Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-10-11
pubmed:abstractText
Intracellular transport of the sphingolipids glucosylceramide (GlcCer) and sphingomyelin (SM), was examined in HT29 human colon adenocarcinoma cells. After synthesis from a fluorescent precursor, 6-[N-(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]hexanoylceramide++ + (C6-NBD-Cer), transfer of SM from the Golgi complex to the plasma membrane can occur independently of that of GlcCer, as revealed by temperature-dependent experiments. Thus, at 20 degrees C, SM trafficking to the cell surface is essentially unaffected, whereas GlcCer transport to the plasma membrane is inhibited by approximately 75%, when compared to the transfer of both lipids at 37 degrees C. The mechanism by which SM and GlcCer are transported to the cell surface involves at least in part a vesicular mechanism. Transport vesicles, containing both lipids at their luminal surface, as revealed by the inaccessibility of the NBD fluorescence to the quencher sodium dithionite, have been isolated from cells, permeabilized by filter stripping. As evidenced by electron microscopic and biochemical criteria, no vesicles or lipids were released when cell permeabilization had been carried out with streptolysin. Density gradient analysis indicates the potential existence of several vesicle populations, distinctly enriched in either lipid, involved in transport of sphingolipids to the plasma membrane in HT29 cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0171-9335
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
172-81
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Transport of biosynthetic sphingolipids from Golgi to plasma membrane in HT29 cells: involvement of different carrier vesicle populations.
pubmed:affiliation
Laboratory of Physiological Chemistry, University of Groningen, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't