Identification and characterization of a new binding site for angiotensin II in mouse neuroblastoma neuro-2A cells
Specific binding site for ^1^2^5I-angiotensin II (Ang II), with unique pharmacological properties uncommon to the hitherto recognized receptor subtypes, was observed in mouse neuroblastoma cells (Neuro-2A). Differentiation of the cells with 100 nM PGE"1 resulted in a 10-fold increase in the num...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
|---|
| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1992 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 182(1992), 1, Seite 388-394 |
| Übergeordnetes Werk: |
volume:182 ; year:1992 ; number:1 ; pages:388-394 |
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| 245 | 1 | 0 | |a Identification and characterization of a new binding site for angiotensin II in mouse neuroblastoma neuro-2A cells |
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| 520 | |a Specific binding site for ^1^2^5I-angiotensin II (Ang II), with unique pharmacological properties uncommon to the hitherto recognized receptor subtypes, was observed in mouse neuroblastoma cells (Neuro-2A). Differentiation of the cells with 100 nM PGE"1 resulted in a 10-fold increase in the number of Ang II binding sites without changing the binding affinity (Kd value: 12.0 nM). ^1^2^5I-Ang II binding to membranes of differentiated Neuro-2A was inhibited by unlabeled Ang II with a Ki value of 7.06 +/- 1.09 nM but not by Ang III (1 μM). Both AT"1 antagonist, Dup753, and AT"2 antagonist, PD123319, failed to inhibit ^1^2^5I-Ang II binding at 1 μM. ^1^2^5I-Ang II binding was not affected by GTP analogs such as GTPγS and Gpp(NH)p. These results suggest that Neuro-2A cells possess a binding site for Ang II which is different from the presently known subtypes of Ang II receptors, and that the number of the binding site is regulated by cell differentiation. | ||
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(DE-627)NLEJ18500122X (DE-599)GBVNLZ18500122X DE-627 ger DE-627 rakwb eng Identification and characterization of a new binding site for angiotensin II in mouse neuroblastoma neuro-2A cells 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Specific binding site for ^1^2^5I-angiotensin II (Ang II), with unique pharmacological properties uncommon to the hitherto recognized receptor subtypes, was observed in mouse neuroblastoma cells (Neuro-2A). Differentiation of the cells with 100 nM PGE"1 resulted in a 10-fold increase in the number of Ang II binding sites without changing the binding affinity (Kd value: 12.0 nM). ^1^2^5I-Ang II binding to membranes of differentiated Neuro-2A was inhibited by unlabeled Ang II with a Ki value of 7.06 +/- 1.09 nM but not by Ang III (1 μM). Both AT"1 antagonist, Dup753, and AT"2 antagonist, PD123319, failed to inhibit ^1^2^5I-Ang II binding at 1 μM. ^1^2^5I-Ang II binding was not affected by GTP analogs such as GTPγS and Gpp(NH)p. These results suggest that Neuro-2A cells possess a binding site for Ang II which is different from the presently known subtypes of Ang II receptors, and that the number of the binding site is regulated by cell differentiation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Chaki, S. oth Inagami, T. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 182(1992), 1, Seite 388-394 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:182 year:1992 number:1 pages:388-394 http://dx.doi.org/10.1016/S0006-291X(05)80157-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 182 1992 1 388-394 |
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(DE-627)NLEJ18500122X (DE-599)GBVNLZ18500122X DE-627 ger DE-627 rakwb eng Identification and characterization of a new binding site for angiotensin II in mouse neuroblastoma neuro-2A cells 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Specific binding site for ^1^2^5I-angiotensin II (Ang II), with unique pharmacological properties uncommon to the hitherto recognized receptor subtypes, was observed in mouse neuroblastoma cells (Neuro-2A). Differentiation of the cells with 100 nM PGE"1 resulted in a 10-fold increase in the number of Ang II binding sites without changing the binding affinity (Kd value: 12.0 nM). ^1^2^5I-Ang II binding to membranes of differentiated Neuro-2A was inhibited by unlabeled Ang II with a Ki value of 7.06 +/- 1.09 nM but not by Ang III (1 μM). Both AT"1 antagonist, Dup753, and AT"2 antagonist, PD123319, failed to inhibit ^1^2^5I-Ang II binding at 1 μM. ^1^2^5I-Ang II binding was not affected by GTP analogs such as GTPγS and Gpp(NH)p. These results suggest that Neuro-2A cells possess a binding site for Ang II which is different from the presently known subtypes of Ang II receptors, and that the number of the binding site is regulated by cell differentiation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Chaki, S. oth Inagami, T. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 182(1992), 1, Seite 388-394 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:182 year:1992 number:1 pages:388-394 http://dx.doi.org/10.1016/S0006-291X(05)80157-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 182 1992 1 388-394 |
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(DE-627)NLEJ18500122X (DE-599)GBVNLZ18500122X DE-627 ger DE-627 rakwb eng Identification and characterization of a new binding site for angiotensin II in mouse neuroblastoma neuro-2A cells 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Specific binding site for ^1^2^5I-angiotensin II (Ang II), with unique pharmacological properties uncommon to the hitherto recognized receptor subtypes, was observed in mouse neuroblastoma cells (Neuro-2A). Differentiation of the cells with 100 nM PGE"1 resulted in a 10-fold increase in the number of Ang II binding sites without changing the binding affinity (Kd value: 12.0 nM). ^1^2^5I-Ang II binding to membranes of differentiated Neuro-2A was inhibited by unlabeled Ang II with a Ki value of 7.06 +/- 1.09 nM but not by Ang III (1 μM). Both AT"1 antagonist, Dup753, and AT"2 antagonist, PD123319, failed to inhibit ^1^2^5I-Ang II binding at 1 μM. ^1^2^5I-Ang II binding was not affected by GTP analogs such as GTPγS and Gpp(NH)p. These results suggest that Neuro-2A cells possess a binding site for Ang II which is different from the presently known subtypes of Ang II receptors, and that the number of the binding site is regulated by cell differentiation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Chaki, S. oth Inagami, T. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 182(1992), 1, Seite 388-394 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:182 year:1992 number:1 pages:388-394 http://dx.doi.org/10.1016/S0006-291X(05)80157-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 182 1992 1 388-394 |
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(DE-627)NLEJ18500122X (DE-599)GBVNLZ18500122X DE-627 ger DE-627 rakwb eng Identification and characterization of a new binding site for angiotensin II in mouse neuroblastoma neuro-2A cells 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Specific binding site for ^1^2^5I-angiotensin II (Ang II), with unique pharmacological properties uncommon to the hitherto recognized receptor subtypes, was observed in mouse neuroblastoma cells (Neuro-2A). Differentiation of the cells with 100 nM PGE"1 resulted in a 10-fold increase in the number of Ang II binding sites without changing the binding affinity (Kd value: 12.0 nM). ^1^2^5I-Ang II binding to membranes of differentiated Neuro-2A was inhibited by unlabeled Ang II with a Ki value of 7.06 +/- 1.09 nM but not by Ang III (1 μM). Both AT"1 antagonist, Dup753, and AT"2 antagonist, PD123319, failed to inhibit ^1^2^5I-Ang II binding at 1 μM. ^1^2^5I-Ang II binding was not affected by GTP analogs such as GTPγS and Gpp(NH)p. These results suggest that Neuro-2A cells possess a binding site for Ang II which is different from the presently known subtypes of Ang II receptors, and that the number of the binding site is regulated by cell differentiation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Chaki, S. oth Inagami, T. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 182(1992), 1, Seite 388-394 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:182 year:1992 number:1 pages:388-394 http://dx.doi.org/10.1016/S0006-291X(05)80157-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 182 1992 1 388-394 |
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(DE-627)NLEJ18500122X (DE-599)GBVNLZ18500122X DE-627 ger DE-627 rakwb eng Identification and characterization of a new binding site for angiotensin II in mouse neuroblastoma neuro-2A cells 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Specific binding site for ^1^2^5I-angiotensin II (Ang II), with unique pharmacological properties uncommon to the hitherto recognized receptor subtypes, was observed in mouse neuroblastoma cells (Neuro-2A). Differentiation of the cells with 100 nM PGE"1 resulted in a 10-fold increase in the number of Ang II binding sites without changing the binding affinity (Kd value: 12.0 nM). ^1^2^5I-Ang II binding to membranes of differentiated Neuro-2A was inhibited by unlabeled Ang II with a Ki value of 7.06 +/- 1.09 nM but not by Ang III (1 μM). Both AT"1 antagonist, Dup753, and AT"2 antagonist, PD123319, failed to inhibit ^1^2^5I-Ang II binding at 1 μM. ^1^2^5I-Ang II binding was not affected by GTP analogs such as GTPγS and Gpp(NH)p. These results suggest that Neuro-2A cells possess a binding site for Ang II which is different from the presently known subtypes of Ang II receptors, and that the number of the binding site is regulated by cell differentiation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Chaki, S. oth Inagami, T. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 182(1992), 1, Seite 388-394 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:182 year:1992 number:1 pages:388-394 http://dx.doi.org/10.1016/S0006-291X(05)80157-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 182 1992 1 388-394 |
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identification and characterization of a new binding site for angiotensin ii in mouse neuroblastoma neuro-2a cells |
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Identification and characterization of a new binding site for angiotensin II in mouse neuroblastoma neuro-2A cells |
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Specific binding site for ^1^2^5I-angiotensin II (Ang II), with unique pharmacological properties uncommon to the hitherto recognized receptor subtypes, was observed in mouse neuroblastoma cells (Neuro-2A). Differentiation of the cells with 100 nM PGE"1 resulted in a 10-fold increase in the number of Ang II binding sites without changing the binding affinity (Kd value: 12.0 nM). ^1^2^5I-Ang II binding to membranes of differentiated Neuro-2A was inhibited by unlabeled Ang II with a Ki value of 7.06 +/- 1.09 nM but not by Ang III (1 μM). Both AT"1 antagonist, Dup753, and AT"2 antagonist, PD123319, failed to inhibit ^1^2^5I-Ang II binding at 1 μM. ^1^2^5I-Ang II binding was not affected by GTP analogs such as GTPγS and Gpp(NH)p. These results suggest that Neuro-2A cells possess a binding site for Ang II which is different from the presently known subtypes of Ang II receptors, and that the number of the binding site is regulated by cell differentiation. |
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Specific binding site for ^1^2^5I-angiotensin II (Ang II), with unique pharmacological properties uncommon to the hitherto recognized receptor subtypes, was observed in mouse neuroblastoma cells (Neuro-2A). Differentiation of the cells with 100 nM PGE"1 resulted in a 10-fold increase in the number of Ang II binding sites without changing the binding affinity (Kd value: 12.0 nM). ^1^2^5I-Ang II binding to membranes of differentiated Neuro-2A was inhibited by unlabeled Ang II with a Ki value of 7.06 +/- 1.09 nM but not by Ang III (1 μM). Both AT"1 antagonist, Dup753, and AT"2 antagonist, PD123319, failed to inhibit ^1^2^5I-Ang II binding at 1 μM. ^1^2^5I-Ang II binding was not affected by GTP analogs such as GTPγS and Gpp(NH)p. These results suggest that Neuro-2A cells possess a binding site for Ang II which is different from the presently known subtypes of Ang II receptors, and that the number of the binding site is regulated by cell differentiation. |
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Specific binding site for ^1^2^5I-angiotensin II (Ang II), with unique pharmacological properties uncommon to the hitherto recognized receptor subtypes, was observed in mouse neuroblastoma cells (Neuro-2A). Differentiation of the cells with 100 nM PGE"1 resulted in a 10-fold increase in the number of Ang II binding sites without changing the binding affinity (Kd value: 12.0 nM). ^1^2^5I-Ang II binding to membranes of differentiated Neuro-2A was inhibited by unlabeled Ang II with a Ki value of 7.06 +/- 1.09 nM but not by Ang III (1 μM). Both AT"1 antagonist, Dup753, and AT"2 antagonist, PD123319, failed to inhibit ^1^2^5I-Ang II binding at 1 μM. ^1^2^5I-Ang II binding was not affected by GTP analogs such as GTPγS and Gpp(NH)p. These results suggest that Neuro-2A cells possess a binding site for Ang II which is different from the presently known subtypes of Ang II receptors, and that the number of the binding site is regulated by cell differentiation. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ18500122X</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506145237.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1992 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ18500122X</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ18500122X</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Identification and characterization of a new binding site for angiotensin II in mouse neuroblastoma neuro-2A cells</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1992</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Specific binding site for ^1^2^5I-angiotensin II (Ang II), with unique pharmacological properties uncommon to the hitherto recognized receptor subtypes, was observed in mouse neuroblastoma cells (Neuro-2A). Differentiation of the cells with 100 nM PGE"1 resulted in a 10-fold increase in the number of Ang II binding sites without changing the binding affinity (Kd value: 12.0 nM). ^1^2^5I-Ang II binding to membranes of differentiated Neuro-2A was inhibited by unlabeled Ang II with a Ki value of 7.06 +/- 1.09 nM but not by Ang III (1 μM). Both AT"1 antagonist, Dup753, and AT"2 antagonist, PD123319, failed to inhibit ^1^2^5I-Ang II binding at 1 μM. ^1^2^5I-Ang II binding was not affected by GTP analogs such as GTPγS and Gpp(NH)p. These results suggest that Neuro-2A cells possess a binding site for Ang II which is different from the presently known subtypes of Ang II receptors, and that the number of the binding site is regulated by cell differentiation.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chaki, S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Inagami, T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochemical and Biophysical Research Communications</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">182(1992), 1, Seite 388-394</subfield><subfield code="w">(DE-627)NLEJ176855645</subfield><subfield code="w">(DE-600)1461396-7</subfield><subfield code="x">0006-291X</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:182</subfield><subfield code="g">year:1992</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:388-394</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/S0006-291X(05)80157-3</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">182</subfield><subfield code="j">1992</subfield><subfield code="e">1</subfield><subfield code="h">388-394</subfield></datafield></record></collection>
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7.399028 |