Ryanodine binding sites measured in small skeletal muscle biopsies
A method allowing measurement of the concentration of [3H]ryanodine binding sites in small skeletal muscle specimens (<10-20 mg) was developed. A membrane fraction containing 87% of the [3H]ryanodine binding sites of the tissue and exhibiting one single KD of 18-27 nmol I-1 in rat and 8 nmol I-1...
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| Published in: | Scandinavian journal of clinical and laboratory investigation Vol. 57; no. 7; pp. 569 - 580 |
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| Main Authors: | , |
| Format: | Journal Article |
| Language: | English |
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Informa UK Ltd
1997
Taylor & Francis Scandinavian University Press |
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| Abstract | A method allowing measurement of the concentration of [3H]ryanodine binding sites in small skeletal muscle specimens (<10-20 mg) was developed. A membrane fraction containing 87% of the [3H]ryanodine binding sites of the tissue and exhibiting one single KD of 18-27 nmol I-1 in rat and 8 nmol I-1 in human muscles (p < 0.05) was obtained. Maximum binding to rat EDL and soleus muscles equalled 59.1 and 16.2 pmol g-1 wet wt, whereas in human gluteus muscles binding was 12.3 pmol g-1 wet wt. The [3H]ryanodine binding showed a dependency on Mg2+ and pH similar to previously published results. As measured by Ca2+ selective mini-electrodes, the [Ca2+] causing 50% of maximum [3H]ryanodine binding (K0.5) was 200-400 nmol I-1 for different muscles. [Ca2+] higher than 1 mmol I-1 caused strong inhibition of the [3H]ryanodine binding, and both high and low [Ca2+] caused rapid dissociation of the complex. At ionic strength lower than 100 mmol I-1, more than 50% of the [3H]ryanodine was bound to particles with size less than 1.2 μn which were not retained by GF/C filters. Thus, we have obtained an almost complete quantitative recovery of functional RyRs from small muscle specimens exhibiting high affinity for Ca2+, which stimulated ligand binding. |
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| AbstractList | A method allowing measurement of the concentration of [3H]ryanodine binding sites in small skeletal muscle specimens (> 10-20 mg) was developed. A membrane fraction containing 87% of the [3H]ryanodine binding sites of the tissue and exhibiting one single KD of 18-27 nmol l-1 in rat and 8 nmol l-1 in human muscles (p < 0.05) was obtained. Maximum binding to rat EDL and soleus muscles equalled 59.1 and 16.2 pmol g-1 wet wt, whereas in human gluteus muscles binding was 12.3 pmol g-1 wet wt. The [3H]ryanodine binding showed a dependency on Mg2+ and pH similar to previously published results. As measured by Ca2+ selective mini-electrodes, the [Ca2+] causing 50% of maximum [3H]ryanodine binding (K0.5) was 200-400 nmol l-1 for different muscles. [Ca2+] higher than 1 mmol l-1 caused strong inhibition of the [3H]ryanodine binding, and both high and low [Ca2+] caused rapid dissociation of the complex. At ionic strength lower than 100 mmol l-1, more than 50% of the [3H]ryanodine was bound to particles with size less than 1.2 microns which were not retained by GF/C filters. Thus, we have obtained an almost complete quantitative recovery of functional RyRs from small muscle specimens exhibiting high affinity for Ca2+, which stimulated ligand binding. A method allowing measurement of the concentration of [ 3 H]ryanodine binding sites in small skeletal muscle specimens (<10-20 mg) was developed. A membrane fraction containing 87% of the [ 3 H]ryanodine binding sites of the tissue and exhibiting one single K D of 18-27 nmol I -1 in rat and 8 nmol I -1 in human muscles (p < 0.05) was obtained. Maximum binding to rat EDL and soleus muscles equalled 59.1 and 16.2 pmol g -1 wet wt, whereas in human gluteus muscles binding was 12.3 pmol g -1 wet wt. The [ 3 H]ryanodine binding showed a dependency on Mg 2+ and pH similar to previously published results. As measured by Ca 2+ selective mini-electrodes, the [Ca 2+ ] causing 50% of maximum [ 3 H]ryanodine binding (K 0.5 ) was 200-400 nmol I -1 for different muscles. [Ca 2+ ] higher than 1 mmol I -1 caused strong inhibition of the [ 3 H]ryanodine binding, and both high and low [Ca 2+ ] caused rapid dissociation of the complex. At ionic strength lower than 100 mmol I -1 , more than 50% of the [ 3 H]ryanodine was bound to particles with size less than 1.2 μn which were not retained by GF/C filters. Thus, we have obtained an almost complete quantitative recovery of functional RyRs from small muscle specimens exhibiting high affinity for Ca 2+ , which stimulated ligand binding. A method allowing measurement of the concentration of [3H]ryanodine binding sites in small skeletal muscle specimens (<10-20 mg) was developed. A membrane fraction containing 87% of the [3H]ryanodine binding sites of the tissue and exhibiting one single KD of 18-27 nmol I-1 in rat and 8 nmol I-1 in human muscles (p < 0.05) was obtained. Maximum binding to rat EDL and soleus muscles equalled 59.1 and 16.2 pmol g-1 wet wt, whereas in human gluteus muscles binding was 12.3 pmol g-1 wet wt. The [3H]ryanodine binding showed a dependency on Mg2+ and pH similar to previously published results. As measured by Ca2+ selective mini-electrodes, the [Ca2+] causing 50% of maximum [3H]ryanodine binding (K0.5) was 200-400 nmol I-1 for different muscles. [Ca2+] higher than 1 mmol I-1 caused strong inhibition of the [3H]ryanodine binding, and both high and low [Ca2+] caused rapid dissociation of the complex. At ionic strength lower than 100 mmol I-1, more than 50% of the [3H]ryanodine was bound to particles with size less than 1.2 μn which were not retained by GF/C filters. Thus, we have obtained an almost complete quantitative recovery of functional RyRs from small muscle specimens exhibiting high affinity for Ca2+, which stimulated ligand binding. A method allowing measurement of the concentration of [3H]ryanodine binding sites in small skeletal muscle specimens (> 10-20 mg) was developed. A membrane fraction containing 87% of the [3H]ryanodine binding sites of the tissue and exhibiting one single KD of 18-27 nmol l-1 in rat and 8 nmol l-1 in human muscles (p < 0.05) was obtained. Maximum binding to rat EDL and soleus muscles equalled 59.1 and 16.2 pmol g-1 wet wt, whereas in human gluteus muscles binding was 12.3 pmol g-1 wet wt. The [3H]ryanodine binding showed a dependency on Mg2+ and pH similar to previously published results. As measured by Ca2+ selective mini-electrodes, the [Ca2+] causing 50% of maximum [3H]ryanodine binding (K0.5) was 200-400 nmol l-1 for different muscles. [Ca2+] higher than 1 mmol l-1 caused strong inhibition of the [3H]ryanodine binding, and both high and low [Ca2+] caused rapid dissociation of the complex. At ionic strength lower than 100 mmol l-1, more than 50% of the [3H]ryanodine was bound to particles with size less than 1.2 microns which were not retained by GF/C filters. Thus, we have obtained an almost complete quantitative recovery of functional RyRs from small muscle specimens exhibiting high affinity for Ca2+, which stimulated ligand binding. |
| Author | Lunde, P. K. Sejersted, O. M. |
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| Cites_doi | 10.1016/S0021-9258(19)52451-6 10.1042/bj2600443 10.1007/BF00242517 10.1016/S0006-3495(90)82563-7 10.1042/bj2850061 10.1007/BF00583469 10.1016/0005-2736(88)90106-X 10.1152/ajpcell.1991.261.2.C237 10.1152/physrev.1986.66.3.542 10.1016/0003-2697(76)90527-3 10.1111/j.1432-1033.1993.tb17744.x 10.1096/fasebj.8.11.8070630 10.1007/BF00130421 10.1085/jgp.88.5.573 10.1152/ajpcell.1991.261.2.C195 10.1021/ac00124a036 10.1038/227680a0 10.1016/0006-291X(85)91699-7 10.1083/jcb.99.3.875 10.1093/oxfordjournals.jbchem.a123144 10.1016/S0021-9258(19)84563-5 10.1021/bi00430a039 10.1016/0003-2697(89)90167-X 10.1007/BF01872638 10.1016/0006-291X(91)91644-R 10.1152/physrev.1996.76.2.537 10.1016/0076-6879(88)57093-3 |
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| Copyright | 1997 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted 1997 1998 INIST-CNRS |
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| Keywords | Human Ryanodine Vertebrata Mammalia Calcium ion Rat Biopsy Rodentia Ionic channel Binding site Striated muscle Quantitative analysis |
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| Snippet | A method allowing measurement of the concentration of [3H]ryanodine binding sites in small skeletal muscle specimens (<10-20 mg) was developed. A membrane... A method allowing measurement of the concentration of [ 3 H]ryanodine binding sites in small skeletal muscle specimens (<10-20 mg) was developed. A membrane... A method allowing measurement of the concentration of [3H]ryanodine binding sites in small skeletal muscle specimens (> 10-20 mg) was developed. A membrane... A method allowing measurement of the concentration of [3H]ryanodine binding sites in small skeletal muscle specimens (> 10-20 mg) was developed. A membrane... |
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| SubjectTerms | Adenosine Triphosphate - pharmacology Animals Binding, Competitive - drug effects Binding, Competitive - physiology Biological and medical sciences Biopsy, Needle Calcium - pharmacology Cholic Acids Cryopreservation Detergents EDL Egtazic Acid - analogs & derivatives Fundamental and applied biological sciences. Psychology Humans Hydrogen-Ion Concentration Indicators and Reagents Magnesium - pharmacology muscle biopsies Muscle, Skeletal - chemistry Muscle, Skeletal - pathology Octoxynol Poloxalene Potassium Chloride - pharmacology Rats Rats, Wistar ryanodine receptor Ryanodine Receptor Calcium Release Channel - analysis Ryanodine Receptor Calcium Release Channel - metabolism Sarcoplasmic Reticulum - chemistry Soleus Striated muscle. Tendons Time Factors Tritium Vertebrates: osteoarticular system, musculoskeletal system |
| Title | Ryanodine binding sites measured in small skeletal muscle biopsies |
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