Integrin β3 Haploinsufficiency Modulates Serotonin Transport and Antidepressant-Sensitive Behavior in Mice.
Mazalouskas M, Jessen T, Varney S, Sutcliffe JS, Veenstra-VanderWeele J, Cook EH, Carneiro AM
(2015) Neuropsychopharmacology 40
: 2015-24MeSH Terms: Analysis of Variance, Animals, Antidepressive Agents, Biological Transport, Gene Expression Regulation, Humans, Infant, Integrin beta3, Mice, Mice, Transgenic, Neurons, Phosphopyruvate Hydratase, Polymorphism, Genetic, Raphe Nuclei, Serotonin, Serotonin Plasma Membrane Transport Proteins, Serotonin Uptake Inhibitors, Synaptic MembranesAdded February 15, 2016
18 MeSH Terms
The cell polarity scaffold Lethal Giant Larvae regulates synapse morphology and function.
Staples J, Broadie K
(2013) J Cell Sci 126
: 1992-2003MeSH Terms: Animals, Drosophila Proteins, Drosophila melanogaster, Gene Expression Regulation, Larva, Receptors, Glutamate, Synaptic Membranes, Synaptic Transmission, Tumor Suppressor ProteinsAdded March 29, 2017
9 MeSH Terms
GPCR mediated regulation of synaptic transmission.
Betke KM, Wells CA, Hamm HE
(2012) Prog Neurobiol 96
: 304-21MeSH Terms: Animals, GTP-Binding Protein beta Subunits, GTP-Binding Protein gamma Subunits, Humans, Receptors, G-Protein-Coupled, Synaptic Membranes, Synaptic TransmissionAdded December 10, 2013
7 MeSH Terms
Chronic desipramine treatment alters tyrosine hydroxylase but not norepinephrine transporter immunoreactivity in norepinephrine axons in the rat prefrontal cortex.
Erickson SL, Gandhi AR, Asafu-Adjei JK, Sampson AR, Miner L, Blakely RD, Sesack SR
(2011) Int J Neuropsychopharmacol 14
: 1219-32MeSH Terms: Adrenergic Neurons, Adrenergic Uptake Inhibitors, Animals, Antidepressive Agents, Tricyclic, Axons, Cell Membrane, Desipramine, Immunohistochemistry, Infusion Pumps, Implantable, Male, Microscopy, Electron, Transmission, Nerve Tissue Proteins, Norepinephrine Plasma Membrane Transport Proteins, Prefrontal Cortex, Protein Transport, Rats, Rats, Sprague-Dawley, Reproducibility of Results, Synaptic Membranes, Tyrosine 3-MonooxygenaseAdded July 10, 2013
20 MeSH Terms
Dopamine depletion alters phosphorylation of striatal proteins in a model of Parkinsonism.
Brown AM, Deutch AY, Colbran RJ
(2005) Eur J Neurosci 22
: 247-56MeSH Terms: Aging, Animals, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Calcium-Calmodulin-Dependent Protein Kinases, Corpus Striatum, Disease Models, Animal, Dopamine, Dopamine and cAMP-Regulated Phosphoprotein 32, Levodopa, Male, Nerve Tissue Proteins, Neural Pathways, Neuronal Plasticity, Parkinsonian Disorders, Phosphoprotein Phosphatases, Phosphoproteins, Phosphorylation, Presynaptic Terminals, Protein Phosphatase 1, Rats, Rats, Sprague-Dawley, Receptors, AMPA, Substantia Nigra, Synaptic Membranes, Up-RegulationAdded June 21, 2013
25 MeSH Terms
Calcium/calmodulin-dependent protein kinase II and synaptic plasticity.
Colbran RJ, Brown AM
(2004) Curr Opin Neurobiol 14
: 318-27MeSH Terms: Animals, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Calcium-Calmodulin-Dependent Protein Kinases, Cell Differentiation, Central Nervous System, Dendrites, Humans, Memory, Neuronal Plasticity, Synapses, Synaptic Membranes, Synaptic TransmissionAdded June 21, 2013
12 MeSH Terms
Structural alterations at the neuromuscular junctions of matrix metalloproteinase 3 null mutant mice.
VanSaun M, Herrera AA, Werle MJ
(2003) J Neurocytol 32
: 1129-42MeSH Terms: Agrin, Animals, Cell Differentiation, Excitatory Postsynaptic Potentials, Fluorescent Antibody Technique, Matrix Metalloproteinase 3, Mice, Mice, Knockout, Microscopy, Electron, Neuromuscular Junction, Reaction Time, Receptors, Cholinergic, Synaptic Membranes, Synaptic Transmission, Up-RegulationAdded May 13, 2014
15 MeSH Terms
High-resolution localization of clathrin assembly protein AP180 in the presynaptic terminals of mammalian neurons.
Yao PJ, Coleman PD, Calkins DJ
(2002) J Comp Neurol 447
: 152-62MeSH Terms: Adaptor Protein Complex 2, Adaptor Proteins, Vesicular Transport, Animals, Carrier Proteins, Cell Compartmentation, Cerebellum, Clathrin, Exocytosis, Humans, Immunohistochemistry, Macaca fascicularis, Membrane Proteins, Microscopy, Electron, Monomeric Clathrin Assembly Proteins, Presynaptic Terminals, Protein Transport, Rats, Rats, Sprague-Dawley, Retina, Synaptic Membranes, Synaptic Transmission, Synaptic VesiclesAdded February 12, 2015
22 MeSH Terms
Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms.
Chen L, Chetkovich DM, Petralia RS, Sweeney NT, Kawasaki Y, Wenthold RJ, Bredt DS, Nicoll RA
(2000) Nature 408
: 936-43MeSH Terms: Action Potentials, Animals, COS Cells, Calcium, Calcium Channels, Cerebellum, Disks Large Homolog 4 Protein, Down-Regulation, Excitatory Postsynaptic Potentials, Glutamic Acid, Guanylate Kinases, Hippocampus, Humans, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Mice, Mice, Mutant Strains, Nerve Tissue Proteins, Neurons, Protein Transport, Receptors, AMPA, Synapses, Synaptic MembranesAdded April 2, 2019
Matrix metalloproteinase-3 removes agrin from synaptic basal lamina.
VanSaun M, Werle MJ
(2000) J Neurobiol 43
: 140-9MeSH Terms: Agrin, Animals, Antibodies, Antibody Specificity, Basement Membrane, Bungarotoxins, Dose-Response Relationship, Drug, Immunohistochemistry, Laminin, Male, Matrix Metalloproteinase 3, Microscopy, Electron, Muscle, Skeletal, Neuromuscular Junction, Rana pipiens, Rhodamines, Synaptic MembranesShow Abstract · Added May 13, 2014
Agrin, a heparin sulfate proteoglycan, is an integral member of the synaptic basal lamina and plays a critical role in the formation and maintenance of the neuromuscular junction. The N-terminal region of agrin binds tightly to basal lamina, while the C-terminal region interacts with a muscle-specific tyrosine kinase (MuSK) to induce the formation of the postsynaptic apparatus. Although the binding of agrin to basal lamina is tight, the binding of agrin to MuSK has yet to be shown; therefore, basal lamina binding is critical for maintaining the presentation of agrin to MuSK. Here we report evidence that supports our hypothesis that matrix metalloproteinase-3 (MMP-3) is responsible for the removal of agrin from synaptic basal lamina. Antibodies to the hinge region of human MMP-3 recognize molecules concentrated at the frog neuromuscular junction in both cross sections and whole mounts. Electron microscopy of neuromuscular junctions stained with antibodies to MMP-3 reveals that staining is found in the extracellular matrix surrounding the Schwann cell. Treatment of sections from frog anterior tibialis muscle with MMP-3 results in a clear and reproducible removal of agrin immunoreactivity from synaptic basal lamina. The same MMP-3 treatment does not alter anti-laminin staining. These results support our hypothesis that synaptic activity results in the activation of MMP-3 at the neuromuscular junction and that MMP-3 specifically removes agrin from synaptic basal lamina.
Copyright 2000 John Wiley & Sons, Inc.
17 MeSH Terms