Document Detail


Protein synthesis within dendrites: glycosylation of newly synthesized proteins in dendrites of hippocampal neurons in culture.
MedLine Citation:
PMID:  8815879     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
There is increasing evidence that certain mRNAs are present in dendrites and can be translated there. The present study uses two strategies to evaluate whether dendrites also possess the machinery for protein glycosylation. First, precursor labeling techniques were used to conjunction with autoradiography to visualize glycosyltransferase activities that are characteristic of the rough endoplasmic reticulum (RER) (mannose) or the Golgi apparatus (GA) (galactose and fucose) in dendrites that had been separated from their cell bodies and in intact neurons treated with brefeldin A or low temperature. Second, immunocytochemical techniques were used to define the subcellular distribution of proteins that are considered markers of the RER (ribophorin I) and GA (p58, alpha-mannosidase II, galactosyltransferase, and TGN38/41). Autoradiographic analysis revealed that isolated dendrites incorporated sugar precursors in a tunicamycin-sensitive and protein synthesis-dependent manner. Moreover, when intact neurons were pulse-labeled with 3H-labeled sugars at low temperature or after treatment with brefeldin A, labeling was distributed over proximal and sometimes distal dendrites. Immunolabeling for RER markers was predominantly localized in cell bodies but extended for a considerable distance into dendrites of all neurons. Immunolabeling for GA markers was confined to the cell body in approximately 70% of the neurons, but in 30% of the neurons, the staining extended into proximal and middle dendrites. These results indicate that the machinery for glycosylation extends well into dendrites in many neurons.
Authors:
E R Torre; O Steward
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of neuroscience : the official journal of the Society for Neuroscience     Volume:  16     ISSN:  0270-6474     ISO Abbreviation:  J. Neurosci.     Publication Date:  1996 Oct 
Date Detail:
Created Date:  1996-12-06     Completed Date:  1996-12-06     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8102140     Medline TA:  J Neurosci     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  5967-78     Citation Subset:  IM    
Affiliation:
Department of Neuroscience, University of Virginia School of Medicine, Charlottesville 22908, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Brefeldin A
Carbohydrate Metabolism
Cells, Cultured
Cyclopentanes / pharmacology
Dendrites / metabolism*
Endoplasmic Reticulum, Rough / metabolism
Glycosylation
Golgi Apparatus / metabolism
Hippocampus / cytology,  metabolism*
Immunohistochemistry
Nerve Tissue Proteins / biosynthesis*
Neurons / drug effects,  metabolism*
Protein Synthesis Inhibitors / pharmacology
Rats / embryology
Temperature
Tissue Distribution
Grant Support
ID/Acronym/Agency:
NS 12333/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/Cyclopentanes; 0/Nerve Tissue Proteins; 0/Protein Synthesis Inhibitors; 20350-15-6/Brefeldin A

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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