CELL ADHESION MOLECULES: Implications for a Molecular Histology

Edelman, Gerald M.; Crossin, Kathryn L.

doi:10.1146/annurev.bi.60.070191.001103

Cited by 684 publications

(300 citation statements)

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“…This domain architecture is also found in adhesion molecules of the cadherin-and immunoglobulin superfamily and in receptor protein tyrosine phosphatases such as LAR or PTPm and PTPk (Edelmann and Crossin, 1991;Fischer et al, 1991;Charbonneau and Tonks, 1992). In addition, unique sequences within the kinase domain distinguish axl and its related kinases (sky and mer) from other type I RTKs.…”

Section: Introductionmentioning

confidence: 88%

Determinants for transformation induced by the Axl receptor tyrosine kinase

et al. 1998

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The Axl receptor tyrosine kinase is a transforming oncogene in NIH3T3 cells. In order to de®ne structural requirements of the Axl receptor necessary for transformation we passaged recombinant retroviruses carrying the axl cDNA in NIH3T3 cells, generating randomly mutated axl variants. Using this strategy, we have isolated three axl viral strains (1B1, SV8, and FFa4) that show augmented 3T3 cell transforming capacity associated with elevated p140 Axl . Upon sequencing, the 1B1 and SV8 proviruses possessed only silent mutations, making p140 Axl overexpression the most likely explanation for their increased transformation activity. However, the characterization of FFa4 revealed a deletion of sequences encoding the carboxy-terminal 45 amino acids leading to the generation of a chimeric transcript comprised of a truncated Axl receptor with a segment of the 3' UTR region. Mutational analysis revealed that the transforming activity of FFa4 was speci®c to the formation of the chimeric receptor rather than to the carboxyl-terminal truncation. Intriguingly, none of the viral strains were able to transform the murine cell lines NR-6 and 32D despite equivalent expression of surface p140 Axl protein. Further analysis showed that Axl's transforming potential is dependent on the host cell type, the presence of a putative pp190 as a facilitator for transformation, and the level of p140 Axl expression. Taken together, these results underscore the complexity of Axl biology which is dependent on receptor stoichiometry and the cellular background.

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Section: Introductionmentioning

confidence: 88%

Determinants for transformation induced by the Axl receptor tyrosine kinase

et al. 1998

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“…In addition to their role in inflammation, cell adhesion molecules are known regulators of cellcell and cell-matrix interactions that are important for multiple cellular functions of stem cells, including proliferation, differentiation, and migration (60). In bone, cadherins have been reported to mediate cell-cell interaction through adherens junctions that are important for both bone development and osteoblastic functions (61).…”

Section: Genementioning

confidence: 99%

dlk1/FA1 Regulates the Function of Human Bone Marrow Mesenchymal Stem Cells by Modulating Gene Expression of Pro-inflammatory Cytokines and Immune Response-related Factors

Abdallah

Boissy

Tan

et al. 2007

Journal of Biological Chemistry

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dlk1/FA1 (delta-like 1/fetal antigen-1) is a member of the epidermal growth factor-like homeotic protein family whose expression is known to modulate the differentiation signals of mesenchymal and hematopoietic stem cells in bone marrow. We have demonstrated previously that Dlk1 can maintain the human bone marrow mesenchymal stem cells (hMSC) in an undifferentiated state. To identify the molecular mechanisms underlying these effects, we compared the basal gene expression pattern in Dlk1-overexpressing hMSC cells (hMSC-dlk1) versus control hMSC (negative for Dlk1 expression) by using Affymetrix HG-U133A microarrays. In response to Dlk1 expression, 128 genes were significantly up-regulated (with >2-fold; p < 0.001), and 24% of these genes were annotated as immune response-related factors, including pro-inflammatory cytokines, in addition to factors involved in the complement system, apoptosis, and cell adhesion. Also, addition of purified FA1 to hMSC up-regulated the same factors in a dose-dependent manner. As biological consequences of up-regulating these immune response-related factors, we showed that the inhibitory effects of dlk1 on osteoblast and adipocyte differentiation of hMSC are associated with Dlk1-induced cytokine expression. Furthermore, Dlk1 promoted B cell proliferation, synergized the immune response effects of the bacterial endotoxin lipopolysaccharide on hMSC, and led to marked transactivation of the NF-B. Our data suggest a new role for Dlk1 in regulating the multiple biological functions of hMSC by influencing the composition of their microenvironment "niche." Our findings also demonstrate a role for Dlk1 in mediating the immune response.

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“…The neural cell adhesion molecule, N-CAM, 1 is a member of the immunoglobulin superfamily of cell adhesion molecules that mediate Ca 2ϩ -independent cell-cell adhesion, primarily through homophilic binding (8). In addition, N-CAM has also been shown to interact in a heterophilic way with several cell surface and extracellular binding partners (9), and to transduce cellular signals (10).…”

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confidence: 99%