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- Publisher Website: 10.1111/j.1600-079X.1993.tb00499.x
- Scopus: eid_2-s2.0-0027338346
- PMID: 8393924
- WOS: WOS:A1993LJ30100002
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Article: Characteristics of 2-[125I]iodomelatonin binding sites in the pigeon spleen and modulation of binding by guanine nucleotides
Title | Characteristics of 2-[125I]iodomelatonin binding sites in the pigeon spleen and modulation of binding by guanine nucleotides |
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Authors | |
Keywords | guanine nucleotides G‐protein immune system melatonin receptor pigeon pineal gland spleen |
Issue Date | 1993 |
Publisher | Blackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JPI |
Citation | Journal Of Pineal Research, 1993, v. 14 n. 4, p. 169-177 How to Cite? |
Abstract | 2-[125I]Iodomelatonin binding sites in membrane preparations of pigeon spleen have been characterized. The binding was stable, saturable, reversible, and of high affinity. Rosenthal and Hill analyses showed that the radioligand-receptor interaction involved a single class of binding sites. Analysis of the binding results of spleens collected during mid-light revealed an equilibrium dissociation constant (Kd) of 36.6 ± 4.8 pmol/l (mean ± sem, n = 10) and a maximum density (Bmax) of 2.3 ± 0.2 fmol/mg protein. There was no significant difference in the Kd (46.9 ± 5.0 pmol/l) or the Bmax values (2.4 ± 0.3 fmol/mg protein) for spleens collected during mid-dark (n = 9), although the mid-dark serum and pineal melatonin levels were significantly higher (P < 0.05) than the corresponding mid-light values. Kinetic analysis showed a Kd of 8.6 ± 2.0 pmol/l (n ± 4), in agreement with that derived from the saturation studies. Except for inhibition by 2- iodomelatonin, melatonin, 6-chloromelatonin, 6-hydroxymelatonin and N- acetylserotonin, the other indoles or neurotransmitters tested have little inhibition on the binding. In addition, guanosine 5'-O-(3-thiophosphate) (GTPγS), a nonhydrolysable analog of GTP, was found to inhibit the binding in a dose-dependent manner. Saturation studies revealed that this is due to a decrease in both the affinity and density of the binding sites. These data suggest that a single type of melatonin receptor is found in the pigeon spleen and that the site is coupled to a guinine nucleotide binding protein (G-protein). Our findings support a direct pineal melatonin action on the immune system. |
Persistent Identifier | http://hdl.handle.net/10722/171584 |
ISSN | 2023 Impact Factor: 8.3 2023 SCImago Journal Rankings: 2.194 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Poon, AMS | en_US |
dc.contributor.author | Wang, XL | en_US |
dc.contributor.author | Pang, SF | en_US |
dc.date.accessioned | 2012-10-30T06:15:49Z | - |
dc.date.available | 2012-10-30T06:15:49Z | - |
dc.date.issued | 1993 | en_US |
dc.identifier.citation | Journal Of Pineal Research, 1993, v. 14 n. 4, p. 169-177 | en_US |
dc.identifier.issn | 0742-3098 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171584 | - |
dc.description.abstract | 2-[125I]Iodomelatonin binding sites in membrane preparations of pigeon spleen have been characterized. The binding was stable, saturable, reversible, and of high affinity. Rosenthal and Hill analyses showed that the radioligand-receptor interaction involved a single class of binding sites. Analysis of the binding results of spleens collected during mid-light revealed an equilibrium dissociation constant (Kd) of 36.6 ± 4.8 pmol/l (mean ± sem, n = 10) and a maximum density (Bmax) of 2.3 ± 0.2 fmol/mg protein. There was no significant difference in the Kd (46.9 ± 5.0 pmol/l) or the Bmax values (2.4 ± 0.3 fmol/mg protein) for spleens collected during mid-dark (n = 9), although the mid-dark serum and pineal melatonin levels were significantly higher (P < 0.05) than the corresponding mid-light values. Kinetic analysis showed a Kd of 8.6 ± 2.0 pmol/l (n ± 4), in agreement with that derived from the saturation studies. Except for inhibition by 2- iodomelatonin, melatonin, 6-chloromelatonin, 6-hydroxymelatonin and N- acetylserotonin, the other indoles or neurotransmitters tested have little inhibition on the binding. In addition, guanosine 5'-O-(3-thiophosphate) (GTPγS), a nonhydrolysable analog of GTP, was found to inhibit the binding in a dose-dependent manner. Saturation studies revealed that this is due to a decrease in both the affinity and density of the binding sites. These data suggest that a single type of melatonin receptor is found in the pigeon spleen and that the site is coupled to a guinine nucleotide binding protein (G-protein). Our findings support a direct pineal melatonin action on the immune system. | en_US |
dc.language | eng | en_US |
dc.publisher | Blackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JPI | en_US |
dc.relation.ispartof | Journal of Pineal Research | en_US |
dc.subject | guanine nucleotides | - |
dc.subject | G‐protein | - |
dc.subject | immune system | - |
dc.subject | melatonin receptor | - |
dc.subject | pigeon | - |
dc.subject | pineal gland | - |
dc.subject | spleen | - |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Binding Sites - Drug Effects | en_US |
dc.subject.mesh | Cell Membrane - Metabolism | en_US |
dc.subject.mesh | Circadian Rhythm | en_US |
dc.subject.mesh | Columbidae | en_US |
dc.subject.mesh | Gtp-Binding Proteins - Metabolism | en_US |
dc.subject.mesh | Guanine Nucleotides - Pharmacology | en_US |
dc.subject.mesh | Kinetics | en_US |
dc.subject.mesh | Ligands | en_US |
dc.subject.mesh | Melatonin - Analogs & Derivatives - Analysis - Metabolism | en_US |
dc.subject.mesh | Pineal Gland - Chemistry | en_US |
dc.subject.mesh | Radioimmunoassay | en_US |
dc.subject.mesh | Receptors, Melatonin | en_US |
dc.subject.mesh | Receptors, Neurotransmitter - Drug Effects - Metabolism | en_US |
dc.subject.mesh | Spleen - Drug Effects - Metabolism | en_US |
dc.title | Characteristics of 2-[125I]iodomelatonin binding sites in the pigeon spleen and modulation of binding by guanine nucleotides | en_US |
dc.type | Article | en_US |
dc.identifier.email | Poon, AMS:amspoon@hkucc.hku.hk | en_US |
dc.identifier.authority | Poon, AMS=rp00354 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1111/j.1600-079X.1993.tb00499.x | - |
dc.identifier.pmid | 8393924 | - |
dc.identifier.scopus | eid_2-s2.0-0027338346 | en_US |
dc.identifier.volume | 14 | en_US |
dc.identifier.issue | 4 | en_US |
dc.identifier.spage | 169 | en_US |
dc.identifier.epage | 177 | en_US |
dc.identifier.isi | WOS:A1993LJ30100002 | - |
dc.publisher.place | Denmark | en_US |
dc.identifier.scopusauthorid | Poon, AMS=7103068868 | en_US |
dc.identifier.scopusauthorid | Wang, XL=7501861824 | en_US |
dc.identifier.scopusauthorid | Pang, SF=7402528719 | en_US |
dc.identifier.issnl | 0742-3098 | - |