Localization of Neuropeptide Y Binding Sites in the Zona glomerulosa of the Bovine Adrenal Gland

1988 ◽  
Vol 48 (2) ◽  
pp. 207-210 ◽  
Author(s):  
Tichomir Torda ◽  
Ricardo A. Cruciani ◽  
Juan M. Saavedra
Keyword(s):  
Adrenal Gland ◽  
Neuropeptide Y ◽  
Binding Sites ◽  
Zona Glomerulosa

Angiotensin II receptor isoforms in the rat adrenal gland: studies with the selective subtype antagonists DuP 753 and CGP42112A

1993 ◽  
Vol 11 (1) ◽  
pp. 69-75 ◽  
Author(s):  
M Montiel ◽  
S Barker ◽  
G P Vinson ◽  
E Jiménez
Keyword(s):  
Angiotensin Ii ◽  
Adrenal Gland ◽  
Binding Sites ◽  
Specific Binding ◽  
Zona Glomerulosa ◽  
Scatchard Analysis ◽  
Receptor Subtypes ◽  
Ang Ii ◽  
Angiotensin Ii Receptor ◽  
Receptor Isoforms

ABSTRACT The angiotensin II (Ang II)-binding sites in rat adrenal gland membranes were characterized using 125I-radiolabelled Ang II. While Scatchard analysis identified a single population of Ang II receptor sites, isoelectric focusing (IEF) on polyacrylamide gels revealed four peaks of specific Ang II binding which migrated to isoelectric points (pI values) 6·8, 6·7, 6·5 and 6·3. In binding assays in the presence of an excess of the Ang II receptor AT1 subtype antagonist DuP 753, a monophasic dose-dependent displacement of 125I-labelled Ang II binding by the Ang II receptor AT2 subtype antagonist CGP42112A was observed, and vice versa. In this system, reduction of disulphide bridges using 1 mmol dithiothreitol (DTT)/l markedly increased the number of binding sites in the adrenal zona glomerulosa without affecting receptor affinity. Using IEF, it was found that both DuP 753 and CGP42112A were able to reduce specific binding of each of the four peaks to some extent. However, the predominant effect of DuP 753 was to reduce the labelling of the isoform at pI 6·7 substantially, while CGP42112A significantly inhibited the specific 125I-labelled Ang II binding to the pI 6·3 isoform. When DuP 753 and CGP42112A were used together, specific binding of 125I-labelled Ang II to the isoforms of pI values 6·8, 6·7 and 6·3 was completely eliminated. These data suggest that the four peaks of specific binding found may be composed of different isoforms of both AT1 and AT2 receptor subtypes and that the Ang II receptor isoforms which migrated to pI 6·7 and pI 6·3 are predominantly composed of AT1 and AT2 receptor subtypes respectively. Interestingly, in the presence of both antagonists, 8·7 ± 0·9% of the specific binding migrating at pI 6·5 remained unaffected. This finding suggests the presence of an additional subtype, which is neither AT1 nor AT2, in the rat adrenal zona glomerulosa. In further studies, pretreatment with DTT was found to increase the specific 125I-labelled Ang II binding of all four isoforms. Moreover, DTT also produced a further specific binding component between pI 6·5 and pI 6·7 which exhibited AT2 subtype pharmacology in DTT-treated preparations. Since DTT has been reported to enhance only AT2 subtype binding this also suggests that the different isoforms may contain components related to both AT1 and AT2 receptor subtypes.

scholarly journals Atrial natriuretic factor mRNA and binding sites in the adrenal gland

1990 ◽  
Vol 271 (2) ◽  
pp. 555-558 ◽  
Author(s):  
D J R Nunez ◽  
A P Davenport ◽  
M J Brown
Keyword(s):  
Angiotensin Ii ◽  
Adrenal Gland ◽  
Adrenal Medulla ◽  
Binding Sites ◽  
Atrial Natriuretic Factor ◽  
Zona Glomerulosa ◽  
Aldosterone Secretion ◽  
Natriuretic Factor ◽  
Atrial Natriuretic

The factor inhibiting aldosterone secretion produced by the adrenal medulla may be atrial natriuretic factor (ANF), since the latter abolishes aldosterone release in response to a number of secretagogues, including angiotensin II and K+. In this study we have shown that cells in the adrenal medulla contain ANF mRNA and therefore have the potential to synthesize this peptide. The presence of binding sites for ANF predominantly in the adrenal zona glomerulosa suggests that, if ANF is synthesized in the medulla and transferred to the cortex, it may affect mineralocorticoid status.

scholarly journals Neurotransmitter and Receptor Deficits in Senile Dementia of the Alzheimer Type

1986 ◽  
Vol 13 (S4) ◽  
pp. 503-510 ◽  
Author(s):  
R. Quirion ◽  
J.C. Martel ◽  
Y. Robitaille ◽  
P. Etienne ◽  
P. Wood ◽  
...  
Keyword(s):  
Neuropeptide Y ◽  
Receptor Binding ◽  
Binding Sites ◽  
Senile Dementia ◽  
Somatostatin Receptor ◽  
Brain Regions ◽  
Nucleus Basalis ◽  
Nicotinic Cholinergic Receptors ◽  
Senile Dementia Of The

Abstract:Multiple neurotransmitter systems are affected in senile dementia of the Alzheimer's type (SDAT). Among them, acetylcholine has been most studied. It is now well accepted that the activity of the enzyme, choline acetyltransferase (ChAT) is much decreased in various brain regions including the frontal and temporal cortices, hippocampus and nucleus basalis of Meynert (nbm) in SDAT. Cortical M2-muscarinic and nicotinic cholinergic receptors are also decreased but only in a certain proportion (30-40%) of SDAT patients. For other systems, it appears that cortical serotonin (5-HT)-type 2 receptor binding sites are decreased in SDAT. This diminution in 5-HT2 receptors correlates well with the decreased levels of somatostatin-like immunoreactive materials found in the cortex of SDAT patients. Cortical somatostatin receptor binding sites are decreased in about one third of SDAT patients. Finally, neuropeptide Y and neuropeptide Y receptor binding sites are distributed in areas enriched in cholinergic cell bodies and nerve fiber terminals and it would be of interest to determine possible involvement of this peptide in SDAT. Thus, it appears that multi-drug clinical trials should be considered for the treatment of SDAT.

Expression and cellular localization of tissue kallikrein-kinin system in human adrenal gland

1996 ◽  
Vol 271 (3) ◽  
pp. F709-F716 ◽  
Author(s):  
D. Z. Wang ◽  
Q. Song ◽  
L. M. Chen ◽  
L. Chao ◽  
J. Chao
Keyword(s):  
Adrenal Gland ◽  
Cellular Localization ◽  
Zona Glomerulosa ◽  
Zona Fasciculata ◽  
Tissue Kallikrein ◽  
Kinin System ◽  
B1 Receptor ◽  
B2 Receptors ◽  
Kallikrein Kinin System

The tissue kallikrein-kinin system has been implicated in regulating blood pressure and electrolyte homeostasis. To understand the function of this system, we identified the expression and cellular localization of its components including tissue kallikrein, kallistatin, kininogen, and bradykinin B1 and B2 receptors in human adrenal gland. Reverse transcription-polymerase chain reaction followed by Southern blot analysis showed that these five components of this system were all expressed in human adrenal gland. In situ hybridization histochemistry with respective digoxigenin-labeled antisense riboprobes revealed localization of kallikrein transcript throughout the adrenal cortex and medulla except the zona glomerulosa, whereas kallistatin mRNA was only localized in the zona fasciculata. Low-molecular-weight kininogen and B2 receptor mRNAs were colocalized in the zona glomerulosa and zona fasciculata and also in the zona reticularis and chromaffin cells but to a lesser degree. The B1 receptor mRNA was stained in the zona fasciculata and medulla. These results show the expression and differential colocalization of the components of the tissue kallikrein-kinin system and reveal the potential action sites of this system in the adrenal gland.

scholarly journals Changes in neuropeptide Y (NPY) binding sites in the rat brain: A quantitative receptor autoradiographic study

1987 ◽  
Vol 43 ◽  
pp. 127
Author(s):  
Tatsunobu Okubo ◽  
Yoshihide Ishida ◽  
Yasufumi Kataoka ◽  
Kazuto Shigematsu ◽  
Masami Niwa ◽  
...  
Keyword(s):  
Neuropeptide Y ◽  
Rat Brain ◽  
Binding Sites ◽  
Autoradiographic Study

Alpha-human atrial natriuretic polypeptide (α-hANP) specific binding sites in bovine adrenal gland

1986 ◽  
Vol 137 (2) ◽  
pp. 657-663 ◽  
Author(s):  
Kazumi Higuchi ◽  
Hajime Nawata ◽  
Ken-Ichi Kato ◽  
Hiroshi Ibayashi ◽  
Hisayuki Matsuo
Keyword(s):  
Adrenal Gland ◽  
Binding Sites ◽  
Specific Binding ◽  
Specific Binding Sites ◽  
Atrial Natriuretic Polypeptide ◽  
Atrial Natriuretic
Sign in / Sign up

Export Citation Format

Share Document