TY  - CHAP
A1  - Klotz, Karl-Norbert
A1  - Keil, Roger
A1  - Zimmer, Franz-Josef
A1  - Schwabe, Ulrich
T1  - Modulation of (§H) DPCPX binding to membrane-bound ans solubilized A1 adenosine receptors by guanine nucleotides
N2  - No abstract available
KW  - Adenosinrezeptor
Y1  - 1989
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-86153
ER  - 
TY  - CHAP
A1  - Spielmann, W. S.
A1  - Arend, L. J.
A1  - Klotz, Karl-Norbert
A1  - Schwabe, U.
T1  - Adenosine control of the renal Collecting tubule: receptors and signaling
N2  - No abstract available.
KW  - Adenosin
Y1  - 1991
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-86129
ER  - 
TY  - CHAP
A1  - Spielmann, W.-S.
A1  - Arend, L. J.
A1  - Klotz, Karl-Norbert
A1  - Schwabe, U.
T1  - Adenosine receptors and singnaling in the kidney
N2  - No abstract available.
KW  - Adenosinrezeptor
KW  - Niere
Y1  - 1990
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-86114
ER  - 
TY  - CHAP
A1  - Lohse, Martin J.
A1  - Klotz, Karl-Norbert
A1  - Maurer, K.
A1  - Ott, I.
A1  - Schwabe, Ulrich
T1  - Effects of adenosine on mast cells
N2  - No abstract available
KW  - Adenosin
KW  - Mastzelle
Y1  - 1990
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-86101
ER  - 
TY  - CHAP
A1  - Lohse, Martin J.
A1  - Klotz, Karl-Norbert
A1  - Schwabe, Ulrich
T1  - Functional characterization of A1 adenoosine receptors by photoaffinity labelling
N2  - The ligand-binding subunit ofthe A1 adenosine receptor has been identified in membranes with the photoaffinity Iabel R-2-azido-N6-p-hydroxyphenylisopropyladenosine (R-AHPIA). Covalent labelling ofthe A1 receptor can also be achieved in intact cells. The dissociation of the radioiodinated label (1251-AHPIA) from isolated rat fat cells was incomplete after UV irradiation, leaving about 20°/o of irreversible specific binding. Such covalent labelling of the receptor led to a concentration-dependent reduction of cellular cyclic AMP levels. This persistent effect of covalent labeHing occurred with an IC50 value of 9 nM, as compared to an IC50 value of 0.9 nM for the direct reduction of cyclic AMP Ievels by the ligand. The difference in the IC5o values can be explained by assuming spare receptors. This hypothesis was verified in binding studies using [ 3HJPIA as a radioligand. R-AHPIA inhibited binding of [3H)PIA to intact fat cells with a K1 value of about 20 nM, which is about 20 tim es high er than the corresponding IC50 value of cyclic AMP reduction. These data show that the A1 receptor is activated according to the occupancy theory. The high sensitivity of the activation in intact ceJis is due to a large number of spare receptors.
KW  - Adenosinrezeptor
Y1  - 1987
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-86097
ER  - 
TY  - CHAP
A1  - Lohse, Martin J.
A1  - Klotz, Karl-Norbert
A1  - Schwabe, Ulrich
T1  - Effects of barbiturates on A1 adenosine receptors of rat brain
N2  - Barbiturates inhibit binding of radioligands to A 1(Ri) adenosine receptors of rat brain membranes. This inhibition is dose-dependent and stereospecific and occurs in the range of pharmacologically active concentrations. The displacement of radiolabelled A1antagonists by barbiturates is not modified by GTP, indicating that barbiturates might act as antagonists at this receptor. This action of barbiturates does not seem to be related to the binding of barbiturates to plasma membranes, as the latter process has different characteristics. Barbiturates also inhibit the binding of radioligands to solubilized A1receptors, and saturation and kinetic experiments suggest that this is due to a competitive antagonism. These results indicate that barbiturates interact with the recognition site of the A1adenosine receptor.
KW  - Barbiturat
KW  - Adenosinrezeptor
KW  - Ratte
Y1  - 1985
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-70100
ER  -