19F-NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles

Ding Rong; Chan Lan S. Lin; D. Andre D'Avignon; Allen J. Lovey; Michael Rosenberger; Ellen Li

doi:10.1016/S0014-5793(96)01509-8

¹⁹F-NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles

Ding Rong, Chan Lan S. Lin, D. Andre D'Avignon, Allen J. Lovey, Michael Rosenberger, Ellen Li

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

8 Scopus citations

Abstract

The cellular retinol binding proteins, CRBP and CRBP II, are implicated in the cellular uptake of retinol and intracellular trafficking of retinol between sites of metabolic processing. ¹⁹F-NMR studies of retinol transfer between CRBP and CRBP II and phospholipid vesicles, using either fluorine-labeled ligand or protein, demonstrated that there was significantly more transfer of retinol from CRBP II to lipid vesicles than from CRBP. Differences in how readily protein-bound retinol is released to lipid bilayers may lead to differences in how these two proteins modulate intracellular retinol metabolism.

Original language	English (US)
Pages (from-to)	116-120
Number of pages	5
Journal	FEBS Letters
Volume	402
Issue number	2-3
DOIs	https://doi.org/10.1016/S0014-5793(96)01509-8
State	Published - Jan 27 1997
Externally published	Yes

Bibliographical note

Funding Information:
This work was supported by National Institutes of Health Grant DK 40172. NMR spectra were collected at the Washington University High Resolution NMR Facility which is funded in part through NIH Biomedical Research support shared instrument grants RR02004, RR05018 and RR07155. E.L. is a Burroughs Wellcome Scholar in Toxicology. We thank Marc Levin and David Cistola for many helpful discussions.

Keywords

Cellular retinol binding protein
Cellular retinol binding protein II
F-NMR
Liposome
Retinol

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title = "19F-NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles",

abstract = "The cellular retinol binding proteins, CRBP and CRBP II, are implicated in the cellular uptake of retinol and intracellular trafficking of retinol between sites of metabolic processing. 19F-NMR studies of retinol transfer between CRBP and CRBP II and phospholipid vesicles, using either fluorine-labeled ligand or protein, demonstrated that there was significantly more transfer of retinol from CRBP II to lipid vesicles than from CRBP. Differences in how readily protein-bound retinol is released to lipid bilayers may lead to differences in how these two proteins modulate intracellular retinol metabolism.",

keywords = "Cellular retinol binding protein, Cellular retinol binding protein II, F-NMR, Liposome, Retinol",

author = "Ding Rong and Lin, {Chan Lan S.} and D'Avignon, {D. Andre} and Lovey, {Allen J.} and Michael Rosenberger and Ellen Li",

note = "Funding Information: This work was supported by National Institutes of Health Grant DK 40172. NMR spectra were collected at the Washington University High Resolution NMR Facility which is funded in part through NIH Biomedical Research support shared instrument grants RR02004, RR05018 and RR07155. E.L. is a Burroughs Wellcome Scholar in Toxicology. We thank Marc Levin and David Cistola for many helpful discussions.",

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AU - Lin, Chan Lan S.

AU - D'Avignon, D. Andre

AU - Lovey, Allen J.

AU - Rosenberger, Michael

AU - Li, Ellen

N1 - Funding Information: This work was supported by National Institutes of Health Grant DK 40172. NMR spectra were collected at the Washington University High Resolution NMR Facility which is funded in part through NIH Biomedical Research support shared instrument grants RR02004, RR05018 and RR07155. E.L. is a Burroughs Wellcome Scholar in Toxicology. We thank Marc Levin and David Cistola for many helpful discussions.

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AB - The cellular retinol binding proteins, CRBP and CRBP II, are implicated in the cellular uptake of retinol and intracellular trafficking of retinol between sites of metabolic processing. 19F-NMR studies of retinol transfer between CRBP and CRBP II and phospholipid vesicles, using either fluorine-labeled ligand or protein, demonstrated that there was significantly more transfer of retinol from CRBP II to lipid vesicles than from CRBP. Differences in how readily protein-bound retinol is released to lipid bilayers may lead to differences in how these two proteins modulate intracellular retinol metabolism.

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