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Dataset on pyrene-labelled apolipoprotein A-I, model development and fitting to monitor oligomeric species of its lipid-free form.

ABSTRACT: This article contains data for the self-association of pyrene-labelled single Cys-mutants of apolipoprotein A-I (apoA-I). Mathematical models were developed to characterise the self-association events at different cysteine positions on apoA-I obtained as a function of protein concentration based on the multi-parametric spectrum of pyrene, particularly P-value and excimer emissions. The present work complements data related to the article entitled "Analysis of pyrene-labelled apolipoprotein A-I oligomerisation in solution: Spectra deconvolution and changes in P-value and excimer formation" Tárraga et al. [1].

SUBMITTER: Tarraga WA

PROVIDER: S-EPMC7921477 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature

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Dataset on pyrene-labelled apolipoprotein A-I, model development and fitting to monitor oligomeric species of its lipid-free form.

Tárraga Wilson A WA Garda Horacio A HA Falomir Lockhart Lisandro J LJ Gonzalez Marina C MC

Data in brief 20210213

This article contains data for the self-association of pyrene-labelled single Cys-mutants of apolipoprotein A-I (apoA-I). Mathematical models were developed to characterise the self-association events at different cysteine positions on apoA-I obtained as a function of protein concentration based on the multi-parametric spectrum of pyrene, particularly <i>P</i>-value and excimer emissions. The present work complements data related to the article entitled "Analysis of pyrene-labelled apolipoprotei ...[more]

PMID: 33718538

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Project description:In the aim of testing tools for tracing cell trafficking of exogenous cholesterol, two fluorescent derivatives of cholesterol, 22-nitrobenzoxadiazole-cholesterol (NBD-Chol) and 21-methylpyrenyl-cholesterol (Pyr-met-Chol), with distinctive chemico-physical characteristics, have been compared for their cell incorporation properties, using two cell models differently handling cholesterol, with two incorporation routes. In the Caco-2 cell model, the cholesterol probes were delivered in bile salt micelles, as a model of intestinal absorption. The two probes displayed contrasting behaviors for cell uptake characteristics, cell staining, and efflux kinetics. In particular, Pyr-met-Chol cell incorporation involved SR-BI, while that of NBD-Chol appeared purely passive. In the PC-3 cell model, which overexpresses lipoprotein receptors, the cholesterol probes were delivered via the serum components, as a model of systemic delivery. We showed that Pyr-met-Chol-labelled purified LDL or HDL were able to specifically deliver Pyr-met-Chol to the PC-3 cells, while NBD-Chol incorporation was independent of lipoproteins. Observations by fluorescence microscopy evidenced that, while NBD-Chol readily stained the cytosolic lipid droplets, Pyr-met-Chol labelling led to the intense staining of intracellular structures of membranous nature, in agreement with the absence of detectable esterification of Pyr-met-Chol. A 48 h incubation of PC-3 cells with either Pyr-met-Chol-labelled LDL or HDL gave same staining patterns, mainly colocalizing with Lamp1, caveolin-1 and CD63. These data indicated convergent trafficking downwards their respective receptors, LDL-R and SR-BI, toward the cholesterol-rich internal membrane compartments, late endosomes and multivesicular bodies. Interestingly, Pyr-met-Chol staining of these structures exhibited a high excimer fluorescence emission, revealing their ordered membrane environment, and indicating that Pyr-met-Chol behaves as a fair cholesterol tracer regarding its preferential incorporation into cholesterol-rich domains. We conclude that, while NBD-Chol is a valuable marker of cholesterol esterification, Pyr-met-Chol is a reliable new lipoprotein fluorescent marker which allows to probe specific intracellular trafficking of cholesterol-rich membranes.

Dataset Information

Dataset on pyrene-labelled apolipoprotein A-I, model development and fitting to monitor oligomeric species of its lipid-free form.

Publications

Dataset on pyrene-labelled apolipoprotein A-I, model development and fitting to monitor oligomeric species of its lipid-free form.

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