TY - JOUR
T1 - A novel brain-derived member of the epidermal growth factor family that interacts with ErbB3 and ErbB4
AU - Higashiyama, Shigeki
AU - Horikawa, Michiharu
AU - Yamada, Kouji
AU - Ichino, Naohiro
AU - Nakano, Norihiko
AU - Nakagawa, Takatoshi
AU - Miyagawa, Junichiro
AU - Matsushita, Natsuki
AU - Nagatsu, Toshiharu
AU - Taniguchi, Naoyuki
AU - Ishiguro, Hiroshi
PY - 1997/9
Y1 - 1997/9
N2 - A novel member of the epidermal growth factor (EGF) family, the neural- and thymus-derived activator for ErbB kinases (NTAK), has been purified and cloned. Five alternative spliced isoforms have been detected in the rat adrenal pheochromocytoma cell line, PC-12 cells. The rat NTAK(α)2a isoform exhibits 94% identity in its primary sequence with the human NTAK(α) isoform. In vivo, NTAK is only expressed in the brain of rat E11.5 embryos, and in the brain and thymus of adult rats. The soluble 46 kDa form binds directly to ErbB3 and B4, but not to ErbB1 or B2. NTAK, however, transactivates ErbB1 and B2 via heterodimerization with ErbB3 or B4. NTAK stimulates the differentiation of MDA-MB-453 cells and competitively inhibits the binding of [125I]neuregulin to these cells. In addition to these neuregulin-like properties, NTAK exhibits limited structural homology to neuregulins in the immunoglobulin (Ig)-like, EGF-like, and hydrophobic domains. Thus, NTAK appears to be a new member of the EGF family displaying neuregulin properties.
AB - A novel member of the epidermal growth factor (EGF) family, the neural- and thymus-derived activator for ErbB kinases (NTAK), has been purified and cloned. Five alternative spliced isoforms have been detected in the rat adrenal pheochromocytoma cell line, PC-12 cells. The rat NTAK(α)2a isoform exhibits 94% identity in its primary sequence with the human NTAK(α) isoform. In vivo, NTAK is only expressed in the brain of rat E11.5 embryos, and in the brain and thymus of adult rats. The soluble 46 kDa form binds directly to ErbB3 and B4, but not to ErbB1 or B2. NTAK, however, transactivates ErbB1 and B2 via heterodimerization with ErbB3 or B4. NTAK stimulates the differentiation of MDA-MB-453 cells and competitively inhibits the binding of [125I]neuregulin to these cells. In addition to these neuregulin-like properties, NTAK exhibits limited structural homology to neuregulins in the immunoglobulin (Ig)-like, EGF-like, and hydrophobic domains. Thus, NTAK appears to be a new member of the EGF family displaying neuregulin properties.
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U2 - 10.1093/oxfordjournals.jbchem.a021806
DO - 10.1093/oxfordjournals.jbchem.a021806
M3 - Article
C2 - 9348101
AN - SCOPUS:15444344413
SN - 0021-924X
VL - 122
SP - 675
EP - 680
JO - Journal of Biochemistry
JF - Journal of Biochemistry
IS - 3
ER -