Voltage-gated calcium channel and calcium-binding protein (VGCC/CBP)

Voltage-gated calcium channels (VGCCs) are essential pore-forming transmembrane proteins that mediate the entry of calcium ions into cells upon membrane depolarization, triggering various intracellular processes. These channels are classified into high-voltage activated (L-, P/Q-, N-, and R-type) and low-voltage activated (T-type) groups, each with distinct physiological roles in muscle contraction, hormone secretion, and neurotransmission [1][2]. Calcium-binding proteins (CBPs), such as calmodulin, troponin C, and S100 proteins, function as intracellular calcium sensors or buffers that translate calcium fluctuations into biological responses [3]. Together, these proteins maintain calcium homeostasis and regulate signaling pathways critical for cellular function. Mutations or dysregulation in these proteins are implicated in a wide range of channelopathies and diseases, including hypertension, cardiac arrhythmias, epilepsy, and chronic pain [1][4]. Therapeutic agents targeting VGCCs, such as dihydropyridines and gabapentinoids, are widely used in clinical practice to manage cardiovascular and neurological conditions [4]. This target entry is considered incorrect for structured data purposes as it aggregates multiple distinct protein families and channel types into a single heterogeneous category [5]. Sources: [1] StatPearls, Physiology, Voltage-Gated Calcium Channels (2023). [2] UniProt Consortium, Voltage-dependent L-type calcium channel subunit alpha-1C (P16230). [3] PubMed, Calcium-binding proteins in health and disease, PMID: 30243712. [4] NIH, Calcium Channel Blockers (2023). [5] IUPHAR/BPS Guide to Pharmacology, Voltage-gated calcium channels.

Other names

Voltage-dependent calcium channelVGCCCalcium-binding proteinCBPL-type calcium channelT-type calcium channelN-type calcium channelP/Q-type calcium channelR-type calcium channelCalmodulin-like proteinS100 protein family

Inhibition of calcium ion influx through voltage-gated channels; modulation of calcium-dependent signaling pathways; stabilization of inactive channel conformations.