Imperatoxin A (IpTxa ) from Pandinus imperator stimulates [3 H]ryanodine binding to RyR3 channels
Autor: | Jesús García, Vincenzo Sorrentino, Xinsheng Zhu, Daniela Rossi, Héctor H. Valdivia, Ilenia Simeoni |
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Rok vydání: | 2001 |
Předmět: |
genetics/metabolism
Stimulation medicine.disease_cause Biochemistry Ryanodine receptor 2 Structural Biology Protein Isoforms Cells Cultured Cultured Ryanodine Ryanodine receptor Skeletal musculoskeletal system Immunohistochemistry Electrophysiology chemistry/metabolism Muscle Calcium release channel tissues Excitation contraction coupling chemistry/drug effects medicine.medical_specialty animal structures Cells Sarcoplasmic reticulum Biophysics Scorpion Venoms chemistry.chemical_element Calcium chemistry Tritium Scorpions Microsomes Internal medicine Genetics medicine Animals Muscle Skeletal Molecular Biology RYR1 Toxin Endoplasmic reticulum T-type calcium channel Ryanodine Receptor Calcium Release Channel Cell Biology Animals Calcium metabolism Cattle Cells Cultured Electrophysiology Immunohistochemistry Microsomes chemistry/drug effects Muscle metabolism Protein Isoforms metabolism Ryanodine Receptor Calcium Release Channel genetics/metabolism Ryanodine chemistry/metabolism Scorpion Venoms pharmacology Scorpions chemistry Tritium Endocrinology Cattle pharmacology metabolism |
Zdroj: | FEBS Letters. 508:5-10 |
ISSN: | 0014-5793 |
DOI: | 10.1016/s0014-5793(01)03013-7 |
Popis: | The effect of imperatoxin A (IpTx(a)) on the ryanodine receptor type 3 (RyR3) was studied. IpTx(a) stimulates [(3)H]ryanodine binding to RyR3-containing microsomes, but this effect requires toxin concentrations higher than those required to stimulate RyR1 channels. The effect of IpTx(a) on RyR3 channels was observed at calcium concentrations in the range 0.1 microM to 10 mM. By contrast, RyR2 channels were not significantly affected by IpTx(a) in the same calcium ranges. Single channel current measurements indicated that IpTx(a) induced subconductance state in RyR3 channels that was similar to those observed with RyR1 and RyR2 channels. These results indicate that IpTx(a) is capable of inducing similar subconductance states in all three RyR isoforms, while stimulation of [(3)H]ryanodine binding by this toxin results in isoform-specific responses, with RyR1 being the most sensitive channel, RyR3 displaying an intermediate response and RyR2 the least responsive ones. |
Databáze: | OpenAIRE |
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