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A functional analysis of enterocyte fatty acid-binding proteins

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TypeOfResource
Text
TitleInfo (ID = T-1)
Title
A functional analysis of enterocyte fatty acid-binding proteins
SubTitle
PartName
PartNumber
NonSort
Identifier (displayLabel = ); (invalid = )
ETD_1966
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.000051851
Language (objectPart = )
LanguageTerm (authority = ISO639-2); (type = code)
eng
Genre (authority = marcgt)
theses
Subject (ID = SBJ-1); (authority = RUETD)
Topic
Nutritional Sciences
Subject (ID = SBJ-2); (authority = ETD-LCSH)
Topic
Fatty acid-binding proteins
Abstract
Intestinal- and liver- fatty acid-binding proteins (IFABP and LFABP, respectively) are expressed at high levels in mammalian small intestinal enterocytes and bind the major products of dietary triacylglycerol (TG) digestion. The precise role of FABPs in processing these diet-derived lipids is unknown. We investigated the acute metabolism of fatty acids and monoacylglycerol in fasted WT and FABP-/- in small intestinal mucosa in vivo. Two minutes after intraduodenal administration of [14C]oleate or [3H]monoolein, mucosal radioactivity was recovered primarily in TG. Recovery of [14C]oleate in TG relative to phospholipids (PL) was significantly reduced in IFABP-/- mice. No changes were found in the expression of lipid synthetic genes, suggesting a non-transcriptional, trafficking defect. Recovery of [14C]oleate in lipid fractions was unaffected by LFABP ablation, although significantly less was oxidized. Oxidative capacity was unchanged in LFABP-/- intestinal mucosa homogenates, suggesting LFABP may target fatty acids toward catabolic fates. Incorporation of [3H]monoolein into TG relative to PL was markedly reduced in LFABP-/- despite no changes in the expression of lipid synthetic genes. While those results suggest a trafficking defect, reports on the binding of monoacylglycerol by LFABP are mixed. Therefore, the monoacylglycerol -binding capability of liver cytosol from wild-type and LFABP-/- mice was assessed by gel filtration chromatography. The [14C]oleate associated with ~14kDa proteins was absent in LFABP-/- liver cytosol. Interestingly, [3H]monoolein was present in the ~14kDa fractions from WT but not LFABP-/- cytosol. Immunoblotting confirmed the presence of LFABP in the ~14kDa fractions from WT, but not LFABP-/-. These results suggest that LFABP is a monoacylglycerol-binding protein in a physiological setting.
The systemic effects of enterocyte FABP deletion were examined by comparing body composition via dual energy X-ray absorptiometry and energy metabolism via indirect calorimetry. During food deprivation, IFABP-/- mice lost more fat mass and, accordingly, had a lower respiratory quotient than WT. LFABP-/- mice lost less fat-free mass and maintained a higher level of energy expenditure relative to WT. These findings suggest that ablation of enterocyte FABPs manifest specific cellular effects in their native tissues due to lipid trafficking defects, as well as systemic effects.
PhysicalDescription
Form (authority = gmd)
electronic resource
Extent
ix, 162 p. : ill.
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application/pdf
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text/xml
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references (p. 149-161)
Note (type = statement of responsibility)
by William Stacy Lagakos
Name (ID = NAME-1); (type = personal)
NamePart (type = family)
Lagakos
NamePart (type = given)
William Stacy
NamePart (type = date)
1979-
Role
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author
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William Stacy Lagakos
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NamePart (type = family)
Storch
NamePart (type = given)
Judith
Role
RoleTerm (authority = RULIB); (type = )
chair
Affiliation
Advisory Committee
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Judith Storch
Name (ID = NAME-3); (type = personal)
NamePart (type = family)
Dixon
NamePart (type = given)
Joseph
Role
RoleTerm (authority = RULIB); (type = )
internal member
Affiliation
Advisory Committee
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Joseph Dixon
Name (ID = NAME-4); (type = personal)
NamePart (type = family)
Watford
NamePart (type = given)
Malcolm
Role
RoleTerm (authority = RULIB); (type = )
internal member
Affiliation
Advisory Committee
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Malcolm Watford
Name (ID = NAME-5); (type = personal)
NamePart (type = family)
Blaner
NamePart (type = given)
William
Role
RoleTerm (authority = RULIB); (type = )
outside member
Affiliation
Advisory Committee
DisplayForm
William Blaner
Name (ID = NAME-1); (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB); (type = )
degree grantor
Name (ID = NAME-2); (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB); (type = )
school
OriginInfo
DateCreated (point = ); (qualifier = exact)
2009
DateOther (qualifier = exact); (type = degree)
2009-10
Place
PlaceTerm (type = code)
xx
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T3VX0GPX
Genre (authority = ExL-Esploro)
ETD doctoral
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RightsDeclaration (AUTHORITY = GS); (ID = rulibRdec0006)
The author owns the copyright to this work
Copyright
Status
Copyright protected
Notice
Note
Availability
Status
Open
Reason
Permission or license
Note
RightsHolder (ID = PRH-1); (type = personal)
Name
FamilyName
Lagakos
GivenName
William
Role
Copyright holder
RightsEvent (ID = RE-1); (AUTHORITY = rulib)
Type
Permission or license
Label
Place
DateTime
Detail
AssociatedEntity (ID = AE-1); (AUTHORITY = rulib)
Role
Copyright holder
Name
William Lagakos
Affiliation
Rutgers University. Graduate School - New Brunswick
AssociatedObject (ID = AO-1); (AUTHORITY = rulib)
Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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application/pdf
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application/x-tar
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1863680
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