scholarly journals Sciatin: immunocytochemical localization of a myotrophic protein in chicken neural tissues.

1981 ◽  
Vol 29 (10) ◽  
pp. 1205-1212 ◽  
Author(s):  
T H Oh ◽  
C A Sofia ◽  
Y C Kim ◽  
C Carroll ◽  
H H Kim ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Cardiac Muscle ◽  
Cortical Neurons ◽  
Cultured Cells ◽  
Neuronal Cultures ◽  
Adult Chicken ◽  
Spinal Cord Neurons ◽  
Neural Tissues ◽  
Cerebral Cortical Neurons ◽  
Sciatic Nerves

A mytotrophic protein (sciatin) purified from chicken sciatic nerves has "trophic" or "maintenance" effects on cultured muscle. We have elicited a specific antiserum against purified sciatin in rabbits. Using this antiserum, we investigated the distribution of sciatin in embryonic and adult chicken tissues by an unlabeled peroxidase-an-tiperoxidase method at the light microscopic level. The antiserum stained adult chicken neural tissues in situ and cultured embryonic chick neurons. Staining was intense in the cell bodies of spinal cord neurons and the axoplasm of sciatic nerves. These was reaction product seen in the outer margins of myelin sheaths that corresponded to the Schwann cell cytoplasm. Cerebral cortical neurons were weakly stained by the antiserum. No staining was apparent in oligodendrocytes or astrocytes. Nonneural tissues, such as skeletal, smooth and cardiac muscle, kidney, and liver, were also unstained by the antiserum. Cultured spinal cord neurons, cerebral cortical neurons, and sensory neurons were stained immunocytochemically by the antiserum. There was no reaction product seen in the glial cells that are usually present in neuronal cultures or cultured cells from liver, kidney, skeletal muscle, smooth muscle, and cardiac muscle. Our results thus show that the myotrophic protein is localized in neuronal perikarya and their processes in vivo as well as in vitro.

scholarly journals A plasma membrane integral sialoglycoprotein (Sgp 130) molecularly distinguishes nonjunctional dense plaque sites of microfilament attachment.

1987 ◽  
Vol 105 (2) ◽  
pp. 819-831 ◽  
Author(s):  
A A Rogalski
Keyword(s):  
Smooth Muscle ◽  
Plasma Membrane ◽  
Cardiac Muscle ◽  
Cultured Cells ◽  
Molecular Forms ◽  
Cell Coupling ◽  
Membrane Structures ◽  
Adult Chicken ◽  
Attachment Sites ◽  
Membrane Attachment

An integral sialoglycoprotein with Mr approximately 130,000 (Sgp 130) and highest expression in adult chicken gizzard smooth muscle has been recently identified as an excellent candidate for classification as a plasma membrane protein natively associated (directly or indirectly) with actin microfilaments (Rogalski, A.A., and S.J. Singer, 1985, J. Cell Biol., 101:785-801). In this study, the relative in situ distributions of the Sgp 130 integral species (a designation that also includes non-smooth muscle molecular forms) and the peripheral protein, vinculin, have been simultaneously revealed for the first time in selected cultured cells and tissues abundant in microfilament-membrane attachment sites, particularly, smooth and cardiac muscle. Specific antibody probes against Sgp 130 (mouse mAb 30B6) and vinculin (affinity-purified rabbit antibody) were used in double indirect immunofluorescent and immunoelectron microscopic experiments. In contrast to the widespread distributions of vinculin at microfilament-membrane attachment sites, Sgp 130 has been shown to exhibit striking site-specific variation in its abundancy levels in the plasma membrane. Sgp 130 and vinculin were found coincidentally concentrated at focal contact sites in cultured chick embryo fibroblasts and endothelial cells, membrane dense plaques of smooth muscle, and sarcolemma dense plaque sites overlying the Z line in cardiac muscle. However, at the fascia adherens junctional sites of cardiac muscle where vinculin is sharply confined, Sgp 130 was immunologically undetectable in both intact and EGTA-uncoupled tissue. This latter result was confirmed with immunoblotting experiments using isolated forms of the fascia adherens. The double immunolabeling studies of this report establish Sgp 130 as a major integral protein component of nonjunctional membrane dense plaque structures and raise the possibility that the 130-kD integral sialoglycoprotein (Sgp 130) and vinculin assume stable transmembrane associations at these particular microfilament-membrane attachment sites. Nonjunctional dense plaques are further suggested to be a molecularly distinct class of plasma membrane structures rather than a subgroup of adherens junctions. Our data also support a hypothesis that Sgp 130 is involved in plasma membrane force coupling events but not in junctional-related cell-cell coupling.

scholarly journals Pharmacological reactivation of inactive X-linked Mecp2 in cerebral cortical neurons of living mice

2018 ◽  
Vol 115 (31) ◽  
pp. 7991-7996 ◽  
Author(s):  
Piotr Przanowski ◽  
Urszula Wasko ◽  
Zeming Zheng ◽  
Jun Yu ◽  
Robyn Sherman ◽  
...  
Keyword(s):  
X Chromosome ◽  
Cortical Neurons ◽  
Therapeutic Approach ◽  
Cultured Cells ◽  
Genetic Disorder ◽  
Induced Pluripotent Stem Cell ◽  
Branch Points ◽  
Loss Of Function ◽  
Wild Type ◽  
Cerebral Cortical Neurons

Rett syndrome (RTT) is a genetic disorder resulting from a loss-of-function mutation in one copy of the X-linked gene methyl-CpG–binding protein 2 (MECP2). Typical RTT patients are females and, due to random X chromosome inactivation (XCI), ∼50% of cells express mutant MECP2 and the other ∼50% express wild-type MECP2. Cells expressing mutant MECP2 retain a wild-type copy of MECP2 on the inactive X chromosome (Xi), the reactivation of which represents a potential therapeutic approach for RTT. Previous studies have demonstrated reactivation of Xi-linked MECP2 in cultured cells by biological or pharmacological inhibition of factors that promote XCI (called “XCI factors” or “XCIFs”). Whether XCIF inhibitors in living animals can reactivate Xi-linked MECP2 in cerebral cortical neurons, the cell type most therapeutically relevant to RTT, remains to be determined. Here, we show that pharmacological inhibitors targeting XCIFs in the PI3K/AKT and bone morphogenetic protein signaling pathways reactivate Xi-linked MECP2 in cultured mouse fibroblasts and human induced pluripotent stem cell-derived postmitotic RTT neurons. Notably, reactivation of Xi-linked MECP2 corrects characteristic defects of human RTT neurons including reduced soma size and branch points. Most importantly, we show that intracerebroventricular injection of the XCIF inhibitors reactivates Xi-linked Mecp2 in cerebral cortical neurons of adult living mice. In support of these pharmacological results, we also demonstrate genetic reactivation of Xi-linked Mecp2 in cerebral cortical neurons of living mice bearing a homozygous XCIF deletion. Collectively, our results further establish the feasibility of pharmacological reactivation of Xi-linked MECP2 as a therapeutic approach for RTT.

scholarly journals Sciatic nerve-conditioned medium with the addition of Croton blanchetianus Baill essential oil promotes morphological plasticity in spinal cord cultured cells

2021 ◽  
Vol 10 (5) ◽  
pp. e5410514591
Author(s):  
Luciana Cristina Borges Fernandes ◽  
Salvador Viana Gomes Junior ◽  
Ianara Mendonça da Costa ◽  
Francisca Idalina Neta ◽  
Rodrigo Freire Oliveira ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Sciatic Nerve ◽  
Essential Oil ◽  
Conditioned Medium ◽  
Glial Cells ◽  
Cultured Cells ◽  
Morphological Plasticity ◽  
Significant Disabilities ◽  
Spinal Cord Neurons ◽  
Cord Injury

Spinal cord injury is a devastating condition that leads to significant disabilities. The treatment for this problem is a challenge in neuroscience, and it is necessary to combine different strategies to obtain functional recovery outcomes. There are many herbal natural products, such as Croton blanchetianus Baill (CB) essential oil, a Brazilian semi-arid bush with neuroprotective substances tested in regeneration processes and synaptic plasticity. Thus, this study analyzed the cellular plasticity of spinal cord neurons and glial cells in the presence of sciatic nerve-conditioned medium (SNCM) before the addition of CB essential oil. Cell morphology was assessed over 96 hours, and immunocytochemistry analyses were conducted for GFAP, GAP-43 and NeuN. Photomicrographs were made by scanning electron microscopy (SEM). Morphological analysis showed evident trophic development in the groups that received CB essential oil (P>0.000), immunoreactivity for GFAP, GAP-43 and NeuN and the plasticity of these cells were confirmed by SEM. This pioneer study about the plasticity of spinal cord neurons and glial cells opens new possibilities and techniques with essential oils for cell therapy in the presence of SNCM, which promoted neuroprotective action.

Ultra low concentrations of morphine increase neurite outgrowth in cultured rat spinal cord and cerebral cortical neurons

2004 ◽  
Vol 365 (1) ◽  
pp. 10-13 ◽  
Author(s):  
Eugen Brailoiu ◽  
Jennifer Hoard ◽  
G.Cristina Brailoiu ◽  
Michelle Chi ◽  
Ramona Godbolde ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Neurite Outgrowth ◽  
Cortical Neurons ◽  
Rat Spinal Cord ◽  
Low Concentrations ◽  
Cerebral Cortical Neurons

Expression of GAD mRNA in spinal cord neurons of normal and monoarthritic rats

1994 ◽  
Vol 26 (1-2) ◽  
pp. 169-176 ◽  
Author(s):  
J.M. Castro-Lopes ◽  
T.R. Tölle ◽  
B. Pan ◽  
W. Zieglgänsberger
Keyword(s):  
Spinal Cord ◽  
Spinal Cord Neurons

scholarly journals Ketamine decreases neuronally released glutamate via retrograde stimulation of presynaptic adenosine A1 receptors

2021 ◽  
Author(s):  
Vesna Lazarevic ◽  
Yunting Yang ◽  
Ivana Flais ◽  
Per Svenningsson
Keyword(s):  
Cortical Neurons ◽  
Intracellular Signaling ◽  
Ex Vivo ◽  
Forced Swim Test ◽  
Glutamate Release ◽  
Neuronal Cultures ◽  
Extracellular Glutamate ◽  
Primary Neuronal Cultures ◽  
Adenosine A1 Receptors ◽  
Adenosine A1

AbstractKetamine produces a rapid antidepressant response in patients with major depressive disorder (MDD), but the underlying mechanisms appear multifaceted. One hypothesis, proposes that by antagonizing NMDA receptors on GABAergic interneurons, ketamine disinhibits afferens to glutamatergic principal neurons and increases extracellular glutamate levels. However, ketamine seems also to reduce rapid glutamate release at some synapses. Therefore, clinical studies in MDD patients have stressed the need to identify mechanisms whereby ketamine decreases presynaptic activity and glutamate release. In the present study, the effect of ketamine and its antidepressant metabolite, (2R,6R)-HNK, on neuronally derived glutamate release was examined in rodents. We used FAST methodology to measure depolarization-evoked extracellular glutamate levels in vivo in freely moving or anesthetized animals, synaptosomes to detect synaptic recycling ex vivo and primary cortical neurons to perform functional imaging and to examine intracellular signaling in vitro. In all these versatile approaches, ketamine and (2R,6R)-HNK reduced glutamate release in a manner which could be blocked by AMPA receptor antagonism. Antagonism of adenosine A1 receptors, which are almost exclusively expressed at nerve terminals, also counteracted ketamine’s effect on glutamate release and presynaptic activity. Signal transduction studies in primary neuronal cultures demonstrated that ketamine reduced P-T286-CamKII and P-S9-Synapsin, which correlated with decreased synaptic vesicle recycling. Moreover, systemic administration of A1R antagonist counteracted the antidepressant-like actions of ketamine and (2R,6R)-HNK in the forced swim test. To conclude, by studying neuronally released glutamate, we identified a novel retrograde adenosinergic feedback mechanism that mediate inhibitory actions of ketamine on glutamate release that may contribute to its rapid antidepressant action.

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