Biochem Biophys Res Commun. 2009 Jul 31;385(3):380-4. Epub 2009 May 22.

Recombinant GDNF: tetanus toxin fragment C fusion protein produced from insect cells.

Li J, Chian RJ, Ay I, Celia SA, Kashi BB, Tamrazian E, Matthews JC, Remington MP, Pepinsky RB, Fishman PS, Brown RH Jr, Francis JW.

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Cecil B. Day Laboratory for Neuromuscular Research, Department of Neurology, Massachusetts General Hospital, Charlestown, MA 02129, USA.

Abstract

Glial cell line-derived neurotrophic factor (GDNF) has potent survival-promoting effects on CNS motor neurons in experimental animals. Its therapeutic efficacy in humans, however, may have been limited by poor bioavailability to the brain and spinal cord. With a view toward improving delivery of GDNF to CNS motor neurons in vivo, we generated a recombinant fusion protein comprised of rat GDNF linked to the non-toxic, neuron-binding fragment of tetanus toxin. Recombinant GDNF:TTC produced from insect cells was a soluble homodimer like wild-type GDNF and was bi-functional with respect to GDNF and TTC activity. Like recombinant rat GDNF, the fusion protein increased levels of immunoreactive phosphoAkt in treated NB41A3-hGFRalpha-1 neuroblastoma cells. Like TTC, GDNF:TTC bound to immobilized ganglioside GT1b in vitro with high affinity and selectivity. These results support further testing of recombinant GDNF:TTC as a non-viral vector to improve delivery of GDNF to brain and spinal cord in vivo.

PMID:: 19465006; [PubMed - indexed for MEDLINE]

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