L-type calcium channel protein subunit alpha-1C (Cav1.2 (gene: CACNA1C))

L-type calcium channel protein subunit alpha-1C, commonly known as Cav1.2 and encoded by the *CACNA1C* gene, is the pore-forming subunit of the L-type voltage-dependent calcium channel complex[1][4][7]. It forms the structural and functional core of the channel, composed of four homologous domains with six transmembrane segments each, and is responsible for high-voltage activated, long-lasting calcium currents[1][5][7]. Cav1.2 is primarily expressed in cardiac and smooth muscle but also found in numerous other tissues, including neurons and pancreatic cells[1][4]. In cardiomyocytes, it enables the rapid influx of calcium during membrane depolarization, which triggers further calcium release from the sarcoplasmic reticulum via ryanodine receptors—an essential process for excitation-contraction coupling and normal heart rhythm[1][5][7]. Cav1.2 channels are pharmacologically targeted by a variety of clinically important drugs, including dihydropyridines, phenylalkylamines, and benzothiazepines, all of which modulate calcium entry and, thereby, cardiac and vascular function. Mutations in CACNA1C are associated with cardiac arrhythmias such as long QT syndrome and neurodevelopmental disorders such as Timothy syndrome[4]. The channel's function and properties are further modulated by a range of auxiliary subunits and regulatory proteins, and dysregulation can result in significant cardiovascular and neurological pathologies[1][7].

Other names

Cav1.2Voltage-dependent L-type calcium channel subunit alpha-1CCACNA1CDihydropyridine receptor (cardiac type)

Blockade or inhibition of calcium influx through channel antagonism (by dihydropyridines, phenylalkylamines, benzothiazepines) Modulation of channel function by altering inactivation kinetics or voltage dependence Indirect inhibition/modulation through auxiliary subunits (gabapentinoids)