Expression of a Kinase-DefectiveEph-like Receptor in the Normal Human Brain

Matsuoka, Hiroshi; Iwata, Nobuko; Ito, Mitsuhiro; Shimoyama, Manabu; Nagata, Aki; Chihara, Kazuo; Takai, Setsuo; Matsui, Toshimitsu

doi:10.1006/bbrc.1997.6812

Cited by 56 publications

(67 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our preliminary study demonstrated that the EphB6 transcript was not detectable in MDA-MB-231, an invasive breast carcinoma cell line (Fox and Kandpal, 2004). The EphB6 cDNA was first cloned from normal human brain RNA and its protein product has since been shown to be involved in T-cell function (Matsuoka et al, 1997;Luo et al, 2001;Freywald et al, 2003). EphB6, although kinase deficient, is a target for phosphorylation by EphB1 following stimulation with ephrinB1 or ephrinB2 (Munthe et al, 2000;Freywald et al, 2002;Matsuoka et al, 2005).…”

Section: Introductionmentioning

confidence: 92%

EphB6 receptor significantly alters invasiveness and other phenotypic characteristics of human breast carcinoma cells

Fox

Kandpal

2009

Oncogene

View full text Add to dashboard Cite

Breast cancer mortality in women is largely attributed to the metastasis of primary breast tumors. We have analysed the function of EphB6, a kinase-deficient receptor, in the invasive phenotype of breast cancer cell lines. We have demonstrated the loss of EphB6 protein in invasive breast carcinoma cell lines and absence of EphB6 transcript in a metastatic breast tumor specimen. The function of EphB6 in invasiveness was confirmed by the ability of EphB6 protein to decrease the in vitro invasiveness of MDA-MB-231, MDA-MB-435 and BT549 cells transfected with an EphB6 expression construct. In MDA-MB-231 cells, the decreased invasiveness appeared to be mediated by decreased transcript levels of matrix metalloproteinase (MMP)7 and MMP19, and increased transcript levels of tissue inhibitors of metalloproteinase 2. In addition to affecting invasiveness phenotype, EphB6 overexpression was also responsible for altering the growth rate and colony-forming efficiency of MCF-7 and MDA-MB-231 cells in a cell-line-specific manner. We suggest that the significant decrease in the invasiveness of MDA-MB-231 and other cell lines transfected with EphB6 is likely occurring by the ability of EphB6 to transduce signals to the nucleus and altering relevant gene expression.

show abstract

Section: Introductionmentioning

confidence: 92%

EphB6 receptor significantly alters invasiveness and other phenotypic characteristics of human breast carcinoma cells

Fox

Kandpal

2009

Oncogene

View full text Add to dashboard Cite

show abstract

“…2J-L). The kinase-dead ephrinB2 receptor, EphB6, is expressed at very low levels in lung (Matsuoka et al, 1997) …”

Section: Expression Of Ephb Receptors and Ephrinb Ligands In The Lungmentioning

confidence: 99%

Role for ephrinB2 in postnatal lung alveolar development and elastic matrix integrity

Wilkinson

Schittny

Reinhardt

et al. 2008

Developmental Dynamics

View full text Add to dashboard Cite

Alveoli are formed in the lung by the insertion of secondary tissue folds, termed septa, which are subsequently remodeled to form the mature alveolar wall. Secondary septation requires interplay between three cell types: endothelial cells forming capillaries, contractile interstitial myofibroblasts, and epithelial cells. Here, we report that postnatal lung alveolization critically requires ephrinB2, a ligand for Eph receptor tyrosine kinases expressed by the microvasculature. Mice homozygous for the hypomorphic knockin allele ephrinB2 ⌬V/⌬V , encoding mutant ephrinB2 with a disrupted C-terminal PDZ interaction motif, show severe postnatal lung defects including an almost complete absence of lung alveoli and abnormal and disorganized elastic matrix. Lung alveolar formation is not sensitive to loss of ephrinB2 cytoplasmic tyrosine phosphorylation sites. Postnatal day 1 mutant lungs show extracellular matrix alterations without differences in proportions of major distal cell populations. We conclude that lung alveolar formation relies on endothelial ephrinB2 function. Developmental Dynamics 237:2220 -2234, 2008.

show abstract

“…Lymphocyte surface molecules are essential for cell-cell and cell-environment communications. Thus, receptor tyrosine kinases (RTKs) 3 bear dual importance in lymphocyte function. Eph RTKs are the largest family of RTKs, comprising ϳ25% of the known RTKs; they are now named EphAs (EphA1 to EphA8) and EphBs (EphB1 to EphB6) according to their sequence homology (1).…”

mentioning

confidence: 99%

“…Eph RTKs are the largest family of RTKs, comprising ϳ25% of the known RTKs; they are now named EphAs (EphA1 to EphA8) and EphBs (EphB1 to EphB6) according to their sequence homology (1). At the protein level, EphB6 shares ϳ47-60% homology with other members of EphB subgroups (2,3), whereas homology between human and mouse EphB6 is as high as 91.1% (2,3). Such a high degree of homology suggests important conserved functions of this molecule.…”

mentioning

confidence: 99%

“…A few Eph RTK members, such as EphB6 and EphB4, have high levels of expression in hemopoietic cells and in the thymus (2,3). However, despite their expression in these tissues and their presumed importance as both cell surface receptors and tyrosine kinases, we have no knowledge as to the function of any member of this important RTK family in the immune system.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Cross-Linking of EphB6 Resulting in Signal Transduction and Apoptosis in Jurkat Cells

Luo

Wan

et al. 2001

The Journal of Immunology

View full text Add to dashboard Cite

Eph kinases are the largest family of receptor tyrosine kinases (RTK), and their ligands are cell surface molecules. The known functions of Eph kinases are mainly pattern formation in the CNS. Although several Eph kinases are expressed at high levels in hemopoietic cells and in the thymus, we have no knowledge of the functions of any Eph kinase in the immune system. In this study, we have demonstrated that an Eph kinase, EphB6, was expressed at high levels in Jurkat leukemic T cells. Co-cross-linking of EphB6 and CD3 led to an altered profile of lymphokine secretion along with proliferation inhibition of Jurkat cells. The cells subsequently underwent Fas-mediated apoptosis. Although EphB6 has no intrinsic kinase activity, its cross-linking triggered general protein tyrosine phosphorylation in Jurkat cells. EphB6 was found to associate with a number of molecules in the signaling pathways, notably Cbl. EphB6 cross-linking resulted in Cbl dephosphorylation and dissociation from Src homology 2 domain-containing tyrosine phosphatase-1 (SHP-1). Our results show that EphB6 has important functions in T cells, and it can transduce signals into the cells via proteins it associates with.

show abstract

Expression of a Kinase-DefectiveEph-like Receptor in the Normal Human Brain

Cited by 56 publications

References 23 publications

EphB6 receptor significantly alters invasiveness and other phenotypic characteristics of human breast carcinoma cells

EphB6 receptor significantly alters invasiveness and other phenotypic characteristics of human breast carcinoma cells

Role for ephrinB2 in postnatal lung alveolar development and elastic matrix integrity

Cross-Linking of EphB6 Resulting in Signal Transduction and Apoptosis in Jurkat Cells

Contact Info

Product

Resources

About