TY  - JOUR
A1  - Ritzer, J.
A1  - Lühmann, T.
A1  - Rode, C.
A1  - Pein-Hackelbusch, M.
A1  - Immohr, I.
A1  - Schedler, U.
A1  - Thiele, T.
A1  - Stübinger, S.
A1  - Rechenberg, B.v.
A1  - Waser-Althaus, J.
A1  - Schlottig, F.
A1  - Merli, M.
A1  - Dawe, H.
A1  - Karpíšek, M.
A1  - Wyrwa, R.
A1  - Schnabelrauch, M.
A1  - Meinel, L.
T1  - Diagnosing peri-implant disease using the tongue as a 24/7 detector
JF  - Nature Communications
N2  - Our ability of screening broad communities for clinically asymptomatic diseases critically drives population health. Sensory chewing gums are presented targeting the tongue as 24/7 detector allowing diagnosis by “anyone, anywhere, anytime”. The chewing gum contains peptide sensors consisting of a protease cleavable linker in between a bitter substance and a microparticle. Matrix metalloproteinases in the oral cavity, as upregulated in peri-implant disease, specifically target the protease cleavable linker while chewing the gum, thereby generating bitterness for detection by the tongue. The peptide sensors prove significant success in discriminating saliva collected from patients with peri-implant disease versus clinically asymptomatic volunteers. Superior outcome is demonstrated over commercially available protease-based tests in saliva. “Anyone, anywhere, anytime” diagnostics are within reach for oral inflammation. Expanding this platform technology to other diseases in the future features this diagnostic as a massive screening tool potentially maximizing impact on population health.
KW  - peri-implant disease
KW  - sensory chewing gums
KW  - tongue
KW  - detector
KW  - peptide sensors
Y1  - 2017
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-170471
VL  - 8
IS  - 264
ER  - 
TY  - JOUR
A1  - Richter, K.
A1  - Mathes, V.
A1  - Fronius, M.
A1  - Althaus, M.
A1  - Hecker, A.
A1  - Krasteva-Christ, G.
A1  - Padberg, W.
A1  - Hone, A. J.
A1  - McIntosh, J. M.
A1  - Zakrzewicz, A.
A1  - Grau, V.
T1  - Phosphocholine - an agonist of metabotropic but not of ionotropic functions of α9-containing nicotinic acetylcholine receptors
JF  - Scientific Reports
N2  - We demonstrated previously that phosphocholine and phosphocholine-modified macromolecules efficiently inhibit ATP-dependent release of interleukin-1β from human and murine monocytes by a mechanism involving nicotinic acetylcholine receptors (nAChR). Interleukin-1β is a potent pro-inflammatory cytokine of innate immunity that plays pivotal roles in host defence. Control of interleukin-1β release is vital as excessively high systemic levels cause life threatening inflammatory diseases. In spite of its structural similarity to acetylcholine, there are no other reports on interactions of phosphocholine with nAChR. In this study, we demonstrate that phosphocholine inhibits ion-channel function of ATP receptor P2X7 in monocytic cells via nAChR containing α9 and α10 subunits. In stark contrast to choline, phosphocholine does not evoke ion current responses in Xenopus laevis oocytes, which heterologously express functional homomeric nAChR composed of α9 subunits or heteromeric receptors containing α9 and α10 subunits. Preincubation of these oocytes with phosphocholine, however, attenuated choline-induced ion current changes, suggesting that phosphocholine may act as a silent agonist. We conclude that phophocholine activates immuno-modulatory nAChR expressed by monocytes but does not stimulate canonical ionotropic receptor functions.
KW  - phosphocholine
KW  - interleukin-1β
KW  - nicotinic acetylcholine receptors
Y1  - 2016
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-167655
VL  - 6
IS  - 28660
ER  -