Search results for "Neurotoxin"
showing 3 items of 53 documents
D2-dopamine receptor blockade modulates temporal resolution in goldfish.
2002
A possible effect of dopamine on the temporal resolution of goldfish was investigated in a behavioral, two-alternative, forced-choice procedure. Flicker fusion frequency (FFF) was measured before and after bilateral intravitreal injections of D1- or D2-dopamine receptor (D1-/D2-R) antagonists, or after depletion of retinal dopamine by bilateral intravitreal injections of the dopaminergic neurotoxin 6-hydroxydopamine (6-OHDA). Prior to drug injections, fish achieved FFFs of 33–39 Hz. A D1-R antagonist, SCH 23390, reduced FFF by about 12% (P > 0.1), whereas a D2 antagonist, sulpiride, reduced the relative FFF by 25% (P < 0.03). Depletion of retinal dopamine with 6-OHDA induced a gradual…
Prosurvival effect of human wild-type alpha-synuclein on MPTP-induced toxicity to central but not peripheral catecholaminergic neurons isolated from …
2010
In the present work we report the generation of a new line of alpha-synuclein (alpha-SYN) transgenic mice in which the human wild-type alpha-SYN cDNA is expressed under the control of a tyrosine hydroxylase (TH) promoter. We provide evidence that the ectopic protein is found in TH expressing neurons of both central and peripheral nervous systems. The transgene is expressed very early in development coinciding with the activity of the TH promoter and in the adult brain the human protein distributes normally to the nerve endings and cell bodies of dopaminergic nigral neurons without any evidence of abnormal aggregation. Our results indicate that expression of human wild-type alpha-SYN does no…
A single mutation in the recombinant light chain of tetanus toxin abolishes its proteolytic activity and removes the toxicity seen after reconstituti…
1994
Specific proteolysis by the tetanus toxin light chain of a vesicle-associated membrane protein (VAMP) involved in exocytosis is thought to underlie its intracellular blockade of neurotransmitter release. To substantiate this mechanism, recombinant light chain was expressed as a maltose binding protein-light chain fusion product in Escherichia coli. After purification of affinity chromatography and cleavage with factor Xa, the resultant light chain was isolated and its identity confirmed by Western blotting and N-terminal sequencing. It exhibited activity similar to that of the native light chain in proteolyzing its target in isolated bovine small synaptic vesicles and in hydrolyzing a 62-re…