ErbB-2 receptor

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In biochemistry, erbB-2 (Human Epidermal growth factor Receptor 2, HER2, HER-2, HER2/neu) is a cell surface receptor that is a "protein-tyrosine kinase receptor that is found to be overexpressed in a significant number of adenocarcinomas including gastric, esophageal, salivary, colon, bladder and lung cancers (6-7). It has extensive homology to and can heterodimerize with the EGF receptor (epidermal growth factor receptor), the erbB-3 receptor and the erbB-4 receptor. "[1] The ErbB-2 gene is located on chromosome 17q21 and encodes a protein of 1255 amino acids which weighs, when glycosylated, 185 kDa. The human ErbB-2 was cloned by homology screening with v-ErbB (1) and has the highest homology to the EGFR among ErbB family members. It is mostly related to EGFR in its kinase domain (82%) and mostly distinct in the C-terminus, which contains most of the autophosphorylation sites. ErbB-2 is the only orphan receptor of the ErbB family, since no ligand binding it has been found up to date. Activation of ErbB-2 is, therefore, highly dependent on the expression of other family members, to which it is recruited as a preferred heterodimeric partner (2). On the other hand, overexpression and/or mutation of ErbB-2 are thought to lead to spontaneous dimerisation and the stabilization of the receptor dimmers in a ligandindependent manner (3-5). ErbB2 is amplified and/or overexpressed in a number of human cancers (102, 103). ErbB2 overexpression correlates with tumor progression and aggressiveness, poor prognosis and an elevated metastatic potential.

Trastuzumab is a monoclonal antibody against the ErbB-2 receptor that lengthens remission time in metastatic breast cancer.[2]

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