What is the clinical evidence from this study?

Study design: Other. Population: Malignant hyperthermia. Intervention: Gly2434→ Arg mutation in RYR1. Primary outcome: Sensitivity of RYR1 to activating and inhibiting concentrations of Ca2+ and ligands.

February 1, 1997Journal of Biological ChemistryOpen Access

Functional Characterization of a Distinct Ryanodine Receptor Mutation in Human Malignant Hyperthermia-susceptible Muscle

View Full Paper

Ask AI

Bookmark

Key result

The Gly2434→ Arg mutation in RYR1 enhanced sensitivity to activating Ca2+ and ligands while reducing sensitivity to inhibiting Ca2+ and calmodulin, creating a hyperexcitable channel.

Population

Human malignant hyperthermia-susceptible skeletal muscle with RYR1 Gly2434→ Arg mutation

Design

Preclinical

Authors

MRMichael RichterFraunhofer Institute for Interfacial Engineering and Biotechnology LSLothar SchleithoffKarlsruhe Institute of Technology TDThomas DeufelJena University Hospital

Discussion

Member takes

Implication

Hypothesis-generating for RYR1 variant effects in malignant hyperthermia; leaves open clinical testing utility pending validation.

Structured PICO

Population

Human malignant hyperthermia-susceptible skeletal muscle with RYR1 Gly2434→ Arg mutation

Exposure

High affinity [3H]ryanodine binding assay and exposure to Ca2+, caffeine, 4-chloro-m-cresol, and calmodulin

Outcome

Sensitivity of RYR1 to activating and inhibiting concentrations of Ca2+ and ligandssurrogate

The RYR1 Gly2434→ Arg mutation causes malignant hyperthermia susceptibility by transferring the Ca2+ release channel into a hyperexcitable state.

Cite This Study

Richter et al. (1997) studied Malignant hyperthermia. Gly2434→ Arg mutation in RYR1 was evaluated on Sensitivity of RYR1 to activating and inhibiting concentrations of Ca2+ and ligands. The Gly2434→ Arg mutation in RYR1 enhanced sensitivity to activating Ca2+ and ligands while reducing sensitivity to inhibiting Ca2+ and calmodulin, creating a hyperexcitable channel.

synapsesocial.com/papers/6a5f30ef531077db68af3bb3 https://doi.org/10.1074/jbc.272.8.5256

View Full Paper

Ask AI

Bookmark

February 1, 1997Journal of Biological ChemistryOpen Access

Functional Characterization of a Distinct Ryanodine Receptor Mutation in Human Malignant Hyperthermia-susceptible Muscle

View Full Paper

Ask AI

Bookmark

Key result

The Gly2434→ Arg mutation in RYR1 enhanced sensitivity to activating Ca2+ and ligands while reducing sensitivity to inhibiting Ca2+ and calmodulin, creating a hyperexcitable channel.

Population

Human malignant hyperthermia-susceptible skeletal muscle with RYR1 Gly2434→ Arg mutation

Design

Preclinical

Authors

MRMichael RichterFraunhofer Institute for Interfacial Engineering and Biotechnology LSLothar SchleithoffKarlsruhe Institute of Technology TDThomas DeufelJena University Hospital

Discussion

Member takes

Implication

Hypothesis-generating for RYR1 variant effects in malignant hyperthermia; leaves open clinical testing utility pending validation.

Structured PICO

Population

Human malignant hyperthermia-susceptible skeletal muscle with RYR1 Gly2434→ Arg mutation

Exposure

High affinity [3H]ryanodine binding assay and exposure to Ca2+, caffeine, 4-chloro-m-cresol, and calmodulin

Outcome

Sensitivity of RYR1 to activating and inhibiting concentrations of Ca2+ and ligandssurrogate

The RYR1 Gly2434→ Arg mutation causes malignant hyperthermia susceptibility by transferring the Ca2+ release channel into a hyperexcitable state.

Cite This Study

synapsesocial.com/papers/6a5f30ef531077db68af3bb3 https://doi.org/10.1074/jbc.272.8.5256

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

View Full Paper

Ask AI

Bookmark