Neuregulin/Heregulin is a family of structurally related polypeptide growth factors derived from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). To date, there are over 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. HRG1-β1 contains an Ig domain and an EGF-like domain that is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. This binding induces erb3 and erb4 heterodimerization with erb2, stimulating intrinsic kinase activity, which leads to tyrosine phosphorylation. Although HRG1-β1 biological effects is still unclear, it has been found to promote motility and invasiveness of breast cancer cells which may also involve up-regulation of expression and function of the autocrine motility-promoting factor (AMF). Recombinant human Heregulin-β1 (HRG1-β1) is a 7.5 kDa polypeptide consisting of only the EGF domain of Heregulin-β1 (65 amino acid residues).
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