Abstract
The nontoxic C fragment of tetanus toxin (TC) can transport other proteins from the circulation to central nervous system (CNS) motor neurons. Increased levels of CuZn superoxide dismutase (SOD) are protective in experimental models of stroke and Parkinson's disease, whereas mutations in SOD can cause motor neuron disease. We have linked TC to SOD and purified the active recombinant proteins in both the TC-SOD and SOD-TC orientations. Light microscopic immunohistochemistry and quantitative enzyme-linked immunosorbant assays (ELISA) of mouse brainstem, after intramuscular injection, demonstrate that the fusion proteins undergo retrograde axonal transport and transsynaptic transfer as efficiently as TC alone.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Animals
-
Axonal Transport / physiology*
-
Brain Stem / chemistry
-
Brain Stem / cytology*
-
Brain Stem / enzymology
-
Enzyme-Linked Immunosorbent Assay
-
Escherichia coli / genetics
-
Gene Expression / physiology
-
Immunohistochemistry
-
Male
-
Mice
-
Mice, Inbred C57BL
-
Motor Neurons / chemistry
-
Motor Neurons / physiology
-
Rabbits
-
Recombinant Proteins / analysis
-
Recombinant Proteins / metabolism
-
Recombinant Proteins / pharmacokinetics
-
Superoxide Dismutase / genetics
-
Superoxide Dismutase / metabolism
-
Superoxide Dismutase / pharmacokinetics*
-
Tetanus Toxin / analysis
-
Tetanus Toxin / genetics
-
Tetanus Toxin / pharmacokinetics*
Substances
-
Recombinant Proteins
-
Tetanus Toxin
-
Superoxide Dismutase