Literature DB >> 7913542

The neu-oncogene: signal transduction pathways, transformation mechanisms and evolving therapies.

W C Dougall1, X Qian, N C Peterson, M J Miller, A Samanta, M I Greene.   

Abstract

A variety of pathways exist to transmit biological signals. One mechanism used for the regulated control of cell growth and differentiation is through the transduction of signals resulting from the binding of soluble polypeptide growth factors to their cognate receptors. The specificity of growth factor action is mediated by the interaction of ligand with cognate receptors which can lead to exquisite control in a tissue- and developmental-specific manner. In addition, individual receptors on the cell surface can form complex assemblies with other receptor/signal transduction molecules that potentially lead to additional levels of signal transmissions. Biological signaling by peptide ligands can be mediated through the enzymatic activation of the receptor resulting in the triggering of a defined biochemical pathway. Ultimately, a mitogenic or differentiation signal is delivered to the nucleus, completing the biological action of the growth factor. The biochemical mechanisms of signal transduction by the p185 neu/c-erbB-2 growth factor receptor and the subsequent physiological responses are the topics of this review. Study of the p185 growth factor receptor has helped to illustrate the functional role of receptor homo- (and hetero-) dimerization in enzyme activation and, in malignant cells, the detrimental results of structural mutations or aberrant gene expression which may effect this dimerization. The ability of one type of growth factor receptor to affect the activity of another (as illustrated by the p185/epidermal growth factor receptor heterodimeric complex) is likely to be a common regulatory feature of growth factor receptor action. The nomenclature to be used in this review will refer to the oncogenic mutated form of the rat protein as 'p185neu', the proto-oncogenic rat protein as 'p185c-neu' and the human form as 'p185c-erbB-2'. The term 'p185' will be used to refer to any type of protein, regardless of the source.

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Year:  1994        PMID: 7913542

Source DB:  PubMed          Journal:  Oncogene        ISSN: 0950-9232            Impact factor:   9.867


  40 in total

1.  Controlling tumor-derived and vascular endothelial cell growth: role of the 4Ff2 cell surface antigen.

Authors:  M Papetti; I M Herman
Journal:  Am J Pathol       Date:  2001-07       Impact factor: 4.307

2.  Structural analysis of p185c-neu and epidermal growth factor receptor tyrosine kinases: oligomerization of kinase domains.

Authors:  R Murali; P J Brennan; T Kieber-Emmons; M I Greene
Journal:  Proc Natl Acad Sci U S A       Date:  1996-06-25       Impact factor: 11.205

3.  Heregulin-beta promotes matrix metalloproteinase-7 expression via HER2-mediated AP-1 activation in MCF-7 cells.

Authors:  Guogang Yuan; Lu Qian; Lun Song; Ming Shi; Dan Li; Ming Yu; Meiru Hu; Beifen Shen; Ning Guo
Journal:  Mol Cell Biochem       Date:  2008-07-04       Impact factor: 3.396

4.  Chromatin modifications sequentially enhance ErbB2 expression in ErbB2-positive breast cancers.

Authors:  Sathish Kumar Mungamuri; William Murk; Luca Grumolato; Emily Bernstein; Stuart A Aaronson
Journal:  Cell Rep       Date:  2013-10-10       Impact factor: 9.423

5.  Antiproliferative and apoptotic activities of ketonucleosides and keto-C-glycosides against non-small-cell lung cancer cells with intrinsic drug resistance.

Authors:  J Paterson; C Uriel; M J Egron; J Herscovici; K Antonakis; M A Alaoui-Jamali
Journal:  Antimicrob Agents Chemother       Date:  1998-04       Impact factor: 5.191

6.  Truncated ErbB2 expressed in tumor cell nuclei contributes to acquired therapeutic resistance to ErbB2 kinase inhibitors.

Authors:  Wenle Xia; Zuguo Liu; Rongrong Zong; Leihua Liu; Sumin Zhao; Sarah S Bacus; Yubin Mao; Jia He; Julia D Wulfkuhle; Emanuel F Petricoin; Takuya Osada; Xiao-Yi Yang; Zachary C Hartman; Timothy M Clay; Kimberly L Blackwell; Herbert K Lyerly; Neil L Spector
Journal:  Mol Cancer Ther       Date:  2011-06-14       Impact factor: 6.261

7.  Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions.

Authors:  R Pinkas-Kramarski; L Soussan; H Waterman; G Levkowitz; I Alroy; L Klapper; S Lavi; R Seger; B J Ratzkin; M Sela; Y Yarden
Journal:  EMBO J       Date:  1996-05-15       Impact factor: 11.598

8.  Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.

Authors:  C L Burke; D F Stern
Journal:  Mol Cell Biol       Date:  1998-09       Impact factor: 4.272

9.  A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor.

Authors:  E Tzahar; H Waterman; X Chen; G Levkowitz; D Karunagaran; S Lavi; B J Ratzkin; Y Yarden
Journal:  Mol Cell Biol       Date:  1996-10       Impact factor: 4.272

10.  Expression of the integrin-linked kinase (ILK) in mouse skin: loss of expression in suprabasal layers of the epidermis and up-regulation by erbB-2.

Authors:  W Xie; F Li; J E Kudlow; C Wu
Journal:  Am J Pathol       Date:  1998-08       Impact factor: 4.307

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