Campus Units

Chemistry, Ames Laboratory

Document Type

Article

Publication Version

Accepted Manuscript

Publication Date

12-2016

Journal or Book Title

Biochimica et Biophysica Acta (BBA) - Biomembranes

Volume

1858

Issue

12

First Page

3141

Last Page

3149

DOI

10.1016/j.bbamem.2016.10.001

Abstract

The effect of ligand on the lateral diffusion of receptor for advanced glycation endproducts (RAGE), a receptor involved in numerous pathological conditions, remains unknown. Single particle tracking experiments that use quantum dots specifically bound to hemagglutinin (HA)-tagged RAGE (HA-RAGE) are reported to elucidate the effect of ligand binding on HA-RAGE diffusion in GM07373 cell membranes. The ligand used in these studies is methylglyoxal modified-bovine serum albumin (MGO-BSA) containing advanced glycation end products modifications. The binding affinity between soluble RAGE and MGO-BSA increases by 1.8 to 9.7-fold as the percent primary amine modification increases from 24 to 74% and with increasing negative charge on the MGO-BSA. Ligand incubation affects the HA-RAGE diffusion coefficient, the radius of confinement, and duration of confinement. There is, however, no correlation between MGO-BSA ligand binding affinity with soluble RAGE and the extent of the changes in HA-RAGE lateral diffusion. The ligand induced changes to HA-RAGE lateral diffusion do not occur when cholesterol is depleted from the cell membrane, indicating the mechanism for ligand-induced changes to HA-RAGE diffusion is cholesterol dependent. The results presented here serve as a first step in unraveling how ligand influences RAGE lateral diffusion.

Comments

This is a manuscript of an article published as Syed, Aleem, Qiaochu Zhu, and Emily A. Smith. "Ligand binding affinity and changes in the lateral diffusion of receptor for advanced glycation endproducts (RAGE)." Biochimica et Biophysica Acta (BBA)-Biomembranes 1858, no. 12 (2016): 3141-3149. DOI: 10.1016/j.bbamem.2016.10.001. Posted with permission.

Creative Commons License

Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.

Copyright Owner

Elsevier B.V.

Language

en

File Format

application/pdf

Published Version

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