Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
2002-8-5
pubmed:abstractText
Although unesterified long chain fatty acids interact with peroxisome proliferator-activated receptors to initiate transcription within the nucleus, almost nothing is known regarding factors regulating long chain fatty acid distribution to the nucleus of living cells. The possibility that the liver fatty acid-binding protein (L-FABP) may function in this role was addressed in transfected L-cell fibroblasts overexpressing L-FABP using a series of fluorescent fatty acids differing in chain length and unsaturation. After 30 min of incubation, oxidation of BODIPY-, NBD-, and cis-parinaric acids was undetectable in L-cells. Likewise, L-cells very poorly esterified these fluorescent fatty acids in the following order: 0% BODIPY-C5, NBD-C6 (short chain length) < 0-3% NBD-C18, BODIPY-C16, cis-parinaric acid (long chain length) < 11% BODIPY-C12 (medium chain length). Real time confocal and multiphoton laser scanning microscopy (CLSM and MPLSM) showed that these fluorescent fatty acids were generally taken up in the following order: long chain (BODIPY-C16, NBD-C18) > medium chain (BODIPY-C12) short chain (BODIPY-C5, NBD-C6). The fluorescent fatty acids were imaged in the nucleus, primarily associated with the nuclear envelope, at levels about 2-3-fold lower than outside the nucleus. CLSM and MPLSM showed that L-FABP expression enhanced by 2-4-fold the initial rate and/or average maximal uptake of the long and medium chain but not the short chain fluorescent fatty acids in living cells. Furthermore, L-FABP expression increased the targeting of long and medium but not short chain fluorescent fatty acids to the nucleus by 2.9-4.4-fold and increased the proportion (i.e. nuclear:cytoplasm ratio) of medium and long chain but not short chain fatty acids by 2-3.6-fold. In summary, these results showed for the first time the presence of unesterified fatty acids in the nucleus of living cells and demonstrated that expression of a fatty acid-binding protein, L-FABP, specifically enhanced uptake and intracellular targeting of long and medium chain fatty acids to the nucleus.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29139-51
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12023965-Active Transport, Cell Nucleus, pubmed-meshheading:12023965-Animals, pubmed-meshheading:12023965-Carrier Proteins, pubmed-meshheading:12023965-Cell Nucleus, pubmed-meshheading:12023965-Chromatography, Thin Layer, pubmed-meshheading:12023965-Cytoplasm, pubmed-meshheading:12023965-DNA, Complementary, pubmed-meshheading:12023965-Fatty Acid-Binding Proteins, pubmed-meshheading:12023965-Fatty Acids, pubmed-meshheading:12023965-Fibroblasts, pubmed-meshheading:12023965-Liver, pubmed-meshheading:12023965-Mice, pubmed-meshheading:12023965-Microscopy, Confocal, pubmed-meshheading:12023965-Microscopy, Fluorescence, pubmed-meshheading:12023965-Models, Chemical, pubmed-meshheading:12023965-Neoplasm Proteins, pubmed-meshheading:12023965-Nerve Tissue Proteins, pubmed-meshheading:12023965-Phospholipids, pubmed-meshheading:12023965-Protein Binding, pubmed-meshheading:12023965-Time Factors, pubmed-meshheading:12023965-Transcription, Genetic, pubmed-meshheading:12023965-Transfection
pubmed:year
2002
pubmed:articleTitle
Liver fatty acid-binding protein targets fatty acids to the nucleus. Real time confocal and multiphoton fluorescence imaging in living cells.
pubmed:affiliation
Department of Pathobiology, Texas A&M University, College Station, Texas 77843-4466, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.