BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential

Akinori Nakajima; Ken Kataoka; Mei Hong; Masakiyo Sakaguchi; Nam Ho Huh

doi:10.1016/S0304-3835(03)00443-9

BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential

Akinori Nakajima, Ken Kataoka, Mei Hong, Masakiyo Sakaguchi, Nam Ho Huh

Research output: Contribution to journal › Article › peer-review

60 Citations (Scopus)

Abstract

A novel protein kinase named BRPK was isolated and partially characterized. BRPK was expressed at a higher level in three carcinoma cell lines with higher metastatic potential. Mouse and human BRPK cDNAs are well conserved and encode 580 and 581 amino acids, respectively. BRPK has a serine/threonine-type protein kinase domain, and the recombinant proteins of BRPK were capable of autophosphorylation. The results of a comparative sequence analysis indicated a possible link of BRPK to BRAP2. BRAP2 is known to bind the nuclear localization signal of BRCA1. We cloned mouse BRAP2 cDNA and showed the presence of isoforms.

Original language	English
Pages (from-to)	195-201
Number of pages	7
Journal	Cancer Letters
Volume	201
Issue number	2
DOIs	https://doi.org/10.1016/S0304-3835(03)00443-9
Publication status	Published - Nov 14 2003

Keywords

BRAP2
BRCA1
Metastasis
Protein kinase

ASJC Scopus subject areas

Oncology
Cancer Research

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/S0304-3835(03)00443-9

Cite this

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title = "BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential",

abstract = "A novel protein kinase named BRPK was isolated and partially characterized. BRPK was expressed at a higher level in three carcinoma cell lines with higher metastatic potential. Mouse and human BRPK cDNAs are well conserved and encode 580 and 581 amino acids, respectively. BRPK has a serine/threonine-type protein kinase domain, and the recombinant proteins of BRPK were capable of autophosphorylation. The results of a comparative sequence analysis indicated a possible link of BRPK to BRAP2. BRAP2 is known to bind the nuclear localization signal of BRCA1. We cloned mouse BRAP2 cDNA and showed the presence of isoforms.",

keywords = "BRAP2, BRCA1, Metastasis, Protein kinase",

author = "Akinori Nakajima and Ken Kataoka and Mei Hong and Masakiyo Sakaguchi and Huh, {Nam Ho}",

note = "Funding Information: This work was supported by a Grant-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan. We are grateful to Dr Mikiro Takaishi for his technical help and valuable discussion.",

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doi = "10.1016/S0304-3835(03)00443-9",

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T1 - BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential

AU - Nakajima, Akinori

AU - Kataoka, Ken

AU - Hong, Mei

AU - Sakaguchi, Masakiyo

AU - Huh, Nam Ho

N1 - Funding Information: This work was supported by a Grant-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan. We are grateful to Dr Mikiro Takaishi for his technical help and valuable discussion.

PY - 2003/11/14

Y1 - 2003/11/14

N2 - A novel protein kinase named BRPK was isolated and partially characterized. BRPK was expressed at a higher level in three carcinoma cell lines with higher metastatic potential. Mouse and human BRPK cDNAs are well conserved and encode 580 and 581 amino acids, respectively. BRPK has a serine/threonine-type protein kinase domain, and the recombinant proteins of BRPK were capable of autophosphorylation. The results of a comparative sequence analysis indicated a possible link of BRPK to BRAP2. BRAP2 is known to bind the nuclear localization signal of BRCA1. We cloned mouse BRAP2 cDNA and showed the presence of isoforms.

AB - A novel protein kinase named BRPK was isolated and partially characterized. BRPK was expressed at a higher level in three carcinoma cell lines with higher metastatic potential. Mouse and human BRPK cDNAs are well conserved and encode 580 and 581 amino acids, respectively. BRPK has a serine/threonine-type protein kinase domain, and the recombinant proteins of BRPK were capable of autophosphorylation. The results of a comparative sequence analysis indicated a possible link of BRPK to BRAP2. BRAP2 is known to bind the nuclear localization signal of BRCA1. We cloned mouse BRAP2 cDNA and showed the presence of isoforms.

KW - BRAP2

KW - BRCA1

KW - Metastasis

KW - Protein kinase

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DO - 10.1016/S0304-3835(03)00443-9

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AN - SCOPUS:0242321145

SN - 0304-3835

VL - 201

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JO - Cancer Letters

JF - Cancer Letters

IS - 2

ER -

BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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