The hybrid neuroblastoma cell line NG108-15 were differentiated for 48H until axon-like neurites and varicosities were observed and transfected with DNA using the Magnetofection reagent NeuroMag
This paper shows the high efficiency of NeuroMag from OZ Biosciences to transfect any kind of neuronal cell type of whom NG108-15 neuroblastoma cell line.article reference: J Neurosci. 2014 Oct 22;34(43):14210-8.
Regulation of Presynaptic Ca2+, Synaptic Plasticity and Contextual Fear Conditioning by a N-terminal β-Amyloid Fragment.
Lawrence JL, Tong M, Alfulaij N, Sherrin T, Contarino M, White MM, Bellinger FP, Todorovic C, Nichols RA.
AbstractSoluble β-amyloid has been shown to regulate presynaptic Ca(2+) and synaptic plasticity. In particular, picomolar β-amyloid was found to have an agonist-like action on presynaptic
nicotinic receptors and to augment long-term potentiation (LTP) in a
manner dependent upon nicotinic receptors. Here, we report that a
functional N-terminal domain exists within β-amyloid for its
agonist-like activity. This sequence corresponds to a N-terminal
fragment generated by the combined action of α- and β-secretases, and
resident carboxypeptidase. The N-terminal β-amyloid fragment is present
in the brains and CSF of healthy adults as well as in Alzheimer's
patients. Unlike full-length β-amyloid, the N-terminal β-amyloid
fragment is monomeric and nontoxic. In Ca(2+) imaging studies using a
model reconstituted rodent neuroblastoma cell line and isolated mouse
nerve terminals, the N-terminal β-amyloid fragment proved to be highly
potent and more effective than full-length β-amyloid in its agonist-like
action on nicotinic receptors. In addition, the N-terminal β-amyloid
fragment augmented theta burst-induced post-tetanic potentiation and LTP
in mouse hippocampal slices. The N-terminal fragment also rescued LTP
inhibited by elevated levels of full-length β-amyloid. Contextual fear
conditioning was also strongly augmented following bilateral injection
of N-terminal β-amyloid fragment into the dorsal hippocampi of intact
mice. The fragment-induced augmentation of fear conditioning was
attenuated by coadministration of nicotinic antagonist. The activity of
the N-terminal β-amyloid fragment appears to reside largely in a
sequence surrounding a putative metal binding site, YEVHHQ. These
findings suggest that the N-terminal β-amyloid fragment may serve as a
potent and effective endogenous neuromodulator.
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