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Heterogeneous halothane binding in the SR Ca2+-ATPase

D Kosk-Kosicka¹, I Fomitcheva, M M Lopez

¹Johns Hopkins University, School of Medicine, Dept. of Anesthesiology/CCM, Baltimore, MD 21287-4961, USA. dkk@welchlink.welch.jhu.edu

|February 3, 1997

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This study provides direct evidence that halothane, a volatile anesthetic, binds to the skeletal muscle sarcoplasmic reticulum Ca2+-ATPase (SERCA1). This binding may explain the anesthetic

Area of Science:

Biochemistry
Molecular Biology
Anesthesiology

Background:

Volatile anesthetics like halothane affect Ca2+-ATPases, with biphasic effects on skeletal muscle sarcoplasmic reticulum (SR) Ca2+-ATPase (SERCA1).
Previous work suggested volatile anesthetics bind within the Ca2+-ATPase molecule.

Purpose of the Study:

To investigate direct binding of halothane to SERCA1.
To provide evidence for the interaction between halothane and SERCA1.

Main Methods:

Photoaffinity labeling of SR membranes with [14C]halothane.
SDS-gel electrophoresis to quantify halothane incorporation into SERCA1 and lipids.
Tryptic digestion of labeled SERCA1 to analyze binding site heterogeneity.

Main Results:

Related Experiment Videos

Halothane binds saturably to SR membranes with approximately 80% specific binding (KI = 0.6 mM).
38-56% of [14C]halothane incorporated into SERCA1, and 38-53% into lipids.
Tryptic digestion revealed heterogeneous halothane binding to SERCA1, suggesting discrete binding sites.

Conclusions:

Direct evidence confirms halothane binds to SERCA1.
This binding is likely related to the anesthetic's effect on SERCA1 function.