Gomez-Palacio-Schjetnan A. and Escobar M.L. (2008) Neurosci. Lett. 445, 62.
Alomone Labs Recombinant human BDNF protein (#B-250) was used by intrahippocampal microinfusion to analyze its effects on functional and structural synaptic plasticity in adult rats, in vivo. The results support the idea that BDNF plays an important role as synaptic messenger of activity-dependent synaptic plasticity in the adult mammalian.
Huh, C.Y. et al. (2008) J. Neurosci. 28, 1404.
The medial septum and diagonal band of Broca (MS-DBB) sends neurons to the hippocampus and plays an important role in memory. The MS-DBB contains cholinergic, GABAergic, glutamatergic neurons, and neurons that coexpress markers for multiple neurotransmitter phenotypes. Due to the various types of neurons found in MS-DBB, the exact role of NGF regarding synaptic transmission was studied. Native mouse NGF 2.5S protein (99%) (#N-240) was administered to MS-DBB neurons. Chronic exposure to NGF increased choline and glutamate release from cholinergic neurons and did not alter neurotransmitter release from non-cholinergic neurons. In addition, p75NTR was found to mediate the effects of NGF, since exposure to K252a (#K-150), an inhibitor of TrkA receptor had no effect on NGF-mediated synaptic transmission, whereas the use of a p75NTR neutralizing antibody did.
Wiener, R. et al. (2008) J. Biol. Chem. 283, 5815.
The KCNQ (KV7.1-5) subfamily of voltage-gated K+ channels plays important roles in the brain and in the heart. One important structural feature of the KV7 channels is the large intracellular C-terminus which is important for tetramerization and membrane trafficking. An extensive and detailed study of the C-terminal domain of KV7.1 (KCNQ1) channel revealed that the C-terminal can be divided in two different entities. One half is important for functional expression, proper folding and gating of the channel, whereas the other half is in part responsible for membrane trafficking. Immunocytochemistry studies using Alomone Labs Anti-KCNQ1 Antibody (#APC-022) demonstrated that a mutant form of the channel is strongly localized to the cytoplasm compared to the wild type channel.