Vasoactive intestinal peptide (VIP) induces transactivation of EGFR and HER2 in human breast cancer cells

Valdehíta, Ana; Bajo, Ana M.; Schally, Andrew V.; Varga, József; Carmena, Marı́a J.; Prieto, Juan Carlos

doi:10.1016/j.mce.2008.11.024

Cited by 54 publications

(34 citation statements)

References 39 publications

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“…Interestingly, VIP and PACAP analogs have been shown to affect tumor growth in in vitro and in vivo animal tumor models, suggesting that these receptors could be used as novel therapeutic targets or for localization of tumors [116][117][118][119] . The effect of VIP varies with the type of tumor, by either directly promoting tumor growth [76,[120][121][122] , suppressing growth [123] , or promoting its differentiation through VPAC1 receptor signaling [124,125] . More recently, VIP has been shown to modulate tumor cell migration [125] .…”

Section: Resultsmentioning

confidence: 99%

“…However, the role of the VIP signaling pathway in human leukemia is unknown, and only a few in vitro studies have examined the role of this signaling pathway in the survival of leukemic blasts [126] . VIP has been shown to modulate EGFR/HER2 [120] , VEGF [127,128] , FOS expression [48] in breast cancer cell lines. These findings further underscore the importance of this signaling pathway in human cancer and warrants further investigation.…”

Section: Resultsmentioning

confidence: 99%

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Vasoactive intestinal peptide signaling axis in human leukemia

Dorsam

Benton²,

Failing³

et al. 2011

WJBC

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The vasoactive intestinal peptide (VIP) signaling axis constitutes a master "communication coordinator" between cells of the nervous and immune systems. To date, VIP and its two main receptors expressed in T lymphocytes, vasoactive intestinal peptide receptor (VPAC)1 and VPAC2, mediate critical cellular functions regulating adaptive immunity, including arresting CD4 T cells in G1 of the cell cycle, protection from apoptosis and a potent chemotactic recruiter of T cells to the mucosa associated lymphoid compartment of the gastrointestinal tissues. Since the discovery of VIP in 1970, followed by the cloning of VPAC1 and VPAC2 in the early 1990s, this signaling axis has been associated with common human cancers, including leukemia. This review highlights the present day knowledge of the VIP ligand and its receptor expression profile in T cell leukemia and cell lines. Also, there will be a discussion describing how the anti-leukemic DNA binding transcription factor, Ikaros, regulates VIP receptor expression in primary human CD4 T lymphocytes and T cell lymphoblastic cell lines (e.g. Hut-78). Lastly, future goals will be mentioned that are expected to uncover the role of how the VIP signaling axis contributes to human leukemogenesis, and to establish whether the VIP receptor signature expressed by leukemic blasts can provide therapeutic and/or diagnostic information.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Vasoactive intestinal peptide signaling axis in human leukemia

Dorsam

Benton²,

Failing³

et al. 2011

WJBC

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“…In contrast, VPAC1 mediated the transactivation of the EGFR and HER2 in breast cancer cells (Valdehita et al, 2009(Valdehita et al, , 2012. HER2 has an inactive ligand binding domain but functional tyrosine kinase domain and hence it can be phosphorylated when it forms heterodimers with the EGFR (Bhola and Grandis, 2008).…”

Section: Addition Colony Numbermentioning

confidence: 99%

“…HER2 has an inactive ligand binding domain but functional tyrosine kinase domain and hence it can be phosphorylated when it forms heterodimers with the EGFR (Bhola and Grandis, 2008). The addition of 100 nM VIP to T47D breast cancer cells rapidly increased HER2 tyrosine phosphorylation after 1 min; however, it took 15 min to maximally increase tyrosine phosphorylation of the EGFR (Valdehita et al, 2009). In contrast, using lung cancer cells PAC1 maximally increased EGFR tyrosine phosphorylation after 1 min, whereas VIP had no effect.…”

Section: Addition Colony Numbermentioning

confidence: 99%

Pituitary Adenylate Cyclase-Activating Polypeptide Causes Tyrosine Phosphorylation of the Epidermal Growth Factor Receptor in Lung Cancer Cells

Moody

Osefo²,

Nuche-Berenguer³

et al. 2012

J Pharmacol Exp Ther

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Pituitary adenylate cyclase-activating polypeptide (PACAP) is an autocrine growth factor for some lung cancer cells. The activated PACAP receptor (PAC1) causes phosphatidylinositol turnover, elevates cAMP, and increases the proliferation of lung cancer cells. PAC1 and epidermal growth factor receptor (EGFR) are present in non-small-cell lung cancer (NSCLC) cells, and the growth of NSCLC cells is inhibited by the PAC1 antagonist PACAP(6 -38) and the EGFR tyrosine kinase inhibitor gefitinib. Here, the ability of PACAP to transactivate the EGFR was investigated. Western blot analysis indicated that the addition of PACAP but not the structurally related vasoactive intestinal peptide increased EGFR tyrosine phosphorylation in NCI-H838 or H345 cells. PACAP-27, in a concentration-dependent manner, increased EGFR transactivation 4-fold 2 min after addition to NCI-H838 cells. The ability of 100 nM PACAP-27 to increase EGFR or extracellular signal-regulated kinase tyrosine phosphorylation in NCI-H838 cells was inhibited by PACAP(6 -38), gefitinib, 4-amino-5-(4-chlorophenyl)-7-(dimethylethyl)pyrazolo [3,4-d] -[2-[[3-(4-bromophenyl)-2-propenyl]amino-]ethyl]-5-isoquinolinesulfonamide (H89; protein kinase A inhibitor). PACAP addition to NCI-H838 cells significantly increased reactive oxygen species, and the increase was inhibited by tiron. The results indicate that PACAP causes transactivation of the EGFR in NSCLC cells in an oxygen-dependent manner that involves phospholipase C but not protein kinase A.

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“…Note VIP addition to breast cancer cells causes transactivation of the EGF receptor and HER2 (Valdehita et al, 2009). Addition of VIPcamptothecin conjugates causes apoptosis of breast cancer cells .…”

Section: Breast Cancermentioning

confidence: 99%

VIP (vasoactive intestinal peptide)

Moody¹

2014

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Review on VIP, with data on DNA/RNA, on the protein encoded and where the gene is implicated. IdentityOther names: PHM27 HGNC (Hugo): VIP Location: 6q25.2 Local order: The VIP gene has 7 exons. Note: VIP is a secreted protein which binds to membrane G-protein coupled receptors (GPCR) increasing intracellular cAMP signaling. DNA/RNA NoteThe human VIP gene encodes 7 exons and is localized to chromosome 6q25.2 (Fahrenkrug, 2010). DescriptionThe VIP gene spans 8837 bp. TranscriptionThe gene transcript has 1601 bp. ProteinDescription Said and Mutt (1970) sequenced an acid extractable peptide from the porcine duodenum which decreased systemic arterial pressure and increased heart rate, stroke volume, mesenteric and femoral blood flow in the dog. The 27 amino acid peptide was named vasoactive intestinal peptide (VIP). VIP is metabolized (Bodner et al., 1985) from a 170 amino acid precursor protein (preproVIP).

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Vasoactive intestinal peptide (VIP) induces transactivation of EGFR and HER2 in human breast cancer cells

Cited by 54 publications

References 39 publications

Vasoactive intestinal peptide signaling axis in human leukemia

Vasoactive intestinal peptide signaling axis in human leukemia

Pituitary Adenylate Cyclase-Activating Polypeptide Causes Tyrosine Phosphorylation of the Epidermal Growth Factor Receptor in Lung Cancer Cells

VIP (vasoactive intestinal peptide)

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