The ASIC1 Channel: A Potential Drug Target and Biomarker for Acid-Sensitive Tissue

Target Name: ASIC1

NCBI ID: G41

ASIC1

The ASIC1 Channel: A Potential Drug Target and Biomarker for Acid-Sensitive Tissue

Abstract:

Acid sensing ion channel subunit 1 (ASIC1) is a transmembrane protein that plays a crucial role in the regulation of intracellular acidification. As a drug target and biomarker, ASIC1 has been extensively studied, and its functions in various physiological processes have been well-described . This article aims to provide a comprehensive overview of ASIC1, including its structure, function, and potential as a drug target and biomarker.

Introduction:

Acid sensing ion channels (ASICs) are a family of transmembrane proteins that play a central role in the regulation of intracellular acidification. These channels are involved in the transfer of protonation states across the membrane, and their activity is closely linked to the regulation of various physiological processes, including cell signaling, neurotransmission, and chromatin remodeling.

ASICs are characterized by the presence of an ion channel pore, which allows for the passage of ions and protons across the membrane. The pore is typically selective for certain types of ions, and the channel can be either cationic or anionic in its orientation. ASICs are found in various cell types, including neurons, cardiac cells, and epithelial cells, and they play a critical role in maintaining the proper functioning of these cells.

One of the well-studied ASICs is ASIC1, which is a transmembrane protein that is expressed in various tissues and cells. ASIC1 is involved in the regulation of intracellular acidification and has been extensively studied for its functions in various physiological processes.

Structure and Function:

ASIC1 is a type-I transmembrane protein that consists of a catalytic alpha-helices and a transmembrane region. The catalytic alpha-helices are responsible for the regulation of intracellular acidification and are the sites of ASIC1's ion channels. These channels are typically cationic in orientation and are involved in the transfer of H+ ions across the membrane.

ASIC1 is involved in the regulation of a variety of physiological processes, including cell signaling, neurotransmission, and chromatin remodeling. For example, ASIC1 has been shown to be involved in the regulation of neurotransmitter release from axon terminal boutons and to play a role in the regulation of synaptic strength.

ASIC1 has also been shown to be involved in the regulation of ion channels in various tissues, including cardiac and skeletal muscles. For example, studies have shown that ASIC1 is involved in the regulation of Na+ and K+ channels in cardiac myocytes and that it plays a role in the regulation of muscle contractions.

ASIC1 has also been shown to be involved in the regulation of pH homeostasis in various physiological processes, including cell signaling and neurotransmission. For example, studies have shown that ASIC1 is involved in the regulation of acidification in the endoplasmic reticulum and that it plays a role in the regulation of neurotransmitter release from axon terminal boutons.

Drug Targeting and Biomarker Potential:

ASIC1 has been identified as a potential drug target due to its involvement in various physiological processes and its role in the regulation of intracellular acidification. Several studies have shown that inhibiting ASIC1 activity can have beneficial effects on various physiological processes, including neurotransmission and cancer progression.

ASIC1 has also been shown to be involved in the regulation of ion channels in various tissues, including cardiac and skeletal muscles. Therefore, ASIC1 has potential as a biomarker for

Protein Name: Acid Sensing Ion Channel Subunit 1

Functions: Isoform 2 and isoform 3 function as proton-gated sodium channels; they are activated by a drop of the extracellular pH and then become rapidly desensitized. The channel generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Isoform 2 can also transport potassium, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 can also transport calcium ions. Mediates glutamate-independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca(2+) concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear

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