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Functional analysis of a Novel Human Protein Kinase, Nori-2p (MRPK) in the Proliferation of Cancer Cells

Research Project

Project/Area Number 11671165
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field General surgery
Research InstitutionEhime University

Principal Investigator

ABE Yasuhito  Ehime University, School of Medicine, 1st Pathology, Associate Professor, 医学部, 助教授 (30184229)

Co-Investigator(Kenkyū-buntansha) KITO Katsumi  Ehime University, School of Medicine, 1st Pathology, Instructor, 医学部, 助手 (00274308)
Project Period (FY) 1999 – 2000
Project Status Completed (Fiscal Year 2000)
Budget Amount *help
¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 2000: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1999: ¥1,800,000 (Direct Cost: ¥1,800,000)
KeywordsLAK cells / Membrane Lymphotoxin / Protein Kinase / Serine / Threonine / Subtraction Library / YGR262c / Yeast Complementation Assay / Cell Proliferation
Research Abstract

A novel human serine/threonine kinase was identified in a Lymphokine-activated T-killer (T-LAK) cell subtraction library and full length cDNA of both human and mouse were cloned. This protein kinase, namely membrane lymphotoxin-related protein kinase (MRPK/Nori-2p), possesses a serine/threonine kinase motif and appears to be a homologue of a yeast serine/threonine kinase, YGR262c. Similar with YGR 262c, MRPK fails to have some typical sequence patterns of protein kinase but it exerts casein phosphorylation in vitro. The expression of MRPK mRNA was noted markedly in the testicular tissue. The activated but not deactivated form of T-LAK cells express MRPK mRNA.Natural MRPK transcript was identified in some cancer cell lines along with the mRNA expression. MRPK indicated to have a bipartite nuclear localization signal (NLS_BP) that does not exist in the yeast YGR262c. Immunohistochemical study showed that MRPK localizes in the nucleus. A complementation assay using YGR262c-disrupted yeast showed that MRPK may not be a functional homologue of YGR262c. A synchronized cell cycle study showed that MRPK mRNA appeared only in the S-phase. These results suggest that a novel protein kinase, MRPK, may play some important roles in the proliferation of IL-2 driven T-LAK cells and some cancer cells.

Report

(3 results)
  • 2000 Annual Research Report   Final Research Report Summary
  • 1999 Annual Research Report

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Published: 1999-04-01   Modified: 2016-04-21  

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