Structure and function of a novel ErbB ligand, NTAK

H. Ishiguro, S. Higashiyama, K. Yamada, N. Ichino, N. Taniguchi, T. Nagatsu

Research output: Contribution to journalShort survey

4 Citations (Scopus)

Abstract

A novel member of the epidermal growth factor (EGF) family, the neural and thymus-derived activator for ErbB kinase (NTAK) has been cloned from the cDNA library of a rat pheochromocytoma cell line, PC12 cells and human neuroblastoma cell line, SK-N-SH cells. Four alternative spliced isoforms from rat cDNA have been detected by the methods of RT-PCR. The rat NTAKα2a isoform exhibits 94% identity in its sequence with the human NTAKα isoform. Three characteristic Ig-like, EGF-like and hydrophobic domains have been identified in rat and human NTAK molecules. Recombinant NTAK, the soluble 46 kDa form, binds directly to ErbB3 and ErbB4, but not ErbB1 and B2. NTAK, however, transactivates with heterodimer such as ErbB1/B3, B1/B4, B2/B3, B2/B4 and B3/B4. NTAK stimulates the differentiation of MDA-MB-453 cells, derived from blast carcinoma. NTAK competitively inhibits the binding of [125I] NRG-1 to these cells. Thus, NTAK is a new member of the EGF family displaying NRG-1 properties.

Original languageEnglish
Pages (from-to)137-142
Number of pages6
JournalJapanese Journal of Psychopharmacology
Volume18
Issue number4
Publication statusPublished - 11-12-1998

Fingerprint

Thymus Gland
Phosphotransferases
Ligands
Epidermal Growth Factor
Protein Isoforms
PC12 Cells
Neuroblastoma
Gene Library
Complementary DNA
Carcinoma
Cell Line
Polymerase Chain Reaction

All Science Journal Classification (ASJC) codes

  • Medicine(all)

Cite this

Ishiguro, H., Higashiyama, S., Yamada, K., Ichino, N., Taniguchi, N., & Nagatsu, T. (1998). Structure and function of a novel ErbB ligand, NTAK. Japanese Journal of Psychopharmacology, 18(4), 137-142.
Ishiguro, H. ; Higashiyama, S. ; Yamada, K. ; Ichino, N. ; Taniguchi, N. ; Nagatsu, T. / Structure and function of a novel ErbB ligand, NTAK. In: Japanese Journal of Psychopharmacology. 1998 ; Vol. 18, No. 4. pp. 137-142.
@article{81574b6e4689447c9ec3451ad262206d,
title = "Structure and function of a novel ErbB ligand, NTAK",
abstract = "A novel member of the epidermal growth factor (EGF) family, the neural and thymus-derived activator for ErbB kinase (NTAK) has been cloned from the cDNA library of a rat pheochromocytoma cell line, PC12 cells and human neuroblastoma cell line, SK-N-SH cells. Four alternative spliced isoforms from rat cDNA have been detected by the methods of RT-PCR. The rat NTAKα2a isoform exhibits 94{\%} identity in its sequence with the human NTAKα isoform. Three characteristic Ig-like, EGF-like and hydrophobic domains have been identified in rat and human NTAK molecules. Recombinant NTAK, the soluble 46 kDa form, binds directly to ErbB3 and ErbB4, but not ErbB1 and B2. NTAK, however, transactivates with heterodimer such as ErbB1/B3, B1/B4, B2/B3, B2/B4 and B3/B4. NTAK stimulates the differentiation of MDA-MB-453 cells, derived from blast carcinoma. NTAK competitively inhibits the binding of [125I] NRG-1 to these cells. Thus, NTAK is a new member of the EGF family displaying NRG-1 properties.",
author = "H. Ishiguro and S. Higashiyama and K. Yamada and N. Ichino and N. Taniguchi and T. Nagatsu",
year = "1998",
month = "12",
day = "11",
language = "English",
volume = "18",
pages = "137--142",
journal = "Neuropsychopharmacology Reports",
issn = "1340-2544",
publisher = "John Wiley and Sons Inc.",
number = "4",

}

Ishiguro, H, Higashiyama, S, Yamada, K, Ichino, N, Taniguchi, N & Nagatsu, T 1998, 'Structure and function of a novel ErbB ligand, NTAK', Japanese Journal of Psychopharmacology, vol. 18, no. 4, pp. 137-142.

Structure and function of a novel ErbB ligand, NTAK. / Ishiguro, H.; Higashiyama, S.; Yamada, K.; Ichino, N.; Taniguchi, N.; Nagatsu, T.

In: Japanese Journal of Psychopharmacology, Vol. 18, No. 4, 11.12.1998, p. 137-142.

Research output: Contribution to journalShort survey

TY - JOUR

T1 - Structure and function of a novel ErbB ligand, NTAK

AU - Ishiguro, H.

AU - Higashiyama, S.

AU - Yamada, K.

AU - Ichino, N.

AU - Taniguchi, N.

AU - Nagatsu, T.

PY - 1998/12/11

Y1 - 1998/12/11

N2 - A novel member of the epidermal growth factor (EGF) family, the neural and thymus-derived activator for ErbB kinase (NTAK) has been cloned from the cDNA library of a rat pheochromocytoma cell line, PC12 cells and human neuroblastoma cell line, SK-N-SH cells. Four alternative spliced isoforms from rat cDNA have been detected by the methods of RT-PCR. The rat NTAKα2a isoform exhibits 94% identity in its sequence with the human NTAKα isoform. Three characteristic Ig-like, EGF-like and hydrophobic domains have been identified in rat and human NTAK molecules. Recombinant NTAK, the soluble 46 kDa form, binds directly to ErbB3 and ErbB4, but not ErbB1 and B2. NTAK, however, transactivates with heterodimer such as ErbB1/B3, B1/B4, B2/B3, B2/B4 and B3/B4. NTAK stimulates the differentiation of MDA-MB-453 cells, derived from blast carcinoma. NTAK competitively inhibits the binding of [125I] NRG-1 to these cells. Thus, NTAK is a new member of the EGF family displaying NRG-1 properties.

AB - A novel member of the epidermal growth factor (EGF) family, the neural and thymus-derived activator for ErbB kinase (NTAK) has been cloned from the cDNA library of a rat pheochromocytoma cell line, PC12 cells and human neuroblastoma cell line, SK-N-SH cells. Four alternative spliced isoforms from rat cDNA have been detected by the methods of RT-PCR. The rat NTAKα2a isoform exhibits 94% identity in its sequence with the human NTAKα isoform. Three characteristic Ig-like, EGF-like and hydrophobic domains have been identified in rat and human NTAK molecules. Recombinant NTAK, the soluble 46 kDa form, binds directly to ErbB3 and ErbB4, but not ErbB1 and B2. NTAK, however, transactivates with heterodimer such as ErbB1/B3, B1/B4, B2/B3, B2/B4 and B3/B4. NTAK stimulates the differentiation of MDA-MB-453 cells, derived from blast carcinoma. NTAK competitively inhibits the binding of [125I] NRG-1 to these cells. Thus, NTAK is a new member of the EGF family displaying NRG-1 properties.

UR - http://www.scopus.com/inward/record.url?scp=0031734406&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031734406&partnerID=8YFLogxK

M3 - Short survey

C2 - 9866830

AN - SCOPUS:0031734406

VL - 18

SP - 137

EP - 142

JO - Neuropsychopharmacology Reports

JF - Neuropsychopharmacology Reports

SN - 1340-2544

IS - 4

ER -

Ishiguro H, Higashiyama S, Yamada K, Ichino N, Taniguchi N, Nagatsu T. Structure and function of a novel ErbB ligand, NTAK. Japanese Journal of Psychopharmacology. 1998 Dec 11;18(4):137-142.