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HER2
Receptor tyrosine-protein kinase erbB-2 is a protein that normally resides in the membranes of cells and is encoded by the ERBB2 gene. ERBB is abbreviated from erythroblastic oncogene B, a gene originally isolated from the avian genome. The human protein is also frequently referred to as HER2 (human epidermal growth factor receptor 2) or CD340 (cluster of differentiation 340).
HER2 is a member of the human epidermal growth factor receptor (HER/EGFR/ERBB) family. But contrary to other members of the ERBB family, HER2 does not directly bind ligand. HER2 activation results from heterodimerization with another ERBB member or by homodimerization when HER2 concentration are high, for instance in cancer. Amplification or over-expression of this oncogene has been shown to play an important role in the development and progression of certain aggressive types of breast cancer. In recent years the protein has become an important biomarker and target of therapy for approximately 30% of breast cancer patients.
HER2 is named as such due to structural similarities with human epidermal growth factor receptor 1, or HER1.
The Neu alias of HER2 derives its name from the parent glioblastoma cell line - a type of neural tumor found in rodents.
ErbB-2 was named for its similarity to avian erythroblastosis oncogene B, ErbB; the oncogene later shown to code for epidermal growth factor receptor, EGFR.
Molecular cloning of EGFR discovered that HER2, Neu, and ErbB-2 are all encoded by the same orthologs.
ERBB2, a known proto-oncogene, is located at the long arm of human chromosome 17 (17q12).
The ErbB family consists of four individual plasma membrane-bound receptor tyrosine kinases. One of which is erbB-2, and the other members being erbB-1, erbB-3 (neuregulin-binding; lacks kinase domain), and erbB-4. All four contain an extracellular ligand binding domain, a transmembrane domain, and an intracellular domain that can interact with a multitude of signaling molecules and exhibit both ligand-dependent and ligand-independent activity. Notably, no ligands for HER2 have yet been identified. HER2 can heterodimerise with any of the other three receptors and is considered to be the preferred dimerisation partner of the other ErbB receptors.
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HER2
Receptor tyrosine-protein kinase erbB-2 is a protein that normally resides in the membranes of cells and is encoded by the ERBB2 gene. ERBB is abbreviated from erythroblastic oncogene B, a gene originally isolated from the avian genome. The human protein is also frequently referred to as HER2 (human epidermal growth factor receptor 2) or CD340 (cluster of differentiation 340).
HER2 is a member of the human epidermal growth factor receptor (HER/EGFR/ERBB) family. But contrary to other members of the ERBB family, HER2 does not directly bind ligand. HER2 activation results from heterodimerization with another ERBB member or by homodimerization when HER2 concentration are high, for instance in cancer. Amplification or over-expression of this oncogene has been shown to play an important role in the development and progression of certain aggressive types of breast cancer. In recent years the protein has become an important biomarker and target of therapy for approximately 30% of breast cancer patients.
HER2 is named as such due to structural similarities with human epidermal growth factor receptor 1, or HER1.
The Neu alias of HER2 derives its name from the parent glioblastoma cell line - a type of neural tumor found in rodents.
ErbB-2 was named for its similarity to avian erythroblastosis oncogene B, ErbB; the oncogene later shown to code for epidermal growth factor receptor, EGFR.
Molecular cloning of EGFR discovered that HER2, Neu, and ErbB-2 are all encoded by the same orthologs.
ERBB2, a known proto-oncogene, is located at the long arm of human chromosome 17 (17q12).
The ErbB family consists of four individual plasma membrane-bound receptor tyrosine kinases. One of which is erbB-2, and the other members being erbB-1, erbB-3 (neuregulin-binding; lacks kinase domain), and erbB-4. All four contain an extracellular ligand binding domain, a transmembrane domain, and an intracellular domain that can interact with a multitude of signaling molecules and exhibit both ligand-dependent and ligand-independent activity. Notably, no ligands for HER2 have yet been identified. HER2 can heterodimerise with any of the other three receptors and is considered to be the preferred dimerisation partner of the other ErbB receptors.