ArticleThe Biochemical journal1999
Signalling-competent truncated forms of ErbB2 in breast cancer cells: differential regulation by protein kinase C and phosphatidylinositol 3-kinase.
Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- ERK5 Interacts with Mitochondrial Glutaminase and Regulates Its Expression.International journal of molecular sciences · 2024Article
- Etiopathogenic role of ERK5 signaling in sarcoma: prognostic and therapeutic implications.Experimental & molecular medicine · 2023Article
- Clinical, genetic and pharmacological data support targeting the MEK5/ERK5 module in lung cancer.NPJ precision oncology · 2021Article
- Proteolytic cleavages in the extracellular domain of receptor tyrosine kinases by membrane-associated serine proteases.Oncotarget · 2017Article
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- Protein kinases C isozymes are differentially expressed in human breast carcinomas.Life sciences · 2009Article
- Trastuzumab in the management of early and advanced stage breast cancer.Biologics : targets & therapy · 2007Article
- The extracellular linker of pro-neuregulin-alpha2c is required for efficient sorting and juxtacrine function.Molecular biology of the cell · 2007Article
- Different mechanisms are implicated in ERBB2 gene overexpression in breast and in other cancers.British journal of cancer · 2003Article
- Erk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2.Molecular and cellular biology · 2002Article
- Stimulation of cleavage of membrane proteins by calmodulin inhibitors.The Biochemical journal · 2000Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alterations that affect the ectodomain of receptor tyrosine kinases are often associated with constitutive activation of the enzymic activity of the mutant cell-associated receptor. Since the ectodomain of the ErbB2 receptor tyrosine kinase has been detected as a soluble fragment in the culture supernatant of cells and serum from patients with advanced breast cancer, the possible presence of cell-associated truncated forms of ErbB2 in cancer cells was investigated. Several cell-bound N-terminal truncated forms of ErbB2 were identified in breast cancer cells overexpressing this receptor. The presence of the truncated fragments was independent of lysosomal/proteasomal activity, indicating that classical receptor tyrosine kinase degradation systems were not involved in the N-terminal cleavages. The presence of these truncated forms of ErbB2 was up-regulated by protein kinase C and neuregulin; and down-regulated by phosphatidylinositol 3-kinase, and monoclonal antibodies that target the ectodomain of ErbB2, indicating that N-terminal cleavages of ErbB2 were regulated by multiple mechanisms. The truncated fragments were tyrosine-phosphorylated under resting conditions, and associated with the signalling intermediates Shc and Grb2. It is therefore likely that these truncated forms may be endowed with constitutive activity that allows them to permanently signal.
Indexed as
Identifiers
10567214PMC1220649W2050728311What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.