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The accumulation of calcium ions (Ca) was examined in the rat brain by means of 45Ca autoradiography following the application of a weak anodal direct current to the surface of the sensorimotor cortex. Repetition of the anodal polarization with 3.0 microA for 30 min caused more Ca to accumulate in the cerebral cortex. The degree and extent of accumulation(More)
mu-Opioid receptors and their endogenous ligands, including Leu5-enkephalin (LE), are distributed abundantly in the nucleus accumbens (NAC), a region implicated in mechanisms of opiate reinforcement. We used immunoperoxidase and/or immunogold-silver methods to define ultrastructural sites for functions ascribed to mu-opioid receptors and potential sites for(More)
Physiological studies have indicated that agonists at the mu-opioid receptor (mu OR), such as morphine or the endogenous peptide methionine5-enkephalin, can markedly decrease the spontaneous activity of noradrenergic neurons in the locus coeruleus (LC). Messenger RNA and protein for mu OR are also densely expressed by LC neurons. During opiate withdrawal,(More)
Kainate is a potent agonist of an excitatory amino acid receptor subtype in the central nervous system, and causes neuronal death in several regions of the brain. Neurons are preferentially killed in the hippocampus, especially in the CA1 region, by systemic administration of kainate. It is speculated that functional alterations occur in the neurons(More)
We have recently shown, by using immunoelectron microscopy, that the mu-opioid receptor (mu OR) is prominently distributed within noradrenergic perikarya and dendrites of the nucleus locus coeruleus (LC), many of which receive excitatory-type (i.e., asymmetric) synaptic contacts from unlabeled axon terminals. To characterize further the neurotransmitter(More)
The mu opiate receptor is a principal brain site for activities of morphine, other opiate drugs, and opioid peptides in modulating pain and altering mood. Recent cloning of cDNAs encoding rat and human mu receptors reveals charged amino acid residues within putative transmembrane domains (TMs) II, III, and VI, a substantial N-terminal extracellular domain,(More)
Studies with thiol-modifying reagents have suggested that cysteines might play important roles in the function of the dopamine transporter (DAT). To identify DAT cysteines with important thiol groups, we have studied six mutant dopamine transporters in which cysteines were replaced by alanines. Substitutions of cysteines assigned to the DAT's second(More)
Proteins and peptides have been demonstrated to penetrate across the plasma membrane of eukaryotic cells by protein transduction domains. We show that protein transduction by 11 arginine (11R) is an efficient method of delivering proteins into the neurons of brain slices. Here, we demonstrate that PKA inhibitory peptide, fused with 11R and nuclear(More)
An anodal direct current of 0.3 microA or 30.0 microA was unilaterally applied for 30 min or 3 hr to the surface of the sensorimotor cortex of rats, and the effects of anodal polarization on protein kinase C (PKCgamma) activity were examined. The brains were processed by means of immunocytochemistry using the monoclonal antibody 36G9 raised against purified(More)
c-Fos protein-like immunoreactivity (IR) was investigated in the rat brain following an application of weak anodal direct current to the surface of the unilateral sensorimotor cortex in an attempt to elucidate the cellular and molecular bases of central plasticity. Anodal polarization resulted in a massive increase in c-Fos protein-like IR in neurons of the(More)