Abstract

Recombinant human glial cell line-derived neurotrophic factor (GDNF) has been expressed at high levels and produced in large quantities in baculovirus-infected Trichoplusia ni cells (Tn-5B1-4). The glycosylated protein was purified using immunoaffinity chromatography and gel filtration. Pure, recombinant human GDNF promoted the survival and morphological differentiation of embryonic dopaminergic neurons and enhanced axonal regeneration after sciatic nerve transection. Because recombinant bioactive human GDNF can be obtained in large quantities, and purified to near homogeneity, they are suitable for evaluation in animal models.

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