Mammalian-cell-produced neurturin (NTN) is more potent than purified Escherichia coli-produced NTN

Michael R. Hoane, Kamal D. Puri, Lei Xu, Paul F. Stabila, Hongmei Zhao, Amit G. Gulwadi, Heidi S. Phillips, Brigitte Devaux, Mark D. Lindner, Weng Tao

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


Neurturin (NTN) is a recently identified homologue of glial-cell-line- derived neurotrophic factor. Both factors promote the survival of dopaminergic (DA) neurons. We investigated the biological activity of mammalian-cell-produced NTN versus purified Escherichia coli-produced NTN. Baby hamster kidney cells were engineered to stably secrete mature human NTN. Mammalian-cell-derived NTN enhanced the activity of embryonic DA neurons in vitro, with greater potency (maximum effect achieved in the picogram range) than purified E. coli-produced NTN. Cell-based delivery of NTN (less than 10 ng/day) was also shown to be biologically active in vivo. These results suggest that mammalian-cell-derived NTN, synthesized de novo and delivered in small quantities to the parenchyma at the target site, may be as active as much larger quantities of purified, E. coli-produced NTN, delivered by other means. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)189-193
Number of pages5
JournalExperimental Neurology
Issue number1
StatePublished - Mar 2000
Externally publishedYes


  • Bioactivity
  • Delivery
  • Neurturin

ASJC Scopus subject areas

  • Neurology
  • Developmental Neuroscience


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