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L-histidine inhibits production of lysophosphatidic acid by the tumor-associated cytokine,autotaxin
Authors:Timothy?Clair  author-information"  >  author-information__contact u-icon-before"  >  mailto:timclair@helix.nih.gov"   title="  timclair@helix.nih.gov"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author,Eunjin?Koh,Malgorzata?Ptaszynska,Russell?W?Bandle,Lance?A?Liotta,Elliott?Schiffmann,Mary?L?Stracke
Affiliation:(1) Laboratory of Pathology, National Cancer Institute, National Institutes of Health, 20892 Bethesda, Maryland, USA
Abstract:

Background  

Autotaxin (ATX, NPP-2), originally purified as a potent tumor cell motility factor, is now known to be the long-sought plasma lysophospholipase D (LPLD). The integrity of the enzymatic active site, including three crucial histidine moieties, is required for motility stimulation, as well as LPLD and 5'nucleotide phosphodiesterase (PDE) activities. Except for relatively non-specific chelation agents, there are no known inhibitors of the ATX LPLD activity.
Keywords:
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