Brain Res
Department of Anatomy, College of Medicine, University of Iowa, Iowa City 52242.
Published: July 1989
These experiments utilize a paradigm developed to study plastic responses of peptidergic neurons in a discrete brain area following deafferentation. The central nucleus of the amygdala (CNA) is richly innervated by somatostatin-immunoreactive (SS-I) terminal axons. In the course of preliminary light microscopic (LM) investigations by this laboratory, changes were observed in the density of presumed SS-I terminals in the rat CNA after lesioning the medial input. The LM finding of increased density of presumed SS-I terminals in the CNA at the 10-day post-lesion stage underscored the need for a quantitative electron microscopic (EM) study of the SS-I components, including an evaluation of synaptic events at different survival periods. At the 3-day post-lesion stage, EM examination showed degenerating axons in the lesioned CNA, many already engulfed by astrocytes. None of the degenerating profiles were SS-I, supporting the view that the lesion did not interrupt, to any significant extent, SS-I axons entering the nucleus. EM surveys of the 10-day post-lesion material demonstrated that degenerated profiles had almost completely disappeared. Numbers of SS-I axon terminals, particularly of smaller-sized profiles, were increased by 22% over control value. Synaptic frequency was decreased by 16% below control value. Numbers of SS-I terminals making synapses were increased 3.4% above control value. At the 30-day post-lesion stage, the total number of SS-I terminal axons had increased 86% over controls, whereas the synaptic frequency had decreased by about a third below controls. The absolute number of SS-I terminals engaging in synapses had increased by 24% over controls. The 90-day post-lesion CNA showed a further increase in the number of SS-I axon profiles: 136% over control value. The synapse-to-axon ratio (synaptic frequency) of 27% was similar to that observed for the CNA from the unlesioned side or from unoperated animals. At this stage the number of SS-I synapses had increased by 135% over controls. This model presents many possibilities for studying neuroplasticity, particularly involving peptidergic neurons of the central autonomic nervous system.
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http://dx.doi.org/10.1016/0006-8993(89)90916-5 | DOI Listing |
J Neurosci
June 2000
Department of Physiology, University of Toronto, Toronto, Ontario M5S 1A8 Canada.
The NMDA subtype of the glutamate-gated channel exhibits a high permeability to Ca(2+). The influx of Ca(2+) through NMDA channels is limited by a rapid and Ca(2+)/calmodulin (CaM)-dependent inactivation that results from a competitive displacement of cytoskeleton-binding proteins from the NR1 subunit of the receptor by Ca(2+)/CaM (Zhang et al., 1998; Krupp et al.
View Article and Find Full Text PDFPlanta
November 1999
Centro de Investigaciones Biológicas, Fundación para Investigaciones Biológicas Aplicadas (FIBA)-PROBIOP (CONICET), C.C. 1348, 7600 Mar del Plata, Argentina.
The pathway of sucrose metabolism in cyanobacteria is just starting to be elucidated. The present study describes the first isolation and biochemical characterization of a prokaryotic sucrose synthase (SS, EC 2.4.
View Article and Find Full Text PDFJ Biol Chem
December 1995
Research Institute for Food Science, Kyoto University, Japan.
Ovotransferrin N lobe contains six intrachain disulfides (SS-I/Cys10-Cys45; SS-II/Cys20-Cys36; SS-III/Cys115-Cys197; SS-IV/Cys160-Cys174; SS-V/Cys171-Cys182; SS-VI/Cys228-Cys242) in a single polypeptide chain of 332 amino acid residues. Upon the protein disulfide reduction with dithiothreitol under nondenaturing conditions, the intermediate species with four, three, and two disulfides were generated. The partially disulfide-reduced intermediates were isolated, and the localization of intact disulfides in the intermediates was determined by an indirect end-labeling method.
View Article and Find Full Text PDFJ Biol Chem
September 1993
Research Institute for Food Science, Kyoto University, Japan.
The denatured, disulfide-reduced form of the N-terminal half-molecule of ovotransferrin was reoxidized with either oxidized dithiothreitol or GSSG and analyzed for the localization of disulfide bonds. Chemical analyses of the reoxidized proteins revealed that the disulfide peptides corresponding to the six native protein disulfides (SS-I, SS-II, SS-III, SS-IV, SS-V, and SS-VI) are all regained in the reoxidized protein. The peptide recoveries from the reoxidized proteins were, however, about half of those from the native protein with respect to the two inner disulfides (SS-IV and SS-V) in the kringle bridges, but all the disulfide peptides corresponding to the remaining disulfides (SS-I, SS-II, SS-III, and SS-VI) were recovered at almost equivalent yields in the native and reoxidized proteins.
View Article and Find Full Text PDFJ Comp Neurol
October 1990
Section of Neuroanatomy, School of Medicine, Yale University, New Haven, Connecticut 06510.
Synaptic connections and fine structural characteristics of neuropeptide Y-immunoreactive (NPY-i) neurons in the fascia dentata were studied using an antiserum against NPY. Normal and colchicine pretreated rats were examined to study the synaptic connections of NPY-i neurons in the normal fascia dentata. The perforant pathway and fimbria fornix were transected to label afferent fibers to NPY-positive cells.
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