Abstract：
:Carnitine is known to accumulate in brain, therefore transport of carnitine through the blood-brain barrier was studied in an in vitro system using bovine brain capillary endothelial cells (BBCEC) grown on filter inserts in a co-culture system with glial cells. Long-term exposure of BBCEC to carnitine resulted in a high accumulation of long-chain acyl carnitines, which decreased dramatically upon removal of carnitine. Kinetic analysis of carnitine accumulation indicated a possibility of functioning of more than one transporter. BBCEC were incubated in the presence of substrates and inhibitors of known carnitine transporters added from either apical or basolateral side. Inhibition by replacement of sodium and expression of OCTN2 (RT-PCR) were in agreement with earlier reports on the functioning of OCTN2 in apical membrane. For the first time, functioning of OCTN2 was demonstrated in the basolateral membrane, as well as functioning in both membranes of a low affinity carnitine transporter B(0,+). Expression of B(0,+) in BBCEC was confirmed by RT-PCR. These results suggest that OCTN2 and B(0,+) could be involved in carnitine transport in both the apical and basolateral membrane.
journal_name
J Neurochemjournal_title
Journal of neurochemistryauthors
Berezowski V,Miecz D,Marszałek M,Bröer A,Bröer S,Cecchelli R,Nałecz KAdoi
10.1111/j.1471-4159.2004.02752.xkeywords:
subject
Has Abstractpub_date
2004-11-01 00:00:00pages
860-72issue
4eissn
0022-3042issn
1471-4159pii
JNC2752journal_volume
91pub_type
杂志文章abstract：:Parkinson's disease (PD) motor symptoms are caused by degeneration of nigrostriatal dopaminergic (DAergic) neurons. The most common causes of hereditary PD are mutations in the PARKIN gene. The ubiquitin ligase parkin has been shown to mediate neuroprotection in cell culture and in vivo, but the molecular mechanisms a...
journal_title：Journal of neurochemistry
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journal_title：Journal of neurochemistry
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doi：10.1111/j.1471-4159.1992.tb08465.x
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journal_title：Journal of neurochemistry
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journal_title：Journal of neurochemistry
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doi：10.1111/j.1471-4159.1987.tb01001.x
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journal_title：Journal of neurochemistry
pub_type： 杂志文章
doi：10.1111/j.1471-4159.1981.tb00571.x
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pub_type： 杂志文章
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journal_title：Journal of neurochemistry
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journal_title：Journal of neurochemistry
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更新日期：2012-08-01 00:00:00
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更新日期：2018-01-01 00:00:00
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pub_type： 杂志文章
doi：10.1046/j.1471-4159.1998.70041346.x
更新日期：1998-04-01 00:00:00
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journal_title：Journal of neurochemistry
pub_type： 杂志文章
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更新日期：2014-06-01 00:00:00
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pub_type： 杂志文章
doi：10.1046/j.1471-4159.2003.02178.x
更新日期：2004-01-01 00:00:00
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journal_title：Journal of neurochemistry
pub_type： 杂志文章
doi：10.1111/jnc.12192
更新日期：2013-05-01 00:00:00
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journal_title：Journal of neurochemistry
pub_type： 杂志文章
doi：10.1111/j.1471-4159.1985.tb04007.x
更新日期：1985-08-01 00:00:00
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journal_title：Journal of neurochemistry
pub_type： 杂志文章
doi：10.1111/j.1471-4159.1993.tb02182.x
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更新日期：2017-07-01 00:00:00
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pub_type： 杂志文章
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pub_type： 杂志文章
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journal_title：Journal of neurochemistry
pub_type： 杂志文章
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更新日期：1996-08-01 00:00:00
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journal_title：Journal of neurochemistry
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更新日期：2010-05-01 00:00:00
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journal_title：Journal of neurochemistry
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doi：10.1111/j.1471-4159.1993.tb07446.x
更新日期：1993-12-01 00:00:00
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journal_title：Journal of neurochemistry
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doi：10.1111/j.1471-4159.1985.tb08803.x
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abstract：:The parenteral administration of L-phenylalanine or p-tyrosine increases the mouse striatal concentration of p-tyramine, an effect that is enhanced by monoamine oxidase inhibition and reduced by an L-aromatic aminoacid decarboxylase inhibitor. Striatal m-tyramine was increased following administration of L-phenylalani...
journal_title：Journal of neurochemistry
pub_type： 杂志文章
doi：10.1111/j.1471-4159.1982.tb07971.x
更新日期：1982-09-01 00:00:00
abstract：:Tissue plasminogen activator (tPA) is necessary for hippocampal long-term potentiation. Synaptically released zinc also contributes to long-term potentiation, especially in the hippocampal CA3 region. Using cortical cultures, we examined whether zinc increased the concentration and/or activity of tPA. Two hours after ...
journal_title：Journal of neurochemistry
pub_type： 杂志文章
doi：10.1111/j.1471-4159.2011.07322.x
更新日期：2011-09-01 00:00:00
abstract：:The normal cellular prion protein (PrP(C)) is a glycoprotein with two highly conserved potential N-linked glycosylation sites. All prion diseases, whether inherited, infectious or sporadic, are believed to share the same pathogenic mechanism that is based on the conversion of the normal cellular prion protein (PrP(C))...
journal_title：Journal of neurochemistry
pub_type： 杂志文章
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更新日期：2007-02-01 00:00:00
abstract：:Neuronal nicotinic acetylcholine receptors labelled with tritiated agonists are reduced in the cerebral cortex in Alzheimer's disease (AD), but to date it has not been demonstrated which nicotinic receptor subunits contribute to this deficit. In the present study, autopsy tissue from the temporal cortex of 14 AD cases...
journal_title：Journal of neurochemistry
pub_type： 杂志文章
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更新日期：1999-10-01 00:00:00
