西亚试剂：Capsaicin stimulates uncoupled ATP hydrolysis by sarcoplasm

发布时间：2025-06-07

Capsaicin stimulates uncoupled ATP hydrolysis by sarcoplasmic reticulum calcium pump

Yasser Ahmed Mahmmoud

Institute of Physiology and Biophysics, University of Aarhus, Aarhus C DK-8000

Corresponding Author: yam@biophys.au.dk

In muscle cells, the sarcoplasmic reticulum (SR) Ca2+-ATPase (SERCA) couples the free energy of ATP hydrolysis to pump Ca2+ ions from the cytoplasm to the SR lumen. In addition, SERCA plays a key role in non-shivering thermogenesis through uncoupled reactions, where ATP hydrolysis takes place without active Ca2+ translocation. Capsaicin (CPS) is a naturally occurring vanilloid, the consumption of which is linked with increased metabolic rate and core body temperature. Here, we document the stimulation by CPS of the Ca2+-dependent ATP hydrolysis by SERCA without effects on Ca2+ accumulation. The stimulation by CPS was significantly dependent on the presence of a Ca2+ gradient across the SR membrane. ATP activation assays showed that the drug reduced the nucleotide affinity at the catalytic site whereas the affinity at the regulatory site increased. Several biochemical analyses indicated that CPS stabilizes an ADP-insensitive E2P related conformation that dephosphorylates at a higher rate than the control enzyme. Under conditions where uncoupled SERCA was specifically inhibited by the treatment with fluoride, low temperatures, or dimethyl sulfoxide, CPS had no stimulatory effect on ATP hydrolysis by SERCA. It is concluded that CPS stabilizes a SERCA sub-conformation where Ca2+ is released from the phosphorylated intermediate to the cytoplasm instead of the SR lumen, increasing ATP hydrolysis not coupled with Ca2+ transport. To the best of our knowledge, CPS is the first natural drug that augments uncoupled SERCA, presumably resulting in thermogenesis. The role of CPS as a SERCA modulator is discussed. Bioon.com

 

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