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Related Concept Videos

Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory organs,...
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
Antihypertensive Drugs: Action of Calcium Channel Blockers01:18

Antihypertensive Drugs: Action of Calcium Channel Blockers

Calcium ions are essential to contract smooth muscle cells in blood vessels. They enter these cells through voltage-dependent calcium channels, specifically L-type calcium channels in the cell membrane. These L-type calcium channels are integral to the excitation-contraction coupling process in smooth muscle. When a stimulus is received by smooth muscle cells, their membrane depolarizes. This alteration in membrane potential instigates the opening of L-type calcium channels. As a result,...
Antiarrhythmic Drugs: Class IV Agents as Calcium Channel Blockers01:20

Antiarrhythmic Drugs: Class IV Agents as Calcium Channel Blockers

Class IV antiarrhythmic drugs, such as verapamil and diltiazem, block calcium channels. They primarily affect the heart, slowing the conduction in calcium-dependent tissues like the SA and AV nodes. These drugs manage reentrant supraventricular tachycardia (SVT) and reduce ventricular rate in atrial flutter/fibrillation.
Verapamil, a calcium channel blocker, inhibits calcium movement across myocardial cell membranes and vascular smooth muscle. This results in the dilation of coronary and...
Antianginal Drugs: Calcium Channel Blockers and Ranolazine01:25

Antianginal Drugs: Calcium Channel Blockers and Ranolazine

Angina pectoris, a primary symptom of ischemic heart disease, requires careful pharmacological interventions. In this context, calcium channel blockers (CCBs) and ranolazine have emerged as crucial pharmacotherapeutic agents, providing deep insights into the complexities of angina management.
CCBs, a diverse class that includes dihydropyridines (nifedipine) and diphenylalkylamines (verapamil and diltiazem), exert their effect by blocking calcium channels in cardiac and smooth muscle cells. This...

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Related Experiment Video

Updated: Jun 10, 2026

Isolation and Characterization of Primary Rat Valve Interstitial Cells: A New Model to Study Aortic Valve Calcification
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CircZBTB44-Encoded Peptide ZBTB44-342aa Alleviates Aortic Valve Calcification Via cGAS-STING Inhibition.

Dongtu Hu1,2, Yingwen Lin1,2, Hailun Huang1,2

  • 1State Key Laboratory of Multi-Organ Injury Prevention and Treatment, National Clinical Research Center for Kidney and Urological Diseases, Department of Cardiology, Nanfang Hospital, Southern Medical University, 510515, Guangzhou, China (D.H., Y.L., H.H., G.X., J.L., L.H., M.X., X.L., L.W., S.S., X.D., G.Z., Q.Z.).

Circulation Research
|January 5, 2026
PubMed
Summary
This summary is machine-generated.

Circular RNAs like circZBTB44 encode peptides that inhibit calcific aortic valve disease (CAVD) progression. This peptide targets the cGAS-STING pathway, offering potential therapeutic strategies for CAVD.

Keywords:
RNA methylationRNA, circularaortic valve diseasecalcinosisinflammation

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Isolation of Mouse Interstitial Valve Cells to Study the Calcification of the Aortic Valve In Vitro
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Area of Science:

  • Molecular Biology
  • Cardiovascular Research
  • RNA Biology

Background:

  • Circular RNAs (circRNAs) are involved in various diseases, including calcific aortic valve disease (CAVD).
  • The specific roles of coding circRNAs in CAVD pathogenesis are not well understood.
  • This study investigates coding circRNAs in the context of CAVD.

Purpose of the Study:

  • To identify and characterize coding circRNAs in CAVD.
  • To explore the functional mechanisms of identified coding circRNAs in CAVD.
  • To assess the therapeutic potential of circRNAs in CAVD.

Main Methods:

  • Transcriptome sequencing to identify circRNAs.
  • Experimental validation of circRNA translation and function.
  • Cellular and animal models of CAVD.
  • Analysis of the cGAS-STING signaling pathway.

Main Results:

  • Identified circZBTB44, which translates to ZBTB44-342aa via N6-methyladenosine modification.
  • ZBTB44-342aa inhibits mitochondrial damage and suppresses the cGAS-STING pathway.
  • circZBTB44/ZBTB44-342aa alleviates CAVD progression in vitro and in vivo.
  • STING pathway modulation affects osteogenic differentiation in aortic valve cells.

Conclusions:

  • circZBTB44-encoded ZBTB44-342aa mitigates CAVD progression by inhibiting the cGAS-STING pathway.
  • circZBTB44 and STING are identified as potential therapeutic targets for CAVD.
  • This research elucidates a novel molecular mechanism in CAVD pathogenesis.