Abstract
ErbB2 is a transmembrane glycoprotein with intrinsic PTK activity and has extensive homology to EGFR. On the basis of its expression pattern in fetal and adult tissue, ErbB2 is believed to play a general role in development, rather than as a cell lineage-specific receptor. Amplification of the gene and overexpression of the receptor is found in 25%–30% of primary human breast and ovarian cancers. ErbB2 consists of an extracellular ligand binding domain, a single transmembrane domain, and an intracellular tyrosine kinase domain. Fifty cysteine residues, which are clustered in two subdomains, are present in the extracellular domain. The location of the cysteine residues is conserved between EGFR and ErbB2. In the intracellular portion of the receptor, the tyrosine kinase domain is followed by a C-terminal tail, which is presumably involved in cellular signaling. ErbB2 is assayed by phosphorylation in vitro or by immunoblot analysis with antiphosphotyrosine antibody.
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