Journal article


Influence of nonenzymatic posttranslational modifications on constitution, oligomerization and receptor binding of S100A12


Publication Details
Author(s): Augner K, Eichler J, Utz W, Pischetsrieder M
Journal: PLoS ONE
Publisher: Public Library of Science
Publication year: 2014
Volume: 9
Journal issue: 11
Pages range: e113418
ISSN: 1932-6203

Abstract

This study examined the effect of methylglyoxal (MGO)-derived nonenzymatic posttranslational modifications (nePTMs) on the binding affinity of S100A12 to its natural receptor for advanced glycation end-products (RAGE). Binding of MGOmodified S100A12 to RAGE decreased significantly with increasing MGO concentration and incubation time. Ca2+-induced S100A12 hexamerization was impaired only at higher MGO concentrations indicating that the loss of affinity is not predominantly caused by disturbance of ligand oligomerization. nePTM mapping showed carboxyethylation of lysine (CEL) and the N-terminus without preferential modification sites. Besides, hydroimidazolone, hemiaminals, argpyrimidine, and tetrahydropyrimidine rapidly formed at R21. Even at the highest modification rate, hexamerization of synthesized CEL-S100A12 was unaffected and RAGE-binding only slightly impaired. Thus, nePTMs at R21 seem to be the major cause of MGOinduced impairment of S100A12 oligomerization and RAGE binding.



How to cite
APA: Augner, K., Eichler, J., Utz, W., & Pischetsrieder, M. (2014). Influence of nonenzymatic posttranslational modifications on constitution, oligomerization and receptor binding of S100A12. PLoS one, 9(11), e113418. https://dx.doi.org/10.1371/journal.pone.0113418

MLA: Augner, Kerstin, et al. "Influence of nonenzymatic posttranslational modifications on constitution, oligomerization and receptor binding of S100A12." PLoS one 9.11 (2014): e113418.

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