2-Pyrazolyl-N6-Substituted Adenosine Derivatives as High Affinity and Selective Adenosine A3Receptor Agonists

2004 ◽  
Vol 47 (19) ◽  
pp. 4766-4773 ◽  
Author(s):  
Elfatih Elzein ◽  
Venkata Palle ◽  
Yuzhi Wu ◽  
Tenning Maa ◽  
Dewan Zeng ◽  
...  
Keyword(s):  
High Affinity ◽  
Adenosine Derivatives

scholarly journals N6-Cycloalkyl- andN6-Bicycloalkyl-C5′(C2′)-modified Adenosine Derivatives as High-Affinity and Selective Agonists at the Human A1Adenosine Receptor with Antinociceptive Effects in Mice

2009 ◽  
Vol 52 (10) ◽  
pp. 3430-3430 ◽  
Author(s):  
Palmarisa Franchetti ◽  
Loredana Cappellacci ◽  
Patrizia Vita ◽  
Riccardo Petrelli ◽  
Antonio Lavecchia ◽  
...  
Keyword(s):  
High Affinity ◽  
Antinociceptive Effects ◽  
Adenosine Derivatives ◽  
Selective Agonists

Convergent functional groups. 13. High-affinity complexation of adenosine derivatives within induced binding pockets

1993 ◽  
Vol 115 (9) ◽  
pp. 3548-3557 ◽  
Author(s):  
M. Morgan Conn ◽  
Ghislain Deslongchamps ◽  
Javier de Mendoza ◽  
Julius Rebek
Keyword(s):  
Functional Groups ◽  
High Affinity ◽  
Binding Pockets ◽  
Adenosine Derivatives

N6-Cycloalkyl- andN6-Bicycloalkyl-C5′(C2′)-modified Adenosine Derivatives as High-Affinity and Selective Agonists at the Human A1Adenosine Receptor with Antinociceptive Effects in Mice

2009 ◽  
Vol 52 (8) ◽  
pp. 2393-2406 ◽  
Author(s):  
Palmarisa Franchetti ◽  
Loredana Cappellacci ◽  
Patrizia Vita ◽  
Riccardo Petrelli ◽  
Antonio Lavecchia ◽  
...  
Keyword(s):  
High Affinity ◽  
Antinociceptive Effects ◽  
Adenosine Derivatives ◽  
Selective Agonists

N6-Cycloalkyl-2-substituted adenosine derivatives as selective, high affinity adenosine A1 receptor agonists

2007 ◽  
Vol 17 (1) ◽  
pp. 161-166 ◽  
Author(s):  
Elfatih Elzein ◽  
Rao Kalla ◽  
Xiaofen Li ◽  
Thao Perry ◽  
Tim Marquart ◽  
...  
Keyword(s):  
Adenosine A1 Receptor ◽  
Receptor Agonists ◽  
High Affinity ◽  
Adenosine A1 ◽  
A1 Receptor ◽  
Adenosine Derivatives

Neuronal and Extraneuronal Uptake of 3H-Norepinephrine in the Heart of the Active Bat: An Electron Microscopic Radioautographic Study

1973 ◽  
Vol 31 ◽  
pp. 522-523
Author(s):  
Martin Hagopian ◽  
Michael D. Gershon ◽  
Eladio A. Nunez
Keyword(s):  
Smooth Muscle ◽  
Monoamine Oxidase ◽  
Vascular Smooth Muscle ◽  
Cardiac Muscle ◽  
Maximum Rate ◽  
External Medium ◽  
Extraneuronal Uptake ◽  
Electron Microscopic ◽  
Cardiac Tissues ◽  
High Affinity

The ability of cardiac tissues to take up norepinephrine from an external medium is well known. Two mechanisms, called Uptake and Uptake respectively by Iversen have been differentiated. Uptake is a high affinity system associated with adrenergic neuronal elements. Uptake is a low affinity system, with a higher maximum rate than that of Uptake. Uptake has been associated with extraneuronal tissues such as cardiac muscle, fibroblasts or vascular smooth muscle. At low perfusion concentrations of norepinephrine most of the amine taken up by Uptake is metabolized. In order to study the localization of sites of norepinephrine storage following its uptake in the active bat heart, tritiated norepinephrine (2.5 mCi; 0.064 mg) was given intravenously to 2 bats. Monoamine oxidase had been inhibited with pheniprazine (10 mg/kg) one hour previously to decrease metabolism of norepinephrine.

Clinical Application and Results of the Assessment of Coronary Blood Flow by the Regional Precordial Xenon Residue Detection Technique

1978 ◽  
Vol 17 (04) ◽  
pp. 161-171
Author(s):  
H.-J. Engel ◽  
H. Hundeshagen ◽  
P. R. Lichtlen
Keyword(s):  
Wall Motion ◽  
High Flow ◽  
Detection Technique ◽  
Fatty Tissue ◽  
Technical Aspects ◽  
Residue Detection ◽  
High Affinity ◽  
Artery Disease ◽  
The Right ◽  
Drug Interventions

Methodological and technical aspects as well as application and results of the precordial Xenon-residue-detection technique are critically reviewed. The results concern mainly normal flow in various regions of the heart esp. in the free wall of the right and left ventricle, poststenotic flow in patients with coronary artery disease in relation to the degree of proximal nar-rowings as well as wall motion of the corresponding LV segment, bypassgraft flow and flow after drug interventions esp. nitrates, betablockers, the calcium-antagonist Nifedipine and the coronary dilator Dipyridamole. In spite of its serious limitations (high affinity of Xenon for fatty tissue, geometrical problems in the assessment of flow and its relation to anatomy, gas exchange in situations of high flow etc.), the technique is found to be a usefull investigatory tool. Due to its technical display and the related high costs routine application is, however, prohibitive.

Binding of 131I-Labeled Tissue-Type Plasminogen Activator on De-Endothelialized Lesions in Rabbits

1987 ◽  
Vol 26 (05) ◽  
pp. 224-228 ◽  
Author(s):  
Y. Isaka ◽  
H. Etani ◽  
K. Kimura ◽  
S. Yoneda ◽  
T. Kamada ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Abdominal Aorta ◽  
Half Life ◽  
Balloon Catheter ◽  
Biochemical Properties ◽  
Tissue Type ◽  
Fibrin Deposition ◽  
Tissue Type Plasminogen Activator ◽  
High Affinity ◽  
Type Plasminogen Activator

Tissue-type plasminogen activator (t-PA) which has a high affinity for fibrin in the clot, was labeled with 131I by the iodogen method, and its binding to de-endothelialized lesions in the rabbit was measured to assess the detectability of thrombi. The de-endothelialized lesion was induced in the abdominal aorta with a Fogarty 4F balloon catheter. Two hours after the de-endothelialization, 131I-labeled t-PA (125 ± 46 μCi) was injected intravenously. The initial half-life of the agent in blood (n = 12) was 2.9 ± 0.4 min. The degree of binding of 131I-labeled t-PA to the de-endothelialized lesion was evaluated at 15 min (n = 6) or at 30 min (n = 6) after injection of the agent. In spite of the retention of the biochemical properties of 131I-labeled t-PA and the presence of fibrin deposition at the de-endothelialized lesion, the binding of t-PA to the lesion was not sufficiently strong. Lesion-to-control ratios (cpm/g/cpm/g) were 1.65 ± 0.40 (at 15 min) and 1.39 ± 1.31 (at 30 min), and lesion-to-blood ratios were 1.39 ± 0.32 (at 15 min) and 1.36 ± 0.23 (at 30 min). These results suggest that radiolabeled t-PA may be inappropriate as a radiopharmaceutical for the scintigraphic detection of a pre-existing thrombotic lesion.

Characterization of a Mode of Specific Binding of Fibrin Monomer through its Amino-Terminal Domain by Macrophages and Macrophage Cell-Lines

1990 ◽  
Vol 63 (02) ◽  
pp. 193-203 ◽  
Author(s):  
John R Shainoff ◽  
Deborah J Stearns ◽  
Patricia M DiBello ◽  
Youko Hishikawa-Itoh
Keyword(s):  
Peritoneal Macrophages ◽  
Affinity Binding ◽  
Macrophage Cell ◽  
High Affinity Binding ◽  
Amino Terminal ◽  
High Affinity ◽  
Terminal Domain ◽  
Weak Binding ◽  
Amino Terminal Domain

SummaryThe studies reported here probe the existence of a receptor-mediated mode of fibrin-binding by macrophages that is associated with the chemical change underlying the fibrinogen-fibrin conversion (the release of fibrinopeptides from the amino-terminal domain) without depending on fibrin-aggregation. The question is pursued by 1) characterization of binding in relation to fibrinopeptide content of both the intact protein and the CNBr-fragment comprising the amino-terminal domain known as the NDSK of the protein, 2) tests of competition for binding sites, and 3) photo-affinity labeling of macrophage surface proteins. The binding of intact monomers of types lacking either fibrinopeptide A alone (α-fibrin) or both fibrinopeptides A and B (αβ-fibrin) by peritoneal macrophages is characterized as proceeding through both a fibrin-specific low density/high affinity (BMAX ≃ 200–800 molecules/cell, KD ≃ 10−12 M) interaction that is not duplicated with fibrinogen, and a non-specific high density/low affinity (BMAX ≥ 105 molecules/cell, KD ≥ 10−6 M) interaction equivalent to the weak binding of fibrinogen. Similar binding characteristics are displayed by monocyte/macrophage cell lines (J774A.1 and U937) as well as peritoneal macrophages towards the NDSK preparations of these proteins, except for a slightly weaker (KD ≃ 10−10 M) high-affinity binding. The high affinity binding of intact monomer is inhibitable by fibrin-NDSK, but not fibrinogen-NDSK. This binding appears principally dependent on release of fibrinopeptide-A, because a species of fibrin (β-fibrin) lacking fibrinopeptide-B alone undergoes only weak binding similar to that of fibrinogen. Synthetic Gly-Pro-Arg and Gly-His-Arg-Pro corresponding to the N-termini of to the α- and the β-chains of fibrin both inhibit the high affinity binding of the fibrin-NDSKs, and the cell-adhesion peptide Arg-Gly-Asp does not. Photoaffinity-labeling experiments indicate that polypeptides with elec-trophoretically estimated masses of 124 and 187 kDa are the principal membrane components associated with specifically bound fibrin-NDSK. The binding could not be up-regulated with either phorbol myristyl acetate, interferon gamma or ADP, but was abolished by EDTA and by lipopolysaccharide. Because of the low BMAX, it is suggested that the high-affinity mode of binding characterized here would be too limited to function by itself in scavenging much fibrin, but may act cooperatively with other, less limited modes of fibrin binding.

Sign in / Sign up

Export Citation Format

Share Document