I-FABP expression alters the intracellular distribution of the BODIPY C16 fatty acid analog

Julie Karsenty; Olfa Helal; Paulette Lechène de la Porte; Paule Beauclair-Deprez; Claire Martin-Elyazidi; Richard Planells; Judith Storch; Marguerite Gastaldi

doi:https://doi.org/10.1007/s11010-008-0004-2

I-FABP expression alters the intracellular distribution of the BODIPY C16 fatty acid analog

Julie Karsenty, Olfa Helal, Paulette Lechène de la Porte, Paule Beauclair-Deprez, Claire Martin-Elyazidi, Richard Planells, Judith Storch, Marguerite Gastaldi

Rutgers, The State University

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

To investigate the structure-function relationships of intestinal fatty acid-binding protein (I-FABP) in cellular fatty acid (FA) trafficking, we compared the distribution of a fluorescent FA analog (BODIPY FL C16) in Cos-1 cells transiently transfected with the wild type protein (wt I-FABP) to that of a variant deleted of the alpha helical domain (HL I-FABP). In vector-only cells, BODIPY fluorescence was distributed throughout the cytoplasm. In the absence of added FA, wt I-FABP was found largely in the perinuclear region with some cytoplasmic staining as well. Addition of BODIPY FL C16 to transfected cells showed that the fluorescent FA was essentially completely colocalized with the protein in the cytoplasmic and perinuclear regions as well as in cytoplasmic clusters that are not observed in the absence of wt I-FABP. For HL I-FABP, the distribution of the protein in the absence of FA was diffusely cytoplasmic, in marked contrast to the wt protein. Addition of BODIPY led to less extensive colocalization than that observed for wt I-FABP. In particular, no localization to the perinuclear region was found. Organelle colocalization studies showed that both proteins colocalized with mitochondria and endoplasmic reticulum/golgi markers, but little with a lysosomal marker. The perinuclear localization for wt I-FABP and BODIPY did not show colocalization with any of the markers tested. Taken together, these results indicate that I-FABP binds FA in vivo and that the helical domain may be important for targeting I-FABP to a perinuclear domain but not, perhaps, to the endoplasmic reticulum, golgi apparatus or mitochondria.

Original language	American English
Pages (from-to)	97-104
Number of pages	8
Journal	Molecular and Cellular Biochemistry
Volume	326
Issue number	1-2
DOIs	https://doi.org/10.1007/s11010-008-0004-2
State	Published - 2009

ASJC Scopus subject areas

Molecular Biology
Clinical Biochemistry
Cell Biology

Keywords

BODIPY FL C16
Fatty acid
Fatty acid binding protein
Fluorescence
I-FABP

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title = "I-FABP expression alters the intracellular distribution of the BODIPY C16 fatty acid analog",

abstract = "To investigate the structure-function relationships of intestinal fatty acid-binding protein (I-FABP) in cellular fatty acid (FA) trafficking, we compared the distribution of a fluorescent FA analog (BODIPY FL C16) in Cos-1 cells transiently transfected with the wild type protein (wt I-FABP) to that of a variant deleted of the alpha helical domain (HL I-FABP). In vector-only cells, BODIPY fluorescence was distributed throughout the cytoplasm. In the absence of added FA, wt I-FABP was found largely in the perinuclear region with some cytoplasmic staining as well. Addition of BODIPY FL C16 to transfected cells showed that the fluorescent FA was essentially completely colocalized with the protein in the cytoplasmic and perinuclear regions as well as in cytoplasmic clusters that are not observed in the absence of wt I-FABP. For HL I-FABP, the distribution of the protein in the absence of FA was diffusely cytoplasmic, in marked contrast to the wt protein. Addition of BODIPY led to less extensive colocalization than that observed for wt I-FABP. In particular, no localization to the perinuclear region was found. Organelle colocalization studies showed that both proteins colocalized with mitochondria and endoplasmic reticulum/golgi markers, but little with a lysosomal marker. The perinuclear localization for wt I-FABP and BODIPY did not show colocalization with any of the markers tested. Taken together, these results indicate that I-FABP binds FA in vivo and that the helical domain may be important for targeting I-FABP to a perinuclear domain but not, perhaps, to the endoplasmic reticulum, golgi apparatus or mitochondria.",

keywords = "BODIPY FL C16, Fatty acid, Fatty acid binding protein, Fluorescence, I-FABP",

author = "Julie Karsenty and Olfa Helal and {Lech{\`e}ne de la Porte}, Paulette and Paule Beauclair-Deprez and Claire Martin-Elyazidi and Richard Planells and Judith Storch and Marguerite Gastaldi",

note = "Funding Information: Acknowledgments J.S. was the recipient of a Poste-Orange fellowship from INSERM (National Institute of Health and Medical Research). This work was supported in part by U.S. Public Health Service NIH grant DK38389 (J.S.).",

year = "2009",

doi = "https://doi.org/10.1007/s11010-008-0004-2",

language = "American English",

volume = "326",

pages = "97--104",

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T1 - I-FABP expression alters the intracellular distribution of the BODIPY C16 fatty acid analog

AU - Karsenty, Julie

AU - Helal, Olfa

AU - Lechène de la Porte, Paulette

AU - Beauclair-Deprez, Paule

AU - Martin-Elyazidi, Claire

AU - Planells, Richard

AU - Storch, Judith

AU - Gastaldi, Marguerite

N1 - Funding Information: Acknowledgments J.S. was the recipient of a Poste-Orange fellowship from INSERM (National Institute of Health and Medical Research). This work was supported in part by U.S. Public Health Service NIH grant DK38389 (J.S.).

PY - 2009

Y1 - 2009

N2 - To investigate the structure-function relationships of intestinal fatty acid-binding protein (I-FABP) in cellular fatty acid (FA) trafficking, we compared the distribution of a fluorescent FA analog (BODIPY FL C16) in Cos-1 cells transiently transfected with the wild type protein (wt I-FABP) to that of a variant deleted of the alpha helical domain (HL I-FABP). In vector-only cells, BODIPY fluorescence was distributed throughout the cytoplasm. In the absence of added FA, wt I-FABP was found largely in the perinuclear region with some cytoplasmic staining as well. Addition of BODIPY FL C16 to transfected cells showed that the fluorescent FA was essentially completely colocalized with the protein in the cytoplasmic and perinuclear regions as well as in cytoplasmic clusters that are not observed in the absence of wt I-FABP. For HL I-FABP, the distribution of the protein in the absence of FA was diffusely cytoplasmic, in marked contrast to the wt protein. Addition of BODIPY led to less extensive colocalization than that observed for wt I-FABP. In particular, no localization to the perinuclear region was found. Organelle colocalization studies showed that both proteins colocalized with mitochondria and endoplasmic reticulum/golgi markers, but little with a lysosomal marker. The perinuclear localization for wt I-FABP and BODIPY did not show colocalization with any of the markers tested. Taken together, these results indicate that I-FABP binds FA in vivo and that the helical domain may be important for targeting I-FABP to a perinuclear domain but not, perhaps, to the endoplasmic reticulum, golgi apparatus or mitochondria.

AB - To investigate the structure-function relationships of intestinal fatty acid-binding protein (I-FABP) in cellular fatty acid (FA) trafficking, we compared the distribution of a fluorescent FA analog (BODIPY FL C16) in Cos-1 cells transiently transfected with the wild type protein (wt I-FABP) to that of a variant deleted of the alpha helical domain (HL I-FABP). In vector-only cells, BODIPY fluorescence was distributed throughout the cytoplasm. In the absence of added FA, wt I-FABP was found largely in the perinuclear region with some cytoplasmic staining as well. Addition of BODIPY FL C16 to transfected cells showed that the fluorescent FA was essentially completely colocalized with the protein in the cytoplasmic and perinuclear regions as well as in cytoplasmic clusters that are not observed in the absence of wt I-FABP. For HL I-FABP, the distribution of the protein in the absence of FA was diffusely cytoplasmic, in marked contrast to the wt protein. Addition of BODIPY led to less extensive colocalization than that observed for wt I-FABP. In particular, no localization to the perinuclear region was found. Organelle colocalization studies showed that both proteins colocalized with mitochondria and endoplasmic reticulum/golgi markers, but little with a lysosomal marker. The perinuclear localization for wt I-FABP and BODIPY did not show colocalization with any of the markers tested. Taken together, these results indicate that I-FABP binds FA in vivo and that the helical domain may be important for targeting I-FABP to a perinuclear domain but not, perhaps, to the endoplasmic reticulum, golgi apparatus or mitochondria.

KW - BODIPY FL C16

KW - Fatty acid

KW - Fatty acid binding protein

KW - Fluorescence

KW - I-FABP

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U2 - https://doi.org/10.1007/s11010-008-0004-2

DO - https://doi.org/10.1007/s11010-008-0004-2

M3 - Article

C2 - 19125316

SN - 0300-8177

VL - 326

SP - 97

EP - 104

JO - Molecular and Cellular Biochemistry

JF - Molecular and Cellular Biochemistry

IS - 1-2

ER -

I-FABP expression alters the intracellular distribution of the BODIPY C16 fatty acid analog

Abstract

ASJC Scopus subject areas

Keywords

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