Neuroscience. 2008 Feb 6;151(3):671-9. Epub 2007 Nov 17.
The vanadium (IV) compound rescues septo-hippocampal cholinergic neurons from neurodegeneration in olfactory bulbectomized mice.
Han F, Shioda N, Moriguchi S, Qin ZH, Fukunaga K.
Source
Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Tohoku University, Aramaki-Aoba Aoba-ku, Sendai 980-8578, Japan.
Abstract
The bilateral olfactory bulbectomy (OBX) mouse exhibits neurodegeneration of cholinergic neurons in the medial septum with concomitant cognitive deficits. Consistent with our previous observations, choline acetyltransferase (ChAT) protein levels in the medial septum decreased by 43.5% 2 weeks after OBX without changes in glutamic acid decarboxylase-65 (GAD65) levels. Interestingly, levels of the vesicular acetylcholine transporter (VAChT), which is localized at cholinergic neuron terminals, decreased both in hippocampal CA1 and CA3 regions following OBX. Confocal microscopy showed that VAChT expression was more severely reduced in CA3 14 days after OBX compared with CA1. Intriguingly, chronic treatment with a vanadium (IV) compound, VO(OPT) [bis(1-N-oxide-pyridine-2-thiolato)oxovanadium(IV)] (0.5-1 mg as vanadium (V)/kg/day, i.p.), significantly rescued cholinergic neurons in the medial septum in a dose-dependent manner. VO(OPT) treatment also prevented decreased VAChT immunoreactivity both in CA1 and CA3 regions in the hippocampus. Consistent with these findings, an impaired hippocampal long-term potentiation (LTP) and memory deficits seen in OBX mice were significantly prevented by VO(OPT) treatment. Taken together, OBX induces neurodegeneration of septo-hippocampal cholinergic neurons and impairment of memory-related behaviors. The neuroprotective effect of VO(OPT) could lead to novel therapeutic strategies to ameliorate cognitive deficits associated with cholinergic neuron degeneration in Alzheimer's disease and other neurodegenerative disorders.
PMID:
18164824
[PubMed - indexed for MEDLINE]
Mitä on vanadiini(IV)?
http://en.wikipedia.org/wiki/Vanadium%28IV%29_oxide
http://www.ncbi.nlm.nih.gov/pubmed/19029487
Vanadinium(V) katsotaan hivenaineeksi.
http://www.healthy-vitamin-choice.com/vanadium.html
Visar inlägg med etikett Asetylkoliinerginen neuronijärjestelmä. Visa alla inlägg
Visar inlägg med etikett Asetylkoliinerginen neuronijärjestelmä. Visa alla inlägg
söndag 17 juli 2011
Asetylkolinergiset reseptorit
http://jn.physiology.org/content/90/3/1956/F7.expansion.html
Kaavakuva kolinergisistä reseptoreista ja solunsisäisistä aktiivin kalsiumjonin varastoista, mitkä säätelevät Ca++ jonin sisänmenoa ja vapautumista koe-eläimen sydämensisäisessä neuronissa.
Schematic diagram of the cholinergic receptors and intracellular Ca2+ stores mediating Ca2+ entry and release in rat intracardiac neurons.
Agonistin sitoutuminen kolinergiseen nikotiini(n) tai muskariini (m) reseptoriin saattaa mobilisoida aktiivia kalsiumjonia stimuloimalla joko sen sisäänpääsyä tai vastaavasti vapautumista solunsisäisistä varastoista .
Agonist binding to n- and mAChRs may mobilize Ca2+ by stimulating either Ca2+ entry or Ca2+ release from intracellular stores, respectively.
Kolinergisten nikotiinireseptoreitten aktivaatio stimuloi aktiivien kalsiumjonien sisäänvirtausta avointen nikotiini(AK) reseptoreitten kanavien kautta ja edistää CICR ryadiinisensitiivisistä kalsium Ca++ varastoista.
Activation of nAChRs stimulates Ca2+ influx via the open nAChR channel and promotes CICR from ryanodine-sensitive Ca2+ stores.
G-proteiinivälitteisesti fosfolipaasiin (PLC) kytkettyjen Muskariininkaltaisten AK- reseptoreitten aktivaatio hydrolysoi PIP2 ja siitä tuottuu DAG ja IP3 sekundäärivälittäjäaineita. IP3 toimii välittäjänä, missä ER aitiosta käsin vapautuu aktiivia kalsiumjonia.Kohonnut sytoplasminen kalsiumjonipitoisuus taas aktivoi kalsiumista riippuvia kaliumkanavia minkä jälkeen kalsiumia pursuu plasmamembraanin läpi ja sitä kertyy mitokondrioihin tai endoplasmiseen retikulumin aitioihin Ca++ ATPaasi pumpun avulla.
Activation of mAChRs coupled by a G protein to phospholipase C (PLC) hydrolysis of phosphotidylinositol-4,5-bisphosphate (PIP2) yielding diacylglycerol (DAG) and IP3. IP3 serves as mediator of Ca2+ release from a compartment of the endoplasmatic reticulum (ER). Elevated cytoplasmic [Ca2+] activates Ca2+-dependent K+ channels (KCa) before being extruded across the plasma membrane and sequestered into the mitochondria or into the ER compartments via a Ca2+-ATPase pump.
Kaavakuva kolinergisistä reseptoreista ja solunsisäisistä aktiivin kalsiumjonin varastoista, mitkä säätelevät Ca++ jonin sisänmenoa ja vapautumista koe-eläimen sydämensisäisessä neuronissa.
Schematic diagram of the cholinergic receptors and intracellular Ca2+ stores mediating Ca2+ entry and release in rat intracardiac neurons.
Agonistin sitoutuminen kolinergiseen nikotiini(n) tai muskariini (m) reseptoriin saattaa mobilisoida aktiivia kalsiumjonia stimuloimalla joko sen sisäänpääsyä tai vastaavasti vapautumista solunsisäisistä varastoista .
Agonist binding to n- and mAChRs may mobilize Ca2+ by stimulating either Ca2+ entry or Ca2+ release from intracellular stores, respectively.
Kolinergisten nikotiinireseptoreitten aktivaatio stimuloi aktiivien kalsiumjonien sisäänvirtausta avointen nikotiini(AK) reseptoreitten kanavien kautta ja edistää CICR ryadiinisensitiivisistä kalsium Ca++ varastoista.
Activation of nAChRs stimulates Ca2+ influx via the open nAChR channel and promotes CICR from ryanodine-sensitive Ca2+ stores.
G-proteiinivälitteisesti fosfolipaasiin (PLC) kytkettyjen Muskariininkaltaisten AK- reseptoreitten aktivaatio hydrolysoi PIP2 ja siitä tuottuu DAG ja IP3 sekundäärivälittäjäaineita. IP3 toimii välittäjänä, missä ER aitiosta käsin vapautuu aktiivia kalsiumjonia.Kohonnut sytoplasminen kalsiumjonipitoisuus taas aktivoi kalsiumista riippuvia kaliumkanavia minkä jälkeen kalsiumia pursuu plasmamembraanin läpi ja sitä kertyy mitokondrioihin tai endoplasmiseen retikulumin aitioihin Ca++ ATPaasi pumpun avulla.
Activation of mAChRs coupled by a G protein to phospholipase C (PLC) hydrolysis of phosphotidylinositol-4,5-bisphosphate (PIP2) yielding diacylglycerol (DAG) and IP3. IP3 serves as mediator of Ca2+ release from a compartment of the endoplasmatic reticulum (ER). Elevated cytoplasmic [Ca2+] activates Ca2+-dependent K+ channels (KCa) before being extruded across the plasma membrane and sequestered into the mitochondria or into the ER compartments via a Ca2+-ATPase pump.
lördag 16 juli 2011
Koliinierginen hermojärjestelmä
Cholinergic nerve terminals
July 16, 2011
eJ Comp Neurol. 2003 Jun 9;460(4):476-86.
Large cholinergic nerve terminals on subsets of motoneurons and their relation to muscarinic receptor type 2.
Hellström J, Oliveira AL, Meister B, Cullheim S.
SourceDepartment of Neuroscience, The Retzius Laboratory, Karolinska Institutet, SE-171 77 Stockholm, Sweden. johan.hellstrom@neuro.ki.se
Abstract
The cholinergic C-bouton is a large nerve terminal found exclusively apposing motoneuron cell somata and proximal dendrites. The origin and function of the C-bouton is not known. An antiserum against the vesicular acetylcholine transporter was used to identify large cholinergic nerve terminals putatively of the C-type in close apposition to motoneuron cell somata. This type of nerve terminal was present in the rat spinal cord ventral horn, but only in some cranial motor nuclei. Fluoro-Gold tracing showed that subsets of spinal motoneuron cell somata were contacted by different numbers of putative C-boutons. Thus, motoneurons innervating an intrinsic foot muscle were contacted by about half the number of cholinergic terminals found on motoneurons of the predominantly fast-twitch gastrocnemius muscle. Slow-twitch soleus motoneurons showed an intermediate innervation. There was a strong correlation between the presence of putative C-boutons and muscarinic receptor 2 (m2)-like immunoreactivity (-LI) within a motor nucleus. By using confocal laser microscopy, the m2-LI appeared to be confined to the motoneuron cell membrane and strongly enriched beneath the C-type nerve terminal. Thus, our results suggested a differential distribution of large cholinergic C-boutons, depending on motoneuron type, and that the presence of this nerve terminal type is associated with m2-LI in the postsynaptic membrane.
Copyright 2003 Wiley-Liss, Inc.
PMID: 12717708 [PubMed - indexed for MEDLINE]
Posted by Lea Bright
July 16, 2011
eJ Comp Neurol. 2003 Jun 9;460(4):476-86.
Large cholinergic nerve terminals on subsets of motoneurons and their relation to muscarinic receptor type 2.
Hellström J, Oliveira AL, Meister B, Cullheim S.
SourceDepartment of Neuroscience, The Retzius Laboratory, Karolinska Institutet, SE-171 77 Stockholm, Sweden. johan.hellstrom@neuro.ki.se
Abstract
The cholinergic C-bouton is a large nerve terminal found exclusively apposing motoneuron cell somata and proximal dendrites. The origin and function of the C-bouton is not known. An antiserum against the vesicular acetylcholine transporter was used to identify large cholinergic nerve terminals putatively of the C-type in close apposition to motoneuron cell somata. This type of nerve terminal was present in the rat spinal cord ventral horn, but only in some cranial motor nuclei. Fluoro-Gold tracing showed that subsets of spinal motoneuron cell somata were contacted by different numbers of putative C-boutons. Thus, motoneurons innervating an intrinsic foot muscle were contacted by about half the number of cholinergic terminals found on motoneurons of the predominantly fast-twitch gastrocnemius muscle. Slow-twitch soleus motoneurons showed an intermediate innervation. There was a strong correlation between the presence of putative C-boutons and muscarinic receptor 2 (m2)-like immunoreactivity (-LI) within a motor nucleus. By using confocal laser microscopy, the m2-LI appeared to be confined to the motoneuron cell membrane and strongly enriched beneath the C-type nerve terminal. Thus, our results suggested a differential distribution of large cholinergic C-boutons, depending on motoneuron type, and that the presence of this nerve terminal type is associated with m2-LI in the postsynaptic membrane.
Copyright 2003 Wiley-Liss, Inc.
PMID: 12717708 [PubMed - indexed for MEDLINE]
Posted by Lea Bright
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