author_facet HAARMANN, Claudia S.
GREEN, Daniel
CASAROTTO, Marco G.
LAVER, Derek R.
DULHUNTY, Angela F.
HAARMANN, Claudia S.
GREEN, Daniel
CASAROTTO, Marco G.
LAVER, Derek R.
DULHUNTY, Angela F.
author HAARMANN, Claudia S.
GREEN, Daniel
CASAROTTO, Marco G.
LAVER, Derek R.
DULHUNTY, Angela F.
spellingShingle HAARMANN, Claudia S.
GREEN, Daniel
CASAROTTO, Marco G.
LAVER, Derek R.
DULHUNTY, Angela F.
Biochemical Journal
The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
Cell Biology
Molecular Biology
Biochemistry
author_sort haarmann, claudia s.
spelling HAARMANN, Claudia S. GREEN, Daniel CASAROTTO, Marco G. LAVER, Derek R. DULHUNTY, Angela F. 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj20021763 <jats:p>The actions of peptide C, corresponding to 724Glu–Pro760 of the II–III loop of the skeletal dihydropyridine receptor, on ryanodine receptor (RyR) channels incorporated into lipid bilayers with the native sarcoplasmic reticulum membrane show that the peptide is a high-affinity activator of native skeletal RyRs at cytoplasmic concentrations of 100 nM–10 μM. In addition, we found that peptide C inhibits RyRs in a voltage-independent manner when added for longer times or at higher concentrations (up to 150 μM). Peptide C had a random-coil structure indicating that it briefly assumes a variety of structures, some of which might activate and others which might inhibit RyRs. The results suggest that RyR activation and inhibition by peptide C arise from independent stochastic processes. A rate constant of 7.5×105 s−1·M−1 was obtained for activation and a lower estimate for the rate constant for inhibition of 5.9×103 s−1·M−1. The combined actions of peptide C and peptide A (II–III loop sequence 671Thr–Leu690) showed that peptide C prevented activation but not blockage of RyRs by peptide A. We suggest that the effects of peptide C indicate functional interactions between a part of the dihydropyridine receptor and the RyR. These interactions could reflect either dynamic changes that occur during excitation–contraction coupling or interactions between the proteins at rest.</jats:p> The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors Biochemical Journal
doi_str_mv 10.1042/bj20021763
facet_avail Online
Free
finc_class_facet Biologie
Chemie und Pharmazie
format ElectronicArticle
fullrecord blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Mi9iajIwMDIxNzYz
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Mi9iajIwMDIxNzYz
institution DE-D275
DE-Bn3
DE-Brt1
DE-D161
DE-Zwi2
DE-Gla1
DE-Zi4
DE-15
DE-Pl11
DE-Rs1
DE-105
DE-14
DE-Ch1
DE-L229
imprint Portland Press Ltd., 2003
imprint_str_mv Portland Press Ltd., 2003
issn 0264-6021
1470-8728
issn_str_mv 0264-6021
1470-8728
language English
mega_collection Portland Press Ltd. (CrossRef)
match_str haarmann2003therandomcoilcfragmentofthedihydropyridinereceptoriiiiiloopcanactivateorinhibitnativeskeletalryanodinereceptors
publishDateSort 2003
publisher Portland Press Ltd.
recordtype ai
record_format ai
series Biochemical Journal
source_id 49
title The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
title_unstemmed The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
title_full The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
title_fullStr The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
title_full_unstemmed The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
title_short The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
title_sort the random-coil ‘c’ fragment of the dihydropyridine receptor ii-iii loop can activate or inhibit native skeletal ryanodine receptors
topic Cell Biology
Molecular Biology
Biochemistry
url http://dx.doi.org/10.1042/bj20021763
publishDate 2003
physical 305-316
description <jats:p>The actions of peptide C, corresponding to 724Glu–Pro760 of the II–III loop of the skeletal dihydropyridine receptor, on ryanodine receptor (RyR) channels incorporated into lipid bilayers with the native sarcoplasmic reticulum membrane show that the peptide is a high-affinity activator of native skeletal RyRs at cytoplasmic concentrations of 100 nM–10 μM. In addition, we found that peptide C inhibits RyRs in a voltage-independent manner when added for longer times or at higher concentrations (up to 150 μM). Peptide C had a random-coil structure indicating that it briefly assumes a variety of structures, some of which might activate and others which might inhibit RyRs. The results suggest that RyR activation and inhibition by peptide C arise from independent stochastic processes. A rate constant of 7.5×105 s−1·M−1 was obtained for activation and a lower estimate for the rate constant for inhibition of 5.9×103 s−1·M−1. The combined actions of peptide C and peptide A (II–III loop sequence 671Thr–Leu690) showed that peptide C prevented activation but not blockage of RyRs by peptide A. We suggest that the effects of peptide C indicate functional interactions between a part of the dihydropyridine receptor and the RyR. These interactions could reflect either dynamic changes that occur during excitation–contraction coupling or interactions between the proteins at rest.</jats:p>
container_issue 2
container_start_page 305
container_title Biochemical Journal
container_volume 372
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
_version_ 1792341374337548288
geogr_code not assigned
last_indexed 2024-03-01T16:18:54.914Z
geogr_code_person not assigned
openURL url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=The+random-coil+%E2%80%98C%E2%80%99+fragment+of+the+dihydropyridine+receptor+II-III+loop+can+activate+or+inhibit+native+skeletal+ryanodine+receptors&rft.date=2003-06-01&genre=article&issn=1470-8728&volume=372&issue=2&spage=305&epage=316&pages=305-316&jtitle=Biochemical+Journal&atitle=The+random-coil+%E2%80%98C%E2%80%99+fragment+of+the+dihydropyridine+receptor+II-III+loop+can+activate+or+inhibit+native+skeletal+ryanodine+receptors&aulast=DULHUNTY&aufirst=Angela+F.&rft_id=info%3Adoi%2F10.1042%2Fbj20021763&rft.language%5B0%5D=eng
SOLR
_version_ 1792341374337548288
author HAARMANN, Claudia S., GREEN, Daniel, CASAROTTO, Marco G., LAVER, Derek R., DULHUNTY, Angela F.
author_facet HAARMANN, Claudia S., GREEN, Daniel, CASAROTTO, Marco G., LAVER, Derek R., DULHUNTY, Angela F., HAARMANN, Claudia S., GREEN, Daniel, CASAROTTO, Marco G., LAVER, Derek R., DULHUNTY, Angela F.
author_sort haarmann, claudia s.
container_issue 2
container_start_page 305
container_title Biochemical Journal
container_volume 372
description <jats:p>The actions of peptide C, corresponding to 724Glu–Pro760 of the II–III loop of the skeletal dihydropyridine receptor, on ryanodine receptor (RyR) channels incorporated into lipid bilayers with the native sarcoplasmic reticulum membrane show that the peptide is a high-affinity activator of native skeletal RyRs at cytoplasmic concentrations of 100 nM–10 μM. In addition, we found that peptide C inhibits RyRs in a voltage-independent manner when added for longer times or at higher concentrations (up to 150 μM). Peptide C had a random-coil structure indicating that it briefly assumes a variety of structures, some of which might activate and others which might inhibit RyRs. The results suggest that RyR activation and inhibition by peptide C arise from independent stochastic processes. A rate constant of 7.5×105 s−1·M−1 was obtained for activation and a lower estimate for the rate constant for inhibition of 5.9×103 s−1·M−1. The combined actions of peptide C and peptide A (II–III loop sequence 671Thr–Leu690) showed that peptide C prevented activation but not blockage of RyRs by peptide A. We suggest that the effects of peptide C indicate functional interactions between a part of the dihydropyridine receptor and the RyR. These interactions could reflect either dynamic changes that occur during excitation–contraction coupling or interactions between the proteins at rest.</jats:p>
doi_str_mv 10.1042/bj20021763
facet_avail Online, Free
finc_class_facet Biologie, Chemie und Pharmazie
format ElectronicArticle
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
geogr_code not assigned
geogr_code_person not assigned
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Mi9iajIwMDIxNzYz
imprint Portland Press Ltd., 2003
imprint_str_mv Portland Press Ltd., 2003
institution DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Zwi2, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229
issn 0264-6021, 1470-8728
issn_str_mv 0264-6021, 1470-8728
language English
last_indexed 2024-03-01T16:18:54.914Z
match_str haarmann2003therandomcoilcfragmentofthedihydropyridinereceptoriiiiiloopcanactivateorinhibitnativeskeletalryanodinereceptors
mega_collection Portland Press Ltd. (CrossRef)
physical 305-316
publishDate 2003
publishDateSort 2003
publisher Portland Press Ltd.
record_format ai
recordtype ai
series Biochemical Journal
source_id 49
spelling HAARMANN, Claudia S. GREEN, Daniel CASAROTTO, Marco G. LAVER, Derek R. DULHUNTY, Angela F. 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj20021763 <jats:p>The actions of peptide C, corresponding to 724Glu–Pro760 of the II–III loop of the skeletal dihydropyridine receptor, on ryanodine receptor (RyR) channels incorporated into lipid bilayers with the native sarcoplasmic reticulum membrane show that the peptide is a high-affinity activator of native skeletal RyRs at cytoplasmic concentrations of 100 nM–10 μM. In addition, we found that peptide C inhibits RyRs in a voltage-independent manner when added for longer times or at higher concentrations (up to 150 μM). Peptide C had a random-coil structure indicating that it briefly assumes a variety of structures, some of which might activate and others which might inhibit RyRs. The results suggest that RyR activation and inhibition by peptide C arise from independent stochastic processes. A rate constant of 7.5×105 s−1·M−1 was obtained for activation and a lower estimate for the rate constant for inhibition of 5.9×103 s−1·M−1. The combined actions of peptide C and peptide A (II–III loop sequence 671Thr–Leu690) showed that peptide C prevented activation but not blockage of RyRs by peptide A. We suggest that the effects of peptide C indicate functional interactions between a part of the dihydropyridine receptor and the RyR. These interactions could reflect either dynamic changes that occur during excitation–contraction coupling or interactions between the proteins at rest.</jats:p> The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors Biochemical Journal
spellingShingle HAARMANN, Claudia S., GREEN, Daniel, CASAROTTO, Marco G., LAVER, Derek R., DULHUNTY, Angela F., Biochemical Journal, The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors, Cell Biology, Molecular Biology, Biochemistry
title The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
title_full The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
title_fullStr The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
title_full_unstemmed The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
title_short The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
title_sort the random-coil ‘c’ fragment of the dihydropyridine receptor ii-iii loop can activate or inhibit native skeletal ryanodine receptors
title_unstemmed The random-coil ‘C’ fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
topic Cell Biology, Molecular Biology, Biochemistry
url http://dx.doi.org/10.1042/bj20021763