Role of heregulin in human cancer

Breuleux, Madlaina

doi:10.1007/s00018-007-7120-0

Cited by 83 publications

(83 citation statements)

References 201 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several recent comprehensive reviews of NRGs are available. [81][82][83] Alpha and β isoforms utilize different exons for the EGF-like domain. The relative effects of the NRGs on ERBBs appear to relate in part to the cells under study and the type of assay.…”

Section: Erbb3 Interacting Proteins: Activation Signaling and Regulamentioning

confidence: 99%

The ERBB3 receptor in cancer and cancer gene therapy

2008

View full text Add to dashboard Cite

ERBB3, a member of the epidermal growth factor receptor (EGFR) family, is unique in that its tyrosine kinase domain is functionally defective. It is activated by neuregulins, by other ERBB and nonERBB receptors as well as by other kinases, and by novel mechanisms. Downstream it interacts prominently with the phosphoinositol 3-kinase/AKT survival/mitogenic pathway, but also with GRB, SHC, SRC, ABL, rasGAP, SYK and the transcription regulator EBP1. There are likely important but poorly understood roles for nuclear localization and for secreted isoforms. Studies of ERBB3 expression in primary cancers and of its mechanistic contributions in cultured cells have implicated it, with varying degrees of certainty, with causation or sustenance of cancers of the breast, ovary, prostate, certain brain cells, retina, melanocytes, colon, pancreas, stomach, oral cavity and lung. Recent results link high ERBB3 activity with escape from therapy targeting other ERBBs in lung and breast cancers. Thus a wide and centrally important role for ERBB3 in cancer is becoming increasingly apparent. Several approaches for targeting ERBB3 in cancers have been tested or proposed. Small inhibitory RNA (siRNA) to ERBB3 or AKT is showing promise as a therapeutic approach to treatment of lung adenocarcinoma.

show abstract

Section: Erbb3 Interacting Proteins: Activation Signaling and Regulamentioning

confidence: 99%

The ERBB3 receptor in cancer and cancer gene therapy

2008

View full text Add to dashboard Cite

show abstract

“…8c). Several isoforms of hrg2 exist [29,30] and the mol. wt of full length hrg2 is expected to be approximately 85 kDa.…”

Section: Expression Of the Erbb Ligandsmentioning

confidence: 99%

Activation of ErbB3, EGFR and Erk is essential for growth of human breast cancer cell lines with acquired resistance to fulvestrant

Frogne

Benjaminsen

Sonne-Hansen

et al. 2008

Breast Cancer Res Treat

135

106

View full text Add to dashboard Cite

show abstract

“…Increasing evidence indicates that NRGs may have a relevant role in cancer. Thus, expression of NRGs has been described in several tumour types (Breuleux, 2007;Montero et al, 2008), and has been linked to the response to trastuzumab in breast cancer (Yuste et al, 2005;de Alava et al, 2007). In addition, expression of transmembrane NRGs in breast cancer cells activates ErbB2/ HER2, and favours their proliferation in vitro (Yuste et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

P-Rex1 participates in Neuregulin-ErbB signal transduction and its expression correlates with patient outcome in breast cancer

et al. 2010

View full text Add to dashboard Cite

The Neuregulins and their receptors, the ErbB/HER subfamily of receptor tyrosine kinases, have critical roles in animal physiology, and their deregulation is frequent in cancer. Here we report the identification of the guanine nucleotide exchange factor, phosphatidylinositol 3,4,5-triphosphate-dependent Rac exchanger 1 (P-Rex1), as a novel mediator in signalling by ErbB/HER receptors. P-Rex1 was formerly described as a phosphoinositide 3-kinase and Gbc activated protein that regulates Rac function. We define how ErbB/HER receptors regulate P-Rex1 function, which involves dephosphorylation of inhibitory residues, and phosphorylation of activating residues of P-Rex. The net balance resulting from activation of this phosphorylation/dephosphorylation cycle of P-Rex1 favours Rac activation. Molecular and biological studies indicated that P-Rex1 phosphorylation regulated the proliferation of breast cancer cells, and P-Rex1 knockdown affected their migration or invasiveness, as well as their in vivo tumourigenic potential. Moreover, as we found correlation between high P-Rex1 expression and poor patient outcome in breast cancer, P-Rex1 targeting may be therapeutically relevant in cancer.

show abstract

Role of heregulin in human cancer

Cited by 83 publications

References 201 publications

The ERBB3 receptor in cancer and cancer gene therapy

The ERBB3 receptor in cancer and cancer gene therapy

Activation of ErbB3, EGFR and Erk is essential for growth of human breast cancer cell lines with acquired resistance to fulvestrant

P-Rex1 participates in Neuregulin-ErbB signal transduction and its expression correlates with patient outcome in breast cancer

Contact Info

Product

Resources

About