Laminin activates the p185HER2 oncoprotein and mediates growth inhibition of breast carcinoma cells.

The interaction between laminin and the oncoprotein encoded by the c-erbB-2 oncogene was studied in vitro and in vivo in human breast carcinomas. In vitro analysis of breast carcinoma cell lines overexpressing p185HER2 revealed that laminin, but not fibronectin, induced tyrosine phosphorylation and...

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Main Authors:	Tagliabue, E., Ardini, E., Pellegrini, R., Campiglio, M., Bufalino, R., Jeschke, M., Groner, B., Colnaghi, M. I., Ménard, S.
Format:	Online
Language:	English
Published:	Nature Publishing Group 1996
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2074760/

id	pubmed-2074760
recordtype	oai_dc
spelling	pubmed-20747602009-09-10 Laminin activates the p185HER2 oncoprotein and mediates growth inhibition of breast carcinoma cells. Tagliabue, E. Ardini, E. Pellegrini, R. Campiglio, M. Bufalino, R. Jeschke, M. Groner, B. Colnaghi, M. I. Ménard, S. Research Article The interaction between laminin and the oncoprotein encoded by the c-erbB-2 oncogene was studied in vitro and in vivo in human breast carcinomas. In vitro analysis of breast carcinoma cell lines overexpressing p185HER2 revealed that laminin, but not fibronectin, induced tyrosine phosphorylation and down-modulation of oncoprotein membrane expression. Laminin also specifically inhibited growth of p185HER2-positive cell lines. No direct binding between the recombinant extracellular domain of p185HER2 and laminin was found. Induction of oncoprotein down-modulation by anti-integrin antibodies and coprecipitation of the oncoprotein with the beta 4 integrin subunit indicate that the interaction between p185HER2 and laminin occurs through integrin molecules. The relevance of this in vitro observation was verified in vivo by analysing the prognostic value of p185HER2 overexpression as a function of laminin production on archival paraffin-embedded sections of 887 primary breast tumours. The results revealed an association between p185HER2 overexpression and unfavourable prognosis in tumours negative for laminin production, whereas in laminin-producing tumours, the oncoprotein overexpression was not associated with tumour aggressiveness. Nature Publishing Group 1996-11 /pmc/articles/PMC2074760/ /pubmed/8912540 Text en
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Tagliabue, E. Ardini, E. Pellegrini, R. Campiglio, M. Bufalino, R. Jeschke, M. Groner, B. Colnaghi, M. I. Ménard, S.
spellingShingle	Tagliabue, E. Ardini, E. Pellegrini, R. Campiglio, M. Bufalino, R. Jeschke, M. Groner, B. Colnaghi, M. I. Ménard, S. Laminin activates the p185HER2 oncoprotein and mediates growth inhibition of breast carcinoma cells.
author_facet	Tagliabue, E. Ardini, E. Pellegrini, R. Campiglio, M. Bufalino, R. Jeschke, M. Groner, B. Colnaghi, M. I. Ménard, S.
author_sort	Tagliabue, E.
title	Laminin activates the p185HER2 oncoprotein and mediates growth inhibition of breast carcinoma cells.
title_short	Laminin activates the p185HER2 oncoprotein and mediates growth inhibition of breast carcinoma cells.
title_full	Laminin activates the p185HER2 oncoprotein and mediates growth inhibition of breast carcinoma cells.
title_fullStr	Laminin activates the p185HER2 oncoprotein and mediates growth inhibition of breast carcinoma cells.
title_full_unstemmed	Laminin activates the p185HER2 oncoprotein and mediates growth inhibition of breast carcinoma cells.
title_sort	laminin activates the p185her2 oncoprotein and mediates growth inhibition of breast carcinoma cells.
description	The interaction between laminin and the oncoprotein encoded by the c-erbB-2 oncogene was studied in vitro and in vivo in human breast carcinomas. In vitro analysis of breast carcinoma cell lines overexpressing p185HER2 revealed that laminin, but not fibronectin, induced tyrosine phosphorylation and down-modulation of oncoprotein membrane expression. Laminin also specifically inhibited growth of p185HER2-positive cell lines. No direct binding between the recombinant extracellular domain of p185HER2 and laminin was found. Induction of oncoprotein down-modulation by anti-integrin antibodies and coprecipitation of the oncoprotein with the beta 4 integrin subunit indicate that the interaction between p185HER2 and laminin occurs through integrin molecules. The relevance of this in vitro observation was verified in vivo by analysing the prognostic value of p185HER2 overexpression as a function of laminin production on archival paraffin-embedded sections of 887 primary breast tumours. The results revealed an association between p185HER2 overexpression and unfavourable prognosis in tumours negative for laminin production, whereas in laminin-producing tumours, the oncoprotein overexpression was not associated with tumour aggressiveness.
publisher	Nature Publishing Group
publishDate	1996
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2074760/
_version_	1611407881461039104

Laminin activates the p185HER2 oncoprotein and mediates growth inhibition of breast carcinoma cells.

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