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#29025596   2017/10/13 Save this To Up

RANK and EGFR in invasive breast carcinoma.

Breast cancer is the most common malignancy, affecting one in eight women in North America and Europe. The human epidermal growth factor receptor (EGFR) protein comprises a major determinant of normal development but also cancer. RANK receptor (Receptor Activator of Nuclear factor-κB) is a tumor necrosis superfamily member and a binding partner for RANKL, which was recently implicated in breast cancer initiation, progression and metastasis. Here we provide preliminary evidence of a possible interplay between RANK and EGFR signaling in breast cancer. TCGA (cancergenome.nih.gov) publicly available data for EGFR and TNFRSF11A (RANK) genes from breast cancer patients and breast cancer cell lines were retrieved and analyzed. RANK mRNA showed a statistically significant positive correlation (p <0.001) with the mRNA and protein expression of EGFR, but not with ERBB2/3/4. Further analyses of survival data of a group of breast cancer patients (n = 248) from TCGA, revealed an EGFR(hi)/RANK(hi) subpopulation that showed a statistically significant (p = 0.001) reduced overall survival when compared to EGFR(low)/RANK(low) group of patients. Finally, EGFR and RANK combinatorial in vitro analyses revealed a significant upregulation of AKT and ERK signaling after EGF stimulation in cell lines and also an increase of breast cancer cell invasiveness.

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#28994180   2017/10/10 Save this To Up

A Conjugate of an anti-EGFR VHH and a Cell-penetrating Peptide Drives Receptor Internalization and Blocks EGFR Activation.

Overexpression of (mutated) receptor tyrosine kinases is a characteristic of many aggressive tumors and induction of receptor uptake has long been recognized as a therapeutic modality. A conjugate of a synthetically produced cell penetrating peptide, corresponding to amino acids 38-59 of human lactoferrin, and the recombinant llama single-domain antibody (VHH) 7D12 that binds the human epidermal growth factor receptor (EGFR), was generated via sortase A-mediated transpeptidation. The conjugate blocks EGF-mediated EGFR activation with higher efficacy than both modalities alone, a phenomenon that is caused by both effective receptor blockade and internalization. Thus, the VHH-cell penetrating peptide (VHH-CPP) conjugate shows a combination of activities that implements a highly powerful new design principle to block receptor activation by its clearance from the cell surface.

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#28993723   2017/10/10 Save this To Up

BACE1-Dependent Neuregulin-1 Signaling: An Implication for Schizophrenia.

Schizophrenia is a chronic psychiatric disorder with a lifetime prevalence of about 1% in the general population. Recent studies have shown that Neuregulin-1 (Nrg1) is a candidate gene for schizophrenia. At least 15 alternative splicing of NRG1 isoforms all contain an extracellular epidermal growth factor (EGF)-like domain, which is sufficient for Nrg1 biological activity including the formation of myelin sheaths and the regulation of synaptic plasticity. It is known that Nrg1 can be cleaved by β-secretase (BACE1) and the resulting N-terminal fragment (Nrg1-ntf) binds to receptor tyrosine kinase ErbB4, which activates Nrg1/ErbB4 signaling. While changes in Nrg1 expression levels in schizophrenia still remain controversial, understanding the BACE1-cleaved Nrg1-ntf and Nrg1/ErbB4 signaling in schizophrenia neuropathogenesis is essential and important. In this review paper, we included three major parts: (1) Nrg1 structure and cleavage pattern by BACE1; (2) BACE1-dependent Nrg1 cleavage associated with schizophrenia in human studies; and (3) Animal studies of Nrg1 and BACE1 mutations with behavioral observations. Our review will provide a better understanding of Nrg1 in schizophrenia and a potential strategy for using BACE1 cleavage of Nrg1 as a unique biomarker for diagnosis, as well as a new therapeutic target, of schizophrenia.

1936 related Products with: BACE1-Dependent Neuregulin-1 Signaling: An Implication for Schizophrenia.

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#28993193   2017/10/10 Save this To Up

α-Lipoic acid inhibits human lung cancer cell proliferation through Grb2-mediated EGFR downregulation.

Alpha lipoic acid (α -LA) is a naturally occurring antioxidant and metabolic enzyme co-factor. Recently, α -LA has been reported to inhibit the growth of various cancer cells, but the precise signaling pathways that mediate the effects of α -LA on non-small cell lung cancer (NSCLC) development remain unclear.

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Epidermal Growth Factor ( Epidermal Growth Factor ( T-cell proliferation grad TCHI T cell proliferation TCHI T cell proliferation T-cell proliferation grad TCHII T cell proliferatio TCHII T cell proliferatio Lipoic acid synthetase an Human Phospho-EGFR (Activ Human Mouse Rat Phospho-E Human Phospho-EGFR (Y1068

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#28991210   2017/10/09 Save this To Up

A Central Bioactive Region of LTBP-2 Stimulates the Expression of TGF-β1 in Fibroblasts via Akt and p38 Signalling Pathways.

Latent transforming growth factor-β-1 binding protein-2 (LTBP-2) belongs to the LTBP-fibrillin superfamily of extracellular proteins. Unlike other LTBPs, LTBP-2 does not covalently bind transforming growth factor-β1 (TGF-β1) but appears to be implicated in the regulation of TGF-β1 bioactivity, although the mechanisms are largely unknown. In experiments originally designed to study the displacement of latent TGF-β1 complexes from matrix storage, we found that the addition of exogenous LTBP-2 to cultured human MSU-1.1 fibroblasts caused an increase in TGF-β1 levels in the medium. However, the TGF-β1 increase was due to an upregulation of TGF-β1 expression and secretion rather than a displacement of matrix-stored TGF-β1. The secreted TGF-β1 was mainly in an inactive form, and its concentration peaked around 15 h after addition of LTBP-2. Using a series of recombinant LTBP-2 fragments, the bioactivity was identified to a small region of LTBP-2 consisting of an 8-Cys motif flanked by four epidermal growth factor (EGF)-like repeats. The LTBP-2 stimulation of TGF-β expression involved the phosphorylation of both Akt and p38 mitogen-activated protein kinase (MAPK) signalling proteins, and specific inactivation of each protein individually blocked TGF-β1 increase. The search for the cell surface receptor mediating this LTBP-2 activity proved inconclusive. Inhibitory antibodies to integrins β1 and αVβ5 showed no reduction of LTBP-2 stimulation of TGF-β1. However, TGF-β1 upregulation was partially inhibited by anti-αVβ3 integrin antibodies, suggestive of a direct or indirect role for this integrin. Overall, the study indicates that LTBP-2 can directly upregulate cellular TGF-β1 expression and secretion by interaction with cells via a short central bioactive region. This may be significant in connective tissue disorders involving aberrant TGF-β1 signalling.

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#28982763   2017/10/06 Save this To Up

Integrator orchestrates RAS/ERK1/2 signaling transcriptional programs.

Activating mutations in the mitogen-activated protein kinase (MAPK) cascade, also known as the RAS-MEK-extracellular signal-related kinase (ERK1/2) pathway, are an underlying cause of >70% of human cancers. While great strides have been made toward elucidating the cytoplasmic components of MAPK signaling, the key downstream coactivators that coordinate the transcriptional response have not been fully illustrated. Here, we demonstrate that the MAPK transcriptional response in human cells is funneled through Integrator, an RNA polymerase II-associated complex. Integrator depletion diminishes ERK1/2 transcriptional responsiveness and cellular growth in human cancers harboring activating mutations in MAPK signaling. Pharmacological inhibition of the MAPK pathway abrogates the stimulus-dependent recruitment of Integrator at immediate early genes and their enhancers. Following epidermal growth factor (EGF) stimulation, activated ERK1/2 is recruited to immediate early genes and phosphorylates INTS11, the catalytic subunit of Integrator. Importantly, in contrast to the broad effects of Integrator knockdown on MAPK responsiveness, depletion of a number of critical subunits of the coactivator complex Mediator alters only a few MAPK-responsive genes. Finally, human cancers with activating mutations in the MAPK cascade, rendered resistant to targeted therapies, display diminished growth following depletion of Integrator. We propose Integrator as a crucial transcriptional coactivator in MAPK signaling, which could serve as a downstream therapeutic target for cancer treatment.

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#28978315   2017/10/05 Save this To Up

Resveratrol enhances anticancer effects of paclitaxel in HepG2 human liver cancer cells.

The aim of this in vitro study was to measure the enhanced anticancer effects of Res (resveratrol) on PA (paclitaxel) in HepG2 human liver cancer cells.

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#28974440   2017/10/04 Save this To Up

Hijiki and sodium arsenite stimulate growth of human colorectal adenocarcinoma cells through ERK1/2 activation.

Hijiki seaweed (Hijikia fusiformes) contains high levels of inorganic arsenic, a known carcinogen. However, scientific reports on carcinogenic risks associated with the consumption of this seaweed are limited. This study investigated the effects of seaweed extracts contaminated with arsenic on two colorectal cancer cell lines. Two seaweed extracts, including Hijiki and red seaweed, induced H508 but not HT29 cell proliferation. Growth induction of H508 cells after treatments with Hijiki and sodium arsenite at concentrations equivalent to arsenic found in Hijiki was observed by both MTT and BrdU assays. Hijiki and sodium arsenite induced epidermal growth factor receptor (EGFR) and ERK1/2 activations. AG1478, an EGFR inhibitor, decreased the activation of EGFR and ERK1/2 induced by Hijiki and sodium arsenite. U0126, an ERK1/2 upstream inhibitor, and atropine, a muscarinic acetylcholine receptor (mAChR) antagonist, but not AG1478 completely inhibited the proliferative effect of Hijiki. Altogether, the results suggest that the presence of arsenic in seaweed may partly contribute to the proliferation of colorectal cancer cells. EGFR-dependent, and -independent ERK1/2 signaling pathways, and mAChR may be involved in the growth stimulation by Hijiki. These results raise concern regarding the potential colorectal cancer risks from regular consumption of Hijiki containing high contents of inorganic arsenic.

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Epidermal Growth Factor ( Epidermal Growth Factor ( Growth Differentiation Fa Growth Differentiation Fa Human Transforming Growth Human Vascular Endothelia Human Fibroblast Growth F Human Platelet Derived Gr Human Platelet Derived Gr Human Platelet Derived Gr Human Insulin-like Growth Human Vascular Endothelia

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#28973330   2017/10/03 Save this To Up

Prehematopoietic Stem Cell Transplantation Tear Cytokines as Potential Susceptibility Biomarkers for Ocular Chronic Graft-Versus-Host Disease.

To determine if cytokine tear levels before hematopoietic stem cell transplantation (HSCT) can help anticipate the occurrence of ocular chronic graft-versus-host disease (cGVHD).

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#28972165   2017/10/03 Save this To Up

Surfactant protein A downregulates epidermal growth factor receptor by mechanisms different from those of surfactant protein D.

We recently reported that the lectin surfactant protein D (SP-D) suppresses epidermal growth factor receptor (EGFR) signaling by interfering with ligand-binding to EGFR through an interaction between the carbohydrate recognition domain (CRD) of SP-D and N-glycans of EGFR. Here, we report that surfactant protein A (SP-A) also suppresses EGF signaling in A549 human lung adenocarcinoma cells and in CHOK1 cells stably expressing human EGFR and that SP-A inhibits the proliferation and motility of the A549 cells. Results with (125)I-EGF indicated that SP-A interferes with EGF binding to EGFR, and a ligand blot analysis suggested that SP-A binds EGFR in A549 cells. We also found that SP-A directly binds the recombinant extracellular domain of EGFR (soluble EGFR or sEGFR), and this binding, unlike that of SP-D, was not blocked by EDTA, excess mannose, or PNGase F treatment. We prepared a collagenase-resistant fragment (CRF) of SP-A, consisting of CRD plus the neck domain of SP-A, and observed that CRF directly binds sEGFR, but does not suppress EGF-induced phosphorylation of EGFR in or proliferation of A549 cells. These results indicated that SP-A binds EGFR and downregulates EGF signaling by inhibiting ligand binding to EGFR as well as SP-D. However, unlike for SP-D, SP-A lectin activity and EGFR N-glycans were not involved in the interaction between SP-A and EGFR. Furthermore, our results suggested that oligomerization of SP-A is necessary to suppress the effects of SP-A on EGF signaling.

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