Abstract:
:Neurocatin, a neuroregulatory factor isolated from mammalian brain, is a powerful affector of protein phosphorylation in rat striatal synaptosomes. Two major synaptosomal phosphoproteins of approximately 80 and approximately 60 kDa, possibly synapsin I and tyrosine hydroxylase, were especially sensitive to neurocatin. Immunoprecipitation experiments confirmed that the 60-kDa protein is the enzyme tyrosine hydroxylase. At low concentrations of neurocatin (to approximately 7.5 ng/100 microliters of suspension), incorporation of 32P orthophosphate into these proteins increased with increasing neurocatin concentration. At 7.5 ng of neurocatin, incorporation of the label into the two proteins increased by 22 and 26%, respectively. Concentrations of neurocatin > 7.5 ng/100 microliters caused progressive decrease in incorporation of 32P into many synaptosomal proteins; by a concentration of neurocatin of approximately 45 ng/100 microliters, the level of 32P incorporation into many proteins was < or = 70% of control. The effects of neurocatin on synaptosomal protein phosphorylation were also dependent on the time of incubation. At a constant concentration of approximately 7.5 ng/100 microliters of neurocatin, increased incorporation of 32P into many proteins was measurable within 0.5 min and was maximal by 1 min. Incubation times > 2.0 min, showed progressive decrease in 32P incorporation. Removing extrasynaptosomal Ca2+ with EGTA attenuated the increased 32P incorporation induced by low neurocatin concentrations, suggesting that calcium plays a role in neurocatin-induced phosphorylation of rat striatal synaptosomal proteins. The reduced incorporation of label induced by high neurocatin concentrations, however, was not calcium dependent. The effects of neurocatin on the level of 32P incorporation into proteins were observed only in intact synaptosomes, consistent with this compound acting through receptors on the plasma membrane.
journal_name
J Neurochemjournal_title
Journal of neurochemistryauthors
Yee DK,Pastuszko A,Wilson DFdoi
10.1111/j.1471-4159.1993.tb03280.xsubject
Has Abstractpub_date
1993-04-01 00:00:00pages
1220-7issue
4eissn
0022-3042issn
1471-4159journal_volume
60pub_type
杂志文章abstract::This article reports the results of a systematic investigation of the different types of antibodies produced in the course of a long-term immunization of rats with mouse nerve growth factor (NGF). We have characterized three types of monoclonal antibodies, namely: (1) antibodies that bind to NGF and inhibit its bindin...
journal_title:Journal of neurochemistry
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doi:10.1111/j.1471-4159.1988.tb10565.x
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journal_title:Journal of neurochemistry
pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:2011-05-01 00:00:00
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journal_title:Journal of neurochemistry
pub_type: 杂志文章
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journal_title:Journal of neurochemistry
pub_type: 杂志文章
doi:10.1111/j.1471-4159.1993.tb03290.x
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pub_type: 杂志文章
doi:10.1111/j.1471-4159.1991.tb08312.x
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pub_type: 杂志文章
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更新日期:2010-06-01 00:00:00
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journal_title:Journal of neurochemistry
pub_type: 杂志文章
doi:10.1111/j.1471-4159.1991.tb03474.x
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journal_title:Journal of neurochemistry
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journal_title:Journal of neurochemistry
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doi:10.1046/j.1471-4159.1994.62062224.x
更新日期:1994-06-01 00:00:00