DOWN-REGULATION OF ANGIOTENSIN II RECEPTORS IN HYPERTROPHIED HUMAN MYOCARDIUM
SUMMARY 1. Specific [125I]‐angiotensin II (AngII) binding in normal and hypertrophied human myocardial membranes was saturable and of high affinity. Low concentrations of unlabelled AngII and saralasin competed with [125I]‐AngII for the binding sites in these tissues. Thus, saturable [125I]‐AngII bi...
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| Veröffentlicht in: | Clinical and experimental pharmacology & physiology 1996-07, Vol.23 (6-7), p.514-518 |
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| container_title | Clinical and experimental pharmacology & physiology |
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| creator | Nozawa, Yoshihisa Miyake, Hidekazu Haruno, Akihiro Yamada, Shizuo Uchida, Shinya Ohkura, Takashi Kimura, Ryohei Suzuki, Harumi Hoshino, Tsuneo |
| description | SUMMARY
1. Specific [125I]‐angiotensin II (AngII) binding in normal and hypertrophied human myocardial membranes was saturable and of high affinity. Low concentrations of unlabelled AngII and saralasin competed with [125I]‐AngII for the binding sites in these tissues. Thus, saturable [125I]‐AngII binding in human myocardium exhibited pharmacological specificity that characterized high affinity receptors for AngII.
2. There was little difference in the apparent dissociation constant (Kd) values for [125I]‐AngII binding between normal and hypertrophied human myocardium, whereas the maximal number of binding sites (Bmax) was significantly (51%) lower in the hypertrophied group. Further, PD123177, a selective antagonist of the AT2 receptor subtype, showed three orders of magnitude higher affinity for [125I]‐AngII binding sites in both normal and hypertrophied myocardium than losartan, a selective antagonist of the AT1 receptor subtype; the Hill coefficients for these drugs were close to one.
3. A significant decrease in Bmax and Kd values for (—)‐[125I]‐iodocyanopindolol binding between normal and hypertrophied human myocardium rarely occurred.
4. The present study suggests that both normal and hypertrophied human myocardium predominantly contains the AT2 receptor subtype and that these receptors are down‐regulated in hypertrophied tissues. |
| doi_str_mv | 10.1111/j.1440-1681.1996.tb02771.x |
| format | Article |
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1. Specific [125I]‐angiotensin II (AngII) binding in normal and hypertrophied human myocardial membranes was saturable and of high affinity. Low concentrations of unlabelled AngII and saralasin competed with [125I]‐AngII for the binding sites in these tissues. Thus, saturable [125I]‐AngII binding in human myocardium exhibited pharmacological specificity that characterized high affinity receptors for AngII.
2. There was little difference in the apparent dissociation constant (Kd) values for [125I]‐AngII binding between normal and hypertrophied human myocardium, whereas the maximal number of binding sites (Bmax) was significantly (51%) lower in the hypertrophied group. Further, PD123177, a selective antagonist of the AT2 receptor subtype, showed three orders of magnitude higher affinity for [125I]‐AngII binding sites in both normal and hypertrophied myocardium than losartan, a selective antagonist of the AT1 receptor subtype; the Hill coefficients for these drugs were close to one.
3. A significant decrease in Bmax and Kd values for (—)‐[125I]‐iodocyanopindolol binding between normal and hypertrophied human myocardium rarely occurred.
4. The present study suggests that both normal and hypertrophied human myocardium predominantly contains the AT2 receptor subtype and that these receptors are down‐regulated in hypertrophied tissues.</description><identifier>ISSN: 0305-1870</identifier><identifier>EISSN: 1440-1681</identifier><identifier>DOI: 10.1111/j.1440-1681.1996.tb02771.x</identifier><identifier>PMID: 8800576</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>[125I]-angiotensin II ; Aged ; Angiotensin II - metabolism ; angiotensin II receptors ; Angiotensin Receptor Antagonists ; cardiac hypertrophy ; Cardiomegaly - metabolism ; Down-Regulation - physiology ; Female ; human myocardium ; Humans ; Imidazoles - pharmacology ; In Vitro Techniques ; Iodine Radioisotopes ; Iodocyanopindolol ; Kinetics ; Male ; Membranes - metabolism ; Middle Aged ; Myocardium - metabolism ; Pindolol - analogs & derivatives ; Pyridines - pharmacology ; receptor subtype ; Receptors, Angiotensin - biosynthesis</subject><ispartof>Clinical and experimental pharmacology & physiology, 1996-07, Vol.23 (6-7), p.514-518</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4074-36b87cbda1307aa9ebce8eb8497f04d0e769d9467eee44b4bfb31826009cde0e3</citedby><cites>FETCH-LOGICAL-c4074-36b87cbda1307aa9ebce8eb8497f04d0e769d9467eee44b4bfb31826009cde0e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1440-1681.1996.tb02771.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1440-1681.1996.tb02771.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8800576$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nozawa, Yoshihisa</creatorcontrib><creatorcontrib>Miyake, Hidekazu</creatorcontrib><creatorcontrib>Haruno, Akihiro</creatorcontrib><creatorcontrib>Yamada, Shizuo</creatorcontrib><creatorcontrib>Uchida, Shinya</creatorcontrib><creatorcontrib>Ohkura, Takashi</creatorcontrib><creatorcontrib>Kimura, Ryohei</creatorcontrib><creatorcontrib>Suzuki, Harumi</creatorcontrib><creatorcontrib>Hoshino, Tsuneo</creatorcontrib><title>DOWN-REGULATION OF ANGIOTENSIN II RECEPTORS IN HYPERTROPHIED HUMAN MYOCARDIUM</title><title>Clinical and experimental pharmacology & physiology</title><addtitle>Clin Exp Pharmacol Physiol</addtitle><description>SUMMARY
1. Specific [125I]‐angiotensin II (AngII) binding in normal and hypertrophied human myocardial membranes was saturable and of high affinity. Low concentrations of unlabelled AngII and saralasin competed with [125I]‐AngII for the binding sites in these tissues. Thus, saturable [125I]‐AngII binding in human myocardium exhibited pharmacological specificity that characterized high affinity receptors for AngII.
2. There was little difference in the apparent dissociation constant (Kd) values for [125I]‐AngII binding between normal and hypertrophied human myocardium, whereas the maximal number of binding sites (Bmax) was significantly (51%) lower in the hypertrophied group. Further, PD123177, a selective antagonist of the AT2 receptor subtype, showed three orders of magnitude higher affinity for [125I]‐AngII binding sites in both normal and hypertrophied myocardium than losartan, a selective antagonist of the AT1 receptor subtype; the Hill coefficients for these drugs were close to one.
3. A significant decrease in Bmax and Kd values for (—)‐[125I]‐iodocyanopindolol binding between normal and hypertrophied human myocardium rarely occurred.
4. The present study suggests that both normal and hypertrophied human myocardium predominantly contains the AT2 receptor subtype and that these receptors are down‐regulated in hypertrophied tissues.</description><subject>[125I]-angiotensin II</subject><subject>Aged</subject><subject>Angiotensin II - metabolism</subject><subject>angiotensin II receptors</subject><subject>Angiotensin Receptor Antagonists</subject><subject>cardiac hypertrophy</subject><subject>Cardiomegaly - metabolism</subject><subject>Down-Regulation - physiology</subject><subject>Female</subject><subject>human myocardium</subject><subject>Humans</subject><subject>Imidazoles - pharmacology</subject><subject>In Vitro Techniques</subject><subject>Iodine Radioisotopes</subject><subject>Iodocyanopindolol</subject><subject>Kinetics</subject><subject>Male</subject><subject>Membranes - metabolism</subject><subject>Middle Aged</subject><subject>Myocardium - metabolism</subject><subject>Pindolol - analogs & derivatives</subject><subject>Pyridines - pharmacology</subject><subject>receptor subtype</subject><subject>Receptors, Angiotensin - biosynthesis</subject><issn>0305-1870</issn><issn>1440-1681</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkMGO2kAMhkfVVpTSPkKlqIe9JethhplJDytFECACEhqCEKdRJjESLJRtBlR4-00E4l5fbOu3f1sfIT8peLSOl51HOQeXCkU96vvCOxnoSkm9yyfSfkhPpA0Mei5VEr6Qr9buAKAHgrVIS6m6lKJNZoNkFbtpOFpOgyxKYicZOkE8ipIsjBdR7ESRk4b9cJ4l6cKp-_F6HqZZmszHUThwxstZEDuzddIP0kG0nH0jnzf53uL3e-6Q5TDM-mN3moyifjB1Cw6Su0wYJQtT5pSBzHMfTYEKjeK-3AAvAaXwS58LiYicG242hlHVFQB-USIg65Dnm-97dfx7RnvSh60tcL_P_-DxbLVUrOtzxevBX7fBojpaW-FGv1fbQ15dNQXdsNQ73QDTDTDdsNR3lvpSL_-4XzmbA5aP1Tu8Wn-96f-2e7z-h7OugfZo8517M9jaE14eBnn1poVksqdX8UhP-GCiJr8zvWIfoFiMnw</recordid><startdate>199607</startdate><enddate>199607</enddate><creator>Nozawa, Yoshihisa</creator><creator>Miyake, Hidekazu</creator><creator>Haruno, Akihiro</creator><creator>Yamada, Shizuo</creator><creator>Uchida, Shinya</creator><creator>Ohkura, Takashi</creator><creator>Kimura, Ryohei</creator><creator>Suzuki, Harumi</creator><creator>Hoshino, Tsuneo</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199607</creationdate><title>DOWN-REGULATION OF ANGIOTENSIN II RECEPTORS IN HYPERTROPHIED HUMAN MYOCARDIUM</title><author>Nozawa, Yoshihisa ; Miyake, Hidekazu ; Haruno, Akihiro ; Yamada, Shizuo ; Uchida, Shinya ; Ohkura, Takashi ; Kimura, Ryohei ; Suzuki, Harumi ; Hoshino, Tsuneo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4074-36b87cbda1307aa9ebce8eb8497f04d0e769d9467eee44b4bfb31826009cde0e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>[125I]-angiotensin II</topic><topic>Aged</topic><topic>Angiotensin II - metabolism</topic><topic>angiotensin II receptors</topic><topic>Angiotensin Receptor Antagonists</topic><topic>cardiac hypertrophy</topic><topic>Cardiomegaly - metabolism</topic><topic>Down-Regulation - physiology</topic><topic>Female</topic><topic>human myocardium</topic><topic>Humans</topic><topic>Imidazoles - pharmacology</topic><topic>In Vitro Techniques</topic><topic>Iodine Radioisotopes</topic><topic>Iodocyanopindolol</topic><topic>Kinetics</topic><topic>Male</topic><topic>Membranes - metabolism</topic><topic>Middle Aged</topic><topic>Myocardium - metabolism</topic><topic>Pindolol - analogs & derivatives</topic><topic>Pyridines - pharmacology</topic><topic>receptor subtype</topic><topic>Receptors, Angiotensin - biosynthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nozawa, Yoshihisa</creatorcontrib><creatorcontrib>Miyake, Hidekazu</creatorcontrib><creatorcontrib>Haruno, Akihiro</creatorcontrib><creatorcontrib>Yamada, Shizuo</creatorcontrib><creatorcontrib>Uchida, Shinya</creatorcontrib><creatorcontrib>Ohkura, Takashi</creatorcontrib><creatorcontrib>Kimura, Ryohei</creatorcontrib><creatorcontrib>Suzuki, Harumi</creatorcontrib><creatorcontrib>Hoshino, Tsuneo</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Clinical and experimental pharmacology & physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nozawa, Yoshihisa</au><au>Miyake, Hidekazu</au><au>Haruno, Akihiro</au><au>Yamada, Shizuo</au><au>Uchida, Shinya</au><au>Ohkura, Takashi</au><au>Kimura, Ryohei</au><au>Suzuki, Harumi</au><au>Hoshino, Tsuneo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>DOWN-REGULATION OF ANGIOTENSIN II RECEPTORS IN HYPERTROPHIED HUMAN MYOCARDIUM</atitle><jtitle>Clinical and experimental pharmacology & physiology</jtitle><addtitle>Clin Exp Pharmacol Physiol</addtitle><date>1996-07</date><risdate>1996</risdate><volume>23</volume><issue>6-7</issue><spage>514</spage><epage>518</epage><pages>514-518</pages><issn>0305-1870</issn><eissn>1440-1681</eissn><abstract>SUMMARY
1. Specific [125I]‐angiotensin II (AngII) binding in normal and hypertrophied human myocardial membranes was saturable and of high affinity. Low concentrations of unlabelled AngII and saralasin competed with [125I]‐AngII for the binding sites in these tissues. Thus, saturable [125I]‐AngII binding in human myocardium exhibited pharmacological specificity that characterized high affinity receptors for AngII.
2. There was little difference in the apparent dissociation constant (Kd) values for [125I]‐AngII binding between normal and hypertrophied human myocardium, whereas the maximal number of binding sites (Bmax) was significantly (51%) lower in the hypertrophied group. Further, PD123177, a selective antagonist of the AT2 receptor subtype, showed three orders of magnitude higher affinity for [125I]‐AngII binding sites in both normal and hypertrophied myocardium than losartan, a selective antagonist of the AT1 receptor subtype; the Hill coefficients for these drugs were close to one.
3. A significant decrease in Bmax and Kd values for (—)‐[125I]‐iodocyanopindolol binding between normal and hypertrophied human myocardium rarely occurred.
4. The present study suggests that both normal and hypertrophied human myocardium predominantly contains the AT2 receptor subtype and that these receptors are down‐regulated in hypertrophied tissues.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>8800576</pmid><doi>10.1111/j.1440-1681.1996.tb02771.x</doi><tpages>5</tpages></addata></record> |
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| identifier | ISSN: 0305-1870 |
| ispartof | Clinical and experimental pharmacology & physiology, 1996-07, Vol.23 (6-7), p.514-518 |
| issn | 0305-1870 1440-1681 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78329484 |
| source | MEDLINE; Access via Wiley Online Library |
| subjects | [125I]-angiotensin II Aged Angiotensin II - metabolism angiotensin II receptors Angiotensin Receptor Antagonists cardiac hypertrophy Cardiomegaly - metabolism Down-Regulation - physiology Female human myocardium Humans Imidazoles - pharmacology In Vitro Techniques Iodine Radioisotopes Iodocyanopindolol Kinetics Male Membranes - metabolism Middle Aged Myocardium - metabolism Pindolol - analogs & derivatives Pyridines - pharmacology receptor subtype Receptors, Angiotensin - biosynthesis |
| title | DOWN-REGULATION OF ANGIOTENSIN II RECEPTORS IN HYPERTROPHIED HUMAN MYOCARDIUM |
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