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SERCA2a was serotonylated and may regulate sino-atrial node pacemaker activity.

Qingjie Wang1, Dong Wang2, Gaoliang Yan2

  • 1Department of Cardiology, Changzhou Second Hospital of Nanjing Medical University, Gehu Road, 213004, Changzhou, Jiangsu, China; Department of Cardiology, Zhongda Hospital of Southeast University Medical School, Dingjiaqiao Road, 210009, Nanjing, Jiangsu, China.

Biochemical and Biophysical Research Communications
|November 6, 2016
PubMed
Summary

Protein serotonylation, a process involving intracellular 5-HT, impacts heart rate by modifying SERCA2a. This modification in calcium handling by the sarco(endo)plasmic reticulum Ca ATPase type 2a (SERCA2a) pump influences sino-atrial node (SAN) automaticity.

Keywords:
Pacemaker activitySarco(endo)plasmic reticulum Ca ATPaseSerotonylationSino-atrial node

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Area of Science:

  • Cardiology
  • Molecular Biology
  • Physiology

Background:

  • Sino-atrial node (SAN) automaticity is crucial for heart rate but not fully understood.
  • Protein serotonylation, mediated by intracellular 5-HT, plays various physiological roles.
  • The specific role of protein serotonylation in SAN automaticity remains largely unexplored.

Purpose of the Study:

  • To investigate the functional role of protein serotonylation in controlling SAN automaticity.
  • To identify specific proteins in cardiomyocytes that undergo serotonylation.
  • To explore the impact of identified protein modifications on cardiac function.

Main Methods:

  • Screening of cardiomyocyte proteins to identify potential targets of serotonylation.
  • Utilizing mathematical modeling of SAN cell behavior.
  • Simulating the effects of altered protein function on cellular electrophysiology.

Main Results:

  • Sarco(endo)plasmic reticulum Ca ATPase type 2a (SERCA2a) was identified as a protein that can be serotonylated in cardiomyocytes.
  • Mathematical simulations demonstrated that changes in the Ca2+ affinity of the SERCA2a pump can lead to significant alterations in heart rate.
  • Variations in SERCA2a Ca2+ affinity resulted in simulated tachycardia or bradycardia.

Conclusions:

  • Protein serotonylation of SERCA2a is a newly identified mechanism potentially regulating SAN automaticity.
  • The modulation of SERCA2a's calcium-binding properties through serotonylation can influence heart rate.
  • This finding opens new avenues for understanding cardiac rhythm regulation and potential therapeutic targets.