Skip to main navigation Skip to search Skip to main content

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

Abstract

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
Volume162
Issue number1
DOIs
StatePublished - Mar 2000
Externally publishedYes

Keywords

  • Bioactivity
  • Delivery
  • Neurturin

ASJC Scopus subject areas

  • Neurology
  • Developmental Neuroscience

Fingerprint

Dive into the research topics of 'Mammalian-cell-produced neurturin (NTN) is more potent than purified Escherichia coli-produced NTN'. Together they form a unique fingerprint.

Cite this