cadherin expression and inappropriate expression of mesenchymal cadherins coincide with increased invasiveness. Reexpression experiments have established E-cadherin as an invasion suppressor. However, the mechanism by which E-cadherin suppresses invasiveness and the role of mesenchymal cadherins are poorly understood. We show that both p120 catenin and mesenchymal cadherins are required for the invasiveness of E-cadherin–deficient cells. p120 binding promotes the up-regulation of mesenchymal cadherins and the activation of Rac1, which are essential for cell migration and invasiveness. p120 also promotes invasiveness by inhibiting RhoA activity, independently of cadherin association. Furthermore, association of endogenous p120 with E-cadherin is required for E-cadherin–mediated suppression of invasiveness and is accompanied by a reduction in mesenchymal cadherin levels. The data indicate that p120 acts as a rheostat, promoting a sessile cellular phenotype when associated with E-cadherin or a motile phenotype when associated with mesenchymal cadherins.

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5

Suzuki, S., K. Sano, and H. Tanihara. "Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue." Cell Regulation 2, no. 4 (April 1991): 261–70. http://dx.doi.org/10.1091/mbc.2.4.261.

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To examine the diversity of the cadherin family, we isolated cDNAs from brain and retina cDNA preparations with the aid of polymerase chain reaction. The products obtained included cDNAs for two of three known cadherins as well as eight distinct cDNAs, of which deduced amino acid sequences show significant similarity with the known cadherin sequences. Larger cDNA clones were isolated from human cDNA libraries for six of the eight new molecules. The deduced amino acid sequences show that the overall structure of these molecules is very similar to that of the known cadherins, indicating that these molecules are new members of the cadherin family. We have tentatively designated these cadherins as cadherin-4 through -11. The new molecules, with the exception of cadherin-4, exhibit features that distinguish them as a group from previously cloned cadherins; they may belong to a new subfamily of cadherins. Northern blot analysis showed that most of these cadherins are expressed mainly in brain, although some are expressed in other tissues as well. These findings show that the cadherin family of adhesion molecules is much larger than previously thought, and suggest that the new cadherins may play an important role in cell-cell interactions within the central nervous system.

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Vestal, D. J., and B. Ranscht. "Glycosyl phosphatidylinositol--anchored T-cadherin mediates calcium-dependent, homophilic cell adhesion." Journal of Cell Biology 119, no. 2 (October 15, 1992): 451–61. http://dx.doi.org/10.1083/jcb.119.2.451.

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Cadherins are a family of cell adhesion molecules that exhibit calcium-dependent, homophilic binding. Their function depends on both an HisAlaVal sequence in the first extracellular domain, EC1, and the interaction of a conserved cytoplasmic region with intracellular proteins. T-cadherin is an unusual member of the cadherin family that lacks the HisAlaVal motif and is anchored to the membrane through a glycosyl phosphatidylinositol moiety (Ranscht, B., and M. T. Dours-Zimmermann. 1991. Neuron. 7:391-402). To assay the function of T-cadherin in cell adhesion, we have transfected T-cadherin cDNA into CHO cells. Two proteins, mature T-cadherin and the uncleaved T-cadherin precursor, were produced from T-cadherin cDNA. The T-cadherin proteins differed from classical cadherins in several aspects. First, the uncleaved T-cadherin precursor was expressed, together with mature T-cadherin, on the surface of the transfected cells. Second, in the absence of calcium, T-cadherin was more resistant to proteolytic cleavage than other cadherins. Lastly, in contrast to classical cadherins, T-cadherin was not concentrated into cell-cell contacts between transfected cells in monolayer cultures. In cellular aggregation assays, T-cadherin induced calcium-dependent, homophilic adhesion which was abolished by treatment of T-cadherin-transfected cells with phosphatidylinositol-specific phospholipase C. These results demonstrate that T-cadherin is a functional cadherin that differs in several properties from classical cadherins. The function of T-cadherin in homophilic cell recognition implies that the mechanism of T-cadherin-induced adhesion is distinct from that of classical cadherins.

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Tanihara, H., M. Kido, S. Obata, R. L. Heimark, M. Davidson, T. St John, and S. Suzuki. "Characterization of cadherin-4 and cadherin-5 reveals new aspects of cadherins." Journal of Cell Science 107, no. 6 (June 1, 1994): 1697–704. http://dx.doi.org/10.1242/jcs.107.6.1697.

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Several properties of cadherin-4 and cadherin-5 were characterized by using the cDNA transfection approach. The proteins of both cadherins had a relative molecular mass of about 130 kDa and were present at the cell periphery, especially at cell-cell contact sites. These cadherins were easily digested with trypsin, and Ca2+ protected cadherin-4, but not cadherin-5, from the digestion. In immunoprecipitation, cadherin-4 co-precipitated with two major proteins of 105 kDa and 95 kDa, respectively. The 105 kDa and the 95 kDa proteins are likely to correspond to alpha- and beta-catenins. Cadherin-5 co-precipitated with only one major protein of 95 kDa, but seems to associate with the 105 kDa protein. On the other hand, plakoglobin or gamma-catenin did not co-precipitate well with either cadherin-4 or cadherin-5 in immunoprecipitation, but plakoglobin also appears to associated weakly with these cadherins. Cadherin-4 transfectants aggregated within 30 minutes in a cell aggregation assay, but cadherin-5 transfectants did not aggregate under the same conditions. Furthermore, the transfectants of chimeric cadherin-4 with cadherin-5 cytoplasmic domain showed cell aggregation activity comparable to that of wild-type cadherin-4 transfectants, whereas the transfectants of chimeric cadherin-5 with cadherin-4 cytoplasmic domain did not show appreciable cell aggregation, suggesting that the extracellular domains of cadherins, in conjunction with their cytoplasmic domains, play an important role in cell aggregation activity. These results show that cadherin-4 is very similar to the classical cadherins, whereas cadherin-5 is functionally as well as structurally distinct from classical cadherins.

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Kreft, Bertolt, Dietmar Berndorff, Anja Böttinger, Silvia Finnemann, Doris Wedlich, Michael Hortsch, Rudolf Tauber, and Reinhard Geßner. "LI-Cadherin–mediated Cell–Cell Adhesion Does Not Require Cytoplasmic Interactions." Journal of Cell Biology 136, no. 5 (March 10, 1997): 1109–21. http://dx.doi.org/10.1083/jcb.136.5.1109.

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The adhesive function of classical cadherins depends on the association with cytoplasmic proteins, termed catenins, which serve as a link between cadherins and the actin cytoskeleton. LI-cadherin, a structurally different member of the cadherin family, mediates Ca2+-dependent cell–cell adhesion, although its markedly short cytoplasmic domain exhibits no homology to this highly conserved region of classical cadherins. We now examined whether the adhesive function of LI-cadherin depends on the interaction with catenins, the actin cytoskeleton or other cytoplasmic components. In contrast to classical cadherins, LI-cadherin, when expressed in mouse L cells, was neither associated with catenins nor did it induce an upregulation of β-catenin. Consistent with these findings, LI-cadherin was not resistant to detergent extraction and did not induce a reorganization of the actin cytoskeleton. However, LI-cadherin was still able to mediate Ca2+dependent cell–cell adhesion. To analyze whether this function requires any interaction with proteins other than catenins, a glycosyl phosphatidylinositol–anchored form of LI-cadherin (LI-cadherinGPI) was constructed and expressed in Drosophila S2 cells. The mutant protein was able to induce Ca2+-dependent, homophilic cell–cell adhesion, and its adhesive properties were indistinguishable from those of wild type LI-cadherin. These findings indicate that the adhesive function of LI-cadherin is independent of any interaction with cytoplasmic components, and consequently should not be sensitive to regulatory mechanisms affecting the binding of classical cadherins to catenins and to the cytoskeleton. Thus, we postulate that the adhesive function of LI-cadherin is complementary to that of coexpressed classical cadherins ensuring cell–cell contacts even under conditions that downregulate the function of classical cadherins.

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Strale, Pierre-Olivier, Laurence Duchesne, Grégoire Peyret, Lorraine Montel, Thao Nguyen, Evelyn Png, Robert Tampé, et al. "The formation of ordered nanoclusters controls cadherin anchoring to actin and cell–cell contact fluidity." Journal of Cell Biology 210, no. 2 (July 20, 2015): 333–46. http://dx.doi.org/10.1083/jcb.201410111.

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Oligomerization of cadherins could provide the stability to ensure tissue cohesion. Cadherins mediate cell–cell adhesion by forming trans-interactions. They form cis-interactions whose role could be essential to stabilize intercellular junctions by shifting cadherin clusters from a fluid to an ordered phase. However, no evidence has been provided so far for cadherin oligomerization in cellulo and for its impact on cell–cell contact stability. Visualizing single cadherins within cell membrane at a nanometric resolution, we show that E-cadherins arrange in ordered clusters, providing the first demonstration of the existence of oligomeric cadherins at cell–cell contacts. Studying the consequences of the disruption of the cis-interface, we show that it is not essential for adherens junction formation. Its disruption, however, increased the mobility of junctional E-cadherin. This destabilization strongly affected E-cadherin anchoring to actin and cell–cell rearrangement during collective cell migration, indicating that the formation of oligomeric clusters controls the anchoring of cadherin to actin and cell–cell contact fluidity.

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Takeichi, M. "The cadherins: cell-cell adhesion molecules controlling animal morphogenesis." Development 102, no. 4 (April 1, 1988): 639–55. http://dx.doi.org/10.1242/dev.102.4.639.

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Cadherins are a family of glycoproteins involved in the Ca2+-dependent cell-cell adhesion mechanism which is detected in most kinds of tissues. Inhibition of the cadherin activity with antibodies induces dissociation of cell layers, indicating a fundamental importance of these molecules in maintaining the multicellular structure. Cadherins are divided into subclasses, including E-, N- and P-cadherins. While all subclasses are similar in molecular weight, Ca2+- and protease-sensitivity, each subclass is characterized by a unique tissue distribution pattern and immunological specificity. Analysis of amino acid sequences deduced from cDNA encoding these molecules showed that they are integral membrane proteins of 723–748 amino acids long and share common sequences; similarity in the sequences between subclasses is in a range of 50–60% when compared within a single animal species. L cells, with very little endogenous cadherin activity, transfected with the cadherin cDNA acquired high cadherin-mediated aggregating activity. Their colony morphology was altered by the ectopic expression of cadherins from the dispersed type to the compact type, providing direct evidence for a key role of cadherins in cell-cell adhesion. It has been suggested that cadherins bind cells by their homophilic interactions at the extracellular domain and are associated with actin bundles at the cytoplasmic domain. It appears that each cadherin subclass has binding specificity and this molecular family is involved in selective cell-cell adhesion. In development, the expression of each cadherin subclass is spatiotemporally regulated and associated with a variety of morphogenetic events; e.g. the termination or initiation of expression of a cadherin subclass in a given cell collective is correlated with its segregation from or connection with other cell collectives. Antibodies to cadherins were shown to perturb the morphogenesis of some embryonic organs in vitro. These observations suggest that cadherins play a crucial role in construction of tissues and the whole animal body.

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Dissertations / Theses on the topic "Cadherins"

1

Munro, Sandra Bronwen. "An investigation of the cadherins expressed in mouse thymocytes and testis, utilizing the polymerase chain reaction, identification of two novel cadherins, t1-cadherin and t2-cadherin." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0005/NQ30347.pdf.

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Munro, Sandra Bronwen. "An investigation of the cadherins expressed in mouse thymocytes and testis, utilizing the polymerase chain reaction : identification of two novel cadherins, T1-cadherin and T2-cadherin." Thesis, McGill University, 1996. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=42105.

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The cadherins are calcium-dependent cell adhesion molecules. I have used a polymerase chain reaction (PCR) strategy to identify the cadherins expressed in mouse CD4$ sp+$ CD8$ sp+$ thymocytes and testis. Two novel cadherins (designated T1-cadherin and T2-cadherin) were discovered utilizing this approach. cDNAs containing partial coding regions for T1-cadherin and T2-cadherin were used as molecular probes in Northern blot and in situ hybridization protocols to determine the tissue- and cell-specific expression patterns of T1- and T2-cadherin. A T1-cadherin mRNA transcript of 3 kb was detected in adult mouse testes extracts. An mRNA transcript of 3.5 kb was detected for T2-cadherin in mouse brain and testes extracts. In situ hybridization analysis suggested that T2-cadherin is expressed by the Sertoli cells in the seminiferous epithelium. In addition to T1-cadherin and T2-cadherin, five other cadherins (E-cadherin, N-cadherin, P-cadherin, K-cadherin, and OB-cadherin) were found to be expressed at various stages during testicular development. The relative levels of each testicular cadherin mRNA transcript were determined in fetal, newborn, 7-day-old, 21-day-old, and adult mouse testes by semi-quantitative PCR. N-cadherin mRNA was expressed at all stages of testicular development, with maximal levels being present in the testes of 21-day-old mice. E-cadherin, P-cadherin, K-cadherin, OB-cadherin, and T2-cadherin mRNA transcripts were expressed in the fetal gonad. The testicular levels of these cadherin mRNA transcripts decreased dramatically after birth. Conversely, T1-cadherin mRNA was not detected in the fetal, newborn, and 7-day-old testes, but was present in 21-day-old and adult testes. T1-cadherin levels were 10-fold higher in the testes of adult mice, compared to the levels found in the testes of 21-day-old mice. As well, the N-cadherin, T1-cadherin, and T2-cadherin mRNA levels were examined in the estrogen receptor knockout (ERKO) mouse. T1-cadherin mRNA levels

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Zhang, Wentao. "IQGAP1 knockdown enhances the endothelial barrier in vitro." Morgantown, W. Va. : [West Virginia University Libraries], 2006. https://eidr.wvu.edu/etd/documentdata.eTD?documentid=4740.

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Thesis (Ph. D.)--West Virginia University, 2006.
Title from document title page. Document formatted into pages; contains viii, 114 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 101-114).

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Uglow, Elizabeth. "The role of cadherins in vascular disease." Thesis, University of Bristol, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.268829.

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McEvoy, Katherina Yasmin. "The role of desmosomal cadherins in colorectal tumourigenesis." Thesis, University of Birmingham, 2012. http://etheses.bham.ac.uk//id/eprint/3466/.

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In cancer, loss of intercellular contact contributes to tumour progression and invasion. Desmosomal cadherins are essential constituents of desmosomes – intercellular junctions that confer significant adhesive strength to epithelial tissues and cardiac muscle. Although changes in desmosomal components have been noted in a variety of cancers previously, this investigation has shown for the first time altered desmocollin expression in colorectal cancer. Real-time PCR and western blotting were used to assess desmocollin expression in a series of colorectal cancer and matched normal tissue samples. Loss of desmocollin 2 expression was observed in the cancer samples. In addition, de novo expression of desmocollins 1 and 3, which are not normally expressed in the colon, was observed. Desmoglein gene expression was also altered in the cancer samples. Although classical cadherin switching is a hallmark of the epithelial-mesenchymal transition, desmocollin switching has not previously been reported. Further experiments, to investigate the effect of loss of desmocollin 2 and desmoglein 2 on the behaviour of cultured cells were performed. In addition, experiments were carried out to identify those transcription factors that regulate desmosomal cadherin gene expression in the colon. Transcription factors of the CCAAT/enhancer-binding proteins family act as transcriptional activators of desmosomal cadherin promoters in colonic cells.

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Xu, Mei. "Cellular mechanisms of effects of sphingosine 1-phosphate on vascular endothelial barrier." Morgantown, W. Va. : [West Virginia University Libraries], 2008. https://eidr.wvu.edu/etd/documentdata.eTD?documentid=5586.

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Thesis (Ph. D.)--West Virginia University, 2008.
Title from document title page. Document formatted into pages; contains ix, 109 p. : ill. (some col.). Includes abstract. Includes bibliographical references.

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Chan, Wai-man Vivian. "Functional characterization of liver intestine-cadherin (CDH17) in hepatocellular carcinoma." View the Table of Contents & Abstract, 2006. http://sunzi.lib.hku.hk/hkuto/record/B37424671.

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Pon, Yuen-lam. "Regulation of cadherins and catenins in ovarian surface epithelium and ovarian cancer." Click to view the E-thesis via HKUTO, 2007. http://sunzi.lib.hku.hk/hkuto/record/B39634231.

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Lim, Foon Lian. "Role of cadherin 2 in the intervertebral disc." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2012. http://hdl.handle.net/10722/198869.

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Intervertebral disc (IVD) degeneration could lead to many serious complications including low back pain and disc herniation. However, the mechanism of disc degeneration is not fully understood, hindering the development of the therapeutics to cure this disease. The integrity of the nucleus pulposus (NP), which is derived from the notochord and situated in the core of the IVD, has long been implicated in the function and homeostasis of the IVD. Previous puncture-induced disc degeneration mouse model showed segregation of NP cell mass during the early stage of disc degeneration, indicating that an alteration in the cell adhesion molecule activities is involved in this process. By microarray analysis, our group have revealed specific expression of Cdh2 gene, encoding cadherin 2/N-cadherin, a subtype of cadherins in the NP cells, suggesting a regulatory role of cadherin 2 in the IVD. Cadherins are single transmembrane glycoproteins mediating calcium-dependent intercellular adhesions. Cadherin 2 is involved in chondrogenesis and skeletogenesis, suggesting that it is important in skeletal development and function. This study hypothesized that cadherin 2 is required in the normal IVD development and homeostasis. The purposes of this project is firstly to fully characterize changes in cadherin 2 expression in the normal and degenerative discs in rodent and human, and secondly to examine the effect of loss of function of cadherin 2 on IVD homeostasis by functional blocking of the protein in the rodent NP and conditional knock out of cadherin 2 from the murine NP. The rodent adult NP is similar to human fetal NP, where cadherin 2 is homogeneously expressed in the cell membranes of the notochordal (NC) cells, suggesting that cadherin 2 is a potential NC cell marker. The rodent degenerative NP is similar to human adult NP, where down-regulation of cadherin 2 is observed, the NC cells are replaced by small round cells, and the cell-cell contact is lost. Blocking cadherin 2 function in the rodent NP and conditional knock out of cadherin 2 in the notochord and consequently the NP will lead to transformation of NC cells into small cells, loss of cell-cell contact and a change in the extracellular matrix (ECM), suggesting that cadherin 2 is important in the maintenance of the phenotype and intercellular adhesion of the NC cells. In conclusion, this study indicates that cadherin 2 is mainly expressed in the NC cells of the NP and serves as a potential NC cell marker. It plays a regulatory role in the IVD homeostasis through the maintenance of the NC cell phenotype by intercellular adhesions. This study contributes to the knowledge about the role of cadherin 2 in the disc homeostasis and the early mechanism of disc degeneration, and this would help in developing a therapeutic method to intervene or even reverse the disease process of disc degeneration.
published_or_final_version
Orthopaedics and Traumatology
Doctoral
Doctor of Philosophy

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Modak, Debadrita. "Structural and biochemical studies of non-clustered protocadherins." The Ohio State University, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1595567250446369.

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Books on the topic "Cadherins"

1

Legan, Paul Kevin. The Desmocollin family of adhesion molecules: Desmosomal cadherins showing tissue and differentiation specific patterns of expression. Manchester: University of Manchester, 1993.

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Suzuki, Shintaro T., and Shinji Hirano, eds. The Cadherin Superfamily. Tokyo: Springer Japan, 2016. http://dx.doi.org/10.1007/978-4-431-56033-3.

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Leung, Derek K. M. Transcriptional regulation of E-cadherin in Drosophila melanogaster. Ottawa: National Library of Canada, 2001.

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Hardy, Robert George. Alterations in cadherin and catenin expression in colonic neoplasia, injury and repair: Regulation of p-cadherin transcription in the colon. Birmingham: University of Birmingham, 2003.

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Niewiadomska, Paulina Anna. Function and regulation of E-cadherin in drosophila melanogaster. Ottawa: National Library of Canada, 1998.

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Chase, Maretta. A molecular and genetic analysis of drosophila cadherin DCad87A. Ottawa: National Library of Canada, 2003.

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Jones, Mara. N-cadherin-mediated cell-cell adhesion in the arterial wall. Ottawa: National Library of Canada, 2001.

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Woodfield, Richard John. Investigation of the association of P13K with the cadherin-catenin adhesion complex. Birmingham: University of Birmingham, 2000.

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Webber, P. M. Analysis of the promoter region of the Xenopus borealis N-Cadherin gene. [s.l.]: typescript, 1993.

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Judit T. (Judit Terezia) Zubovits. The role of [beta]-catenin and E-cadherin in skin and gastrointestinal neoplasms. Ottawa: National Library of Canada, 2002.

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Book chapters on the topic "Cadherins"

1

van Roy, Frans. "Cadherins." In Encyclopedia of Signaling Molecules, 627–42. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_39.

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van Roy, Frans. "Cadherins." In Encyclopedia of Signaling Molecules, 1–16. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_39-1.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "Cadherins." In Encyclopedia of Signaling Molecules, 211–24. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_39.

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Hulpiau, Paco, and Frans Roy. "Cadherins." In Encyclopedia of Metalloproteins, 319–32. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_40.

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Gumbiner, Barry M. "Classical Cadherins." In The Cadherin Superfamily, 41–69. Tokyo: Springer Japan, 2016. http://dx.doi.org/10.1007/978-4-431-56033-3_3.

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Chidgey, Martyn, and David Garrod. "Desmosomal Cadherins." In The Cadherin Superfamily, 159–93. Tokyo: Springer Japan, 2016. http://dx.doi.org/10.1007/978-4-431-56033-3_7.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "Classic Cadherins." In Encyclopedia of Signaling Molecules, 409. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100274.

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Katoh, Masaru, Giorgio Berton, Anna Baruzzi, Jennifer Boylston, Charles Brenner, Yong-Hun Lee, William Schiemann, et al. "Flamingo Cadherins." In Encyclopedia of Signaling Molecules, 623. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100452.

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Behrens, Jürgen. "Cadherins/Catenins." In Encyclopedia of Molecular Pharmacology, 1–5. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-21573-6_32-1.

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Behrens, Jürgen. "Cadherins/Catenins." In Encyclopedia of Molecular Pharmacology, 393–98. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-57401-7_32.

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Conference papers on the topic "Cadherins"

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Dallon, John. "Modeling Cell-Cell Adhesion With a Cadherin Based Model." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80108.

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Cell-cell adhesion is critical in morphogenesis, tissue formation, cancer, and wound healing. A better understanding of cell-cell adhesion mediated by cadherins will allow all these processes to be mimicked and manipulated to achieve desired objectives. This paper investigates the role of the actin structure associated with cadherin adhesion sites.

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Sotomayor, Marcos, Wilhelm A. Weihofen, Rachelle Gaudet, David P. Corey, Christopher A. Shera, and Elizabeth S. Olson. "Molecular Mechanics of Tip-Link Cadherins." In WHAT FIRE IS IN MINE EARS: PROGRESS IN AUDITORY BIOMECHANICS: Proceedings of the 11th International Mechanics of Hearing Workshop. AIP, 2011. http://dx.doi.org/10.1063/1.3658062.

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MATSUNAGA, EIJI, KENTA SUZUKI, RYOKO NAKAGAWA, TOHRU KUROTANI, and KAZUO OKANOYA. "DYNAMIC EXPRESSION OF CADHERINS CONTROLS VOCAL LEARNING." In Proceedings of the 9th International Conference (EVOLANG9). WORLD SCIENTIFIC, 2012. http://dx.doi.org/10.1142/9789814401500_0098.

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Sheehan, Stephanie A., Edward P. Retzbach, Yongquan Shen, and Gary S. Goldberg. "Abstract 912A: Cadherins control Src kinase induced fibroblast cell motility." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-912a.

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Hsu, Ya-Ting, Joseph Liu, Peter A. Binkley, Robert S. Schenken, Rajshwar R. Tekmal, Tim H. M. Huang, and Nameer B. Kirma. "Abstract 3326: Parallel EMT pathways mediated by epidermal growth factor, EpCAM and mesenchymal cadherins in benign endometriotic lesions and endometrial cancer." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-3326.

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Shiraishi, Toshihiko, Akinori Ishii, and Shin Morishita. "Effects of Mechanical Vibration on Multilayering of Cultured Osteoblasts." In ASME 2014 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2014. http://dx.doi.org/10.1115/imece2014-37731.

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This paper describes the mechanism of cell proliferation promotion by mechanical vibration focusing on multilayering of cultured osteoblasts. After osteoblasts were cultured under the mechanical vibration of 0.5 G and 12.5 Hz, the saturated cell density reached approximately twice as high as control. In the vibration group, multilayer formation of osteoblasts was observed by fluorescent microscopy in contrast with almost single layer in the control group. Fluorescent staining demonstrated that the expression of N-cadherin, which plays an important role of cell-cell adhesion, was lower under mechanical vibration than control. Therefore, the application of mechanical vibration to osteoblasts can downregulate the expression of N-cadherin, resulting in weakening of cell-cell adhesion and multilayer formation followed by promotion of cell proliferation.

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Arulanandam, Rozanne, Mulu Geletu, Adina Vultur, Jun Cao, Lionel Larue, Helene Feracci, and Leda H. Raptis. "Abstract 991: Cadherin-cadherin engagement promotes cell survival via Rac/Cdc42 and Stat3." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-991.

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Mohamed, Islam, Ahmed Moahmed, Mennatallah Abdelkader, Alaaeldin Saleh, and Ala-Eddin Al-Moustafa. "Elaeagnus Angustifolia: a Promising Medicinal Plant for Cancer Theraby." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2020. http://dx.doi.org/10.29117/quarfe.2020.0124.

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Introduction: Elaeagnus angustifolia (EA) is a medicinal plant that has been used for centuries in treating many human diseases, in the Middle East, including fever, amoebic dysentery, gastrointestinal problems. However, the effect of EA plant extract on human cancer progression especially oral malignancy has not been investigated yet. Thus, first we examined the effect of EA flower extract on angiogenesis in ovo, and on selected parameters in human oral cancer cells. Materials and methods: Chorioallantoic membranes (CAMs) of chicken embryos at 3-7 days of incubation were used to assess the effect EAflower plant extract on angiogenesis. Meanwhile, cell proliferation, soft agar, cell cycle, cell invasion and cell wounding assays were performed to explore the outcome of EA plant extract on FaDu and SCC25 oral cancer cell lines. On the other hand, western blot analysis was carried out to evaluate E-cadherin and Erk1/Erk2 expression and activation, respectively, in FaDu and SCC25 under the effect of EA extract. Results: Our data show that EA extract inhibits cell proliferation and colony formation, in addition to the initiation of Scell cycle arrest and reductionof G1/G2 phases. In parallel, EA extract provokes differentiation to an epithelial phenotype “mesenchymal-epithelial transition: MET” which is the opposite of “epithelial-mesenchymal transition, EMT”: an important event in cell invasion and metastasis. Thus, EA extract causes a dramatic decrease in cell motility and invasion abilities of FaDu and SCC25 cancer cells in comparison with their controls. These changes are accompanied by an up-regulation of E-cadherin expression. The molecular pathway analysis of the EA flower extract reveals that it can inhibit the phosphorylation of Erk1/Erk2, which could be behind the inhibition of angiogenesis, the initiation of MET event and the overexpression of E-cadherin. Conclusions: Our findings indicate that EA plant extract can downgrade human oral cancer progression by the inhibition of angiogenesis and cell invasion via Erk1/Erk2 signaling pathways.

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Quadri, Sadiqa K., Li Sun, and Jahar Bhattacharya. "Cadherin Tethering Determines Endothelial Barrier Properties." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1858.

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Tsuduki, K., H. Nakamura, T. Nakajima, T. Shirahata, S. Tsujimura, S. Yoshida, S. Takahashi, et al. "Genetic Polymorphism of E-Cadherin and COPD." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2999.

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Reports on the topic "Cadherins"

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Wheelock, Margaret. Expression of Inappropriate Cadherins in Human Breast Carcinomas. Fort Belvoir, VA: Defense Technical Information Center, October 2001. http://dx.doi.org/10.21236/ada398154.

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Wheelock, Margaret J. Expression of Inappropriate Cadherins in Human Breast Carcinomas. Fort Belvoir, VA: Defense Technical Information Center, August 2001. http://dx.doi.org/10.21236/ada400268.

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Johnson-Pais, Teresa L. Amplification of Type II Cadherins in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2007. http://dx.doi.org/10.21236/ada496321.

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Johnson-Pais, Teresa L. Amplification of Type II Cadherins in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, November 2009. http://dx.doi.org/10.21236/ada526607.

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Pishvaian, Michael, and Stephen Byers. Vitamin A Regulation of Cadherins in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2000. http://dx.doi.org/10.21236/ada392960.

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Wheelock, Margaret. Expression of Inapproptriate Cadherins in Human Breast Carcinomas. Fort Belvoir, VA: Defense Technical Information Center, August 2000. http://dx.doi.org/10.21236/ada393373.

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Wheelock, Margarat J. Expression of Inappropriate Cadherins in Human Breast Carcinomas. Fort Belvoir, VA: Defense Technical Information Center, August 1999. http://dx.doi.org/10.21236/ada383957.

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Johnson-Pais, Teresa L. Amplification of Type II Cadherins in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, November 2007. http://dx.doi.org/10.21236/ada477448.

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Wheelock, Margaret. Expression of Inappropriate Cadherins in Human Breast Carcinomas-CDA. Fort Belvoir, VA: Defense Technical Information Center, October 1999. http://dx.doi.org/10.21236/ada382945.

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Casal, Ignacio. Metástasis, integrinas y cadherinas RGD. Sociedad Española de Bioquímica y Biología Molecular (SEBBM), November 2016. http://dx.doi.org/10.18567/sebbmdiv_anc.2016.11.1.

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