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Site-directed Mutations in the Tumor-associated Cytokine, Autotaxin, Eliminate Nucleotide Phosphodiesterase, Lysophospholipase D, and Motogenic Activities

Authors
 Eunjin Koh  ;  Timothy Clair  ;  Mary Stracke  ;  Lance Liotta  ;  Elliott Schiffmann  ;  Elisa C. Woodhouse 
Citation
 CANCER RESEARCH, Vol.63(9) : 2042-2045, 2003 
Journal Title
 CANCER RESEARCH 
ISSN
 0008-5472 
Issue Date
2003
MeSH
Animals ; COS Cells ; Cell Movement/genetics ; Cercopithecus aethiops ; Glucose-6-Phosphate Isomerase/genetics* ; Glucose-6-Phosphate Isomerase/metabolism* ; Glycoproteins/genetics* ; Glycoproteins/metabolism* ; Humans ; Multienzyme Complexes* ; Mutagenesis, Site-Directed ; Phosphodiesterase I ; Phosphoric Diester Hydrolases/genetics ; Phosphoric Diester Hydrolases/metabolism* ; Point Mutation* ; Protein Structure, Tertiary ; Pyrophosphatases ; Receptors, Purinergic P1/physiology ; Structure-Activity Relationship
Keywords
12727817
Abstract
The exo-enzyme autotaxin/NPP2 (ATX/NPP2) is a potent stimulator of cell migration, invasion, metastasis, and angiogenesis. Recently, ATX/NPP2 was found to possess lysophospholipase D (lyso-LPD) activity, generating the bioactive mediator lysophosphatidic acid from precursors. In the present study, we used site-directed mutagenesis to delineate the active domain of lysophospholipid catalytic activity and to examine potential overlap with the nucleotide phosphodiesterase domain. We found four amino acid residues obligatory for the phosphodiesterase, lyso-PLD, and migration-stimulating activities of ATX/NPP2, suggesting that 5'-nucleotide phosphodiesterase (PDE) and lyso-PLD share a common reaction mechanism and inviting design of enzymatic inhibitors as therapeutic agents for neoplastic disease.
Files in This Item:
T200307562.pdf Download
DOI
OAK-2003-01526
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Biochemistry and Molecular Biology (생화학-분자생물학교실) > 1. Journal Papers
Yonsei Authors
Koh, Eun Jin(고은진) ORCID logo https://orcid.org/0000-0001-8967-6266
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/114686
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