Linked Life Data

15035630

Source:http://linkedlifedata.com/resource/pubmed/id/15035630

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2004-3-23
pubmed:abstractText
Intestinal fatty acid binding protein (IFABP) and liver FABP (LFABP), homologous proteins expressed at high levels in intestinal absorptive cells, employ markedly different mechanisms for the transfer of fatty acids (FAs) to acceptor membranes. Transfer from IFABP occurs during protein-membrane collisional interactions, while for LFABP, transfer occurs by diffusion through the aqueous phase. Earlier, we had shown that the helical domain of IFABP is critical in determining its collisional FA transfer mechanism. In the study presented here, we have engineered a pair of chimeric proteins, one with the "body" (ligand binding domain) of IFABP and the alpha-helical region of LFABP (alphaLbetaIFABP) and the other with the ligand binding pocket of LFABP and the helical domain of IFABP (alphaIbetaLFABP). The objective of this work was to determine whether the change in the alpha-helical domain of each FABP would alter the rate and mechanism of transfer of FA from the chimeric proteins in comparison with those of the wild-type proteins. The fatty acid transfer properties of the FABP chimeras were examined using a fluorescence resonance transfer assay. The results showed a significant modification of the absolute rate of FA transfer from the chimeric proteins compared to that of the wild type, indicating that the slower rate of FA transfer observed for wild-type LFABP relative to that of wild-type IFABP is, in part, determined by the helical domain of the proteins. In addition to these quantitative changes, it was of great interest to observe that the apparent mechanism of FA transfer also changed when the alpha-helical domain was exchanged, with transfer from alphaLbetaIFABP occurring by aqueous diffusion and transfer from alphaIbetaLFABP occurring via protein-membrane collisional interactions. These results demonstrate that the alpha-helical region of LFABP is responsible for its diffusional mechanism of fatty acid transfer to membranes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3600-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15035630-Animals, pubmed-meshheading:15035630-Biological Transport, pubmed-meshheading:15035630-Carrier Proteins, pubmed-meshheading:15035630-Chemistry, Physical, pubmed-meshheading:15035630-Circular Dichroism, pubmed-meshheading:15035630-Diffusion, pubmed-meshheading:15035630-Fatty Acid-Binding Proteins, pubmed-meshheading:15035630-Helix-Turn-Helix Motifs, pubmed-meshheading:15035630-Liver, pubmed-meshheading:15035630-Membranes, Artificial, pubmed-meshheading:15035630-Osmolar Concentration, pubmed-meshheading:15035630-Phospholipids, pubmed-meshheading:15035630-Physicochemical Phenomena, pubmed-meshheading:15035630-Protein Binding, pubmed-meshheading:15035630-Protein Structure, Secondary, pubmed-meshheading:15035630-Protein Structure, Tertiary, pubmed-meshheading:15035630-Rats, pubmed-meshheading:15035630-Recombinant Fusion Proteins, pubmed-meshheading:15035630-Spectrometry, Fluorescence, pubmed-meshheading:15035630-Stearic Acids
pubmed:year
2004
pubmed:articleTitle
The alpha-helical domain of liver fatty acid binding protein is responsible for the diffusion-mediated transfer of fatty acids to phospholipid membranes.
pubmed:affiliation
Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CONICET-UNLP, Facultad de Ciencias Médicas, calles 60 y 120, 1900 La Plata, Argentina. bcorsico@atlas.med.unlp.edu.ar
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.