Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-12-17
pubmed:abstractText
Axonal maturation in situ is accompanied by the transition of neurofilaments (NFs) comprised of only NF-M and NF-L to those also containing NF-H. Since NF-H participates in interactions of NFs with each other and with other cytoskeletal constituents, its appearance represents a critical event in the stabilization of axons that accompanies their maturation. Whether this transition is effected by replacement of "doublet" NFs with "triplet" NFs, or by incorporation of NF-H into existing doublet NFs is unclear. To address this issue, we examined the distribution of NF subunit immunoreactivity within axonal cytoskeletons of differentiated NB2a/d1 cell and DRG neurons between days 3-7 of outgrowth. Endogenous immunoreactivity either declined in a proximal-distal gradient or was relatively uniform along axons. This distribution was paralleled by microinjected biotinylated NF-L. By contrast, biotinylated NF-H displayed a bipolar distribution, with immunoreactivity concentrated within the proximal- and distal-most axonal regions. Proximal biotinylated NF-H accumulation paralleled that of endogenous NF immunoreactivity; however, distal-most biotinylated NF-H accumulation dramatically exceeded that of endogenous NFs and microinjected NF-L. This phenomenon was not due to co-polymerization of biotin-H with vimentin or alpha-internexin. This phenomenon declined with continued time in culture. These data suggest that NF-H can incorporate into existing cytoskeletal structures, and therefore suggest that this mechanism accounts for at least a portion of the accumulation of triplet NFs during axonal maturation. Selective NF-H accumulation into existing cytoskeletal structures within the distal-most region may provide de novo cytoskeletal stability for continued axon extension and/or stabilization.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0886-1544
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-12
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11746668-Animals, pubmed-meshheading:11746668-Axons, pubmed-meshheading:11746668-Biotinylation, pubmed-meshheading:11746668-Carrier Proteins, pubmed-meshheading:11746668-Cattle, pubmed-meshheading:11746668-Cell Differentiation, pubmed-meshheading:11746668-Cell Division, pubmed-meshheading:11746668-Densitometry, pubmed-meshheading:11746668-HSC70 Heat-Shock Proteins, pubmed-meshheading:11746668-Humans, pubmed-meshheading:11746668-Intermediate Filament Proteins, pubmed-meshheading:11746668-Microscopy, Fluorescence, pubmed-meshheading:11746668-Microscopy, Immunoelectron, pubmed-meshheading:11746668-Neurofilament Proteins, pubmed-meshheading:11746668-Neurons, pubmed-meshheading:11746668-Proteins, pubmed-meshheading:11746668-Spinal Cord, pubmed-meshheading:11746668-Time Factors, pubmed-meshheading:11746668-Tumor Cells, Cultured, pubmed-meshheading:11746668-Vimentin
pubmed:year
2001
pubmed:articleTitle
Selective accumulation of the high molecular weight neurofilament subunit within the distal region of growing axonal neurites.
pubmed:affiliation
Center for Cellular Neurobiology and Neurodegeneration Research, Department of Biological Sciences, University of Massachusetts-Lowell, MA 01854, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.