Biophysical characterization of glycosaminoglycan-IL-7 interactions using SPR.

Printer-friendly versionPrinter-friendly versionPDF versionPDF version
TitleBiophysical characterization of glycosaminoglycan-IL-7 interactions using SPR.
Publication TypeJournal Article
Year of Publication2012
AuthorsZhang, F, Liang, X, Pu, D, George, KI, Holland, PJ, Walsh, STR, Linhardt, RJ
JournalBiochimie
Volume94
Issue1
Pagination242-9
Date Published2012 Jan
ISSN1638-6183
KeywordsAnimals, Biophysics, Glycosaminoglycans, Humans, Interleukin-7, Mice, Surface Plasmon Resonance
Abstract

Glycosaminoglycans (GAGs) interact with a number of cytokines and growth factors thereby playing an essential role in the regulation of many physiological processes. These interactions are important for both normal signal transduction and the regulation of the tissue distribution of cytokines/growth factors. In the present study, we employed surface plasmon resonance (SPR) spectroscopy to dissect the binding interactions between GAGs and murine and human forms of interleukin-7 (IL-7). SPR results revealed that heparin binds with higher affinity to human IL-7 than murine IL-7 through a different kinetic mechanism. The optimal oligosaccharide length of heparin for the interactions to human and murine IL-7 involves a sequence larger than a tetrasaccharide. These results further demonstrate that while IL-7 is principally a heparin/heparan sulfate binding protein, it also interacts with dermatan sulfate, chondroitin sulfates C, D, and E, indicating that this cytokine preferentially interacts with GAGs having a higher degree of sulfation.

DOI10.1016/j.biochi.2011.10.015
Alternate JournalBiochimie
PubMed ID22085638
PubMed Central IDPMC3338127
Grant ListAI-72142 / AI / NIAID NIH HHS / United States
GM-38060 / GM / NIGMS NIH HHS / United States
R01 GM038060 / GM / NIGMS NIH HHS / United States
R01 GM038060-23 / GM / NIGMS NIH HHS / United States