Transient receptor potential channel 1 (TRPC1), encoded by the gene TRPC1, is a membrane protein that can compose a non-specific ion channel permeable to calcium and many other cations. TRPC1 is considered to be induced to form channels by depletion of intracellular calcium stores and also by a receptor tyrosine kinase-activated phosphatidylinositol second messenger system. Two transcript variants produced by alternative splicing informs have been reported for TRPC1 gene.
|Basic Information of TRPC1|
|Protein Name||Short transient receptor potential channel 1|
|Aliases||Transient receptor protein 1|
|Organism||Homo sapiens (Human)|
As an ion channel, TRPC1 is located on the plasma membrane of numerous animal and human cell types, where it acts as a non-selective cation channel to transport both calcium and sodium ions. TRPC1 is able to form tetrameric complexes with TRPC4 and/or TRPC5 isoforms, which have recently been involved in the efficiency of synaptic transmission in the hippocampus. TRPC1 is considered to regulate calcium entry in response to the activation of receptors coupled to the phospholipase C system or depletion of endoplasmic calcium stores. TRPC1 has a broad expression in the brain of mammals and has a similar corticolimbic expression pattern as TRPC4 and TRPC5. As one important member of TRPC channels, TRPC1 is shown to have diverse functions in the brain, including the control of neurite outgrowth and axon guidance, regulation of neural progenitor cells proliferation and differentiation, regulation of neuronal apoptosis or survival, modulation of neuronal excitability and excitotoxicity.
Fig.1 Steps in TRPC1 channel activation. (B Pani,2012)
This article shows that TRPC1 may be a target of PPARγ, suggesting that TRPC1 is involved in a mechanism that translates environmental or metabolic stimuli into output in the form of brown adipose tissue activity.
This article suggests that TRPC1/Orai1 may comprise a compound that regulates Ca²⁺ influx and nitric oxide production via store-operated calcium channels and receptor-operated calcium channels activation.
This article confirms that the transmembrane region of TRPC1 can bind to amyloid-β protein precursor and thus decrease amyloid-β(Aβ) production, indicating that the loss of TRPC1 may exacerbate Aβ-induced cell apoptosis and memory deficit, though it does not induce cell death or impair cognitive function in physiological conditions.
This report demonstrates right ventricular specific cellular Ca²⁺ cycling remodeling in pulmonary hypertension rats with maladaptive right ventricular hypertrophy and that the STIM1L/Orai1/TRPC1/C4-dependent Ca²⁺ current participates in this Ca²⁺ remodeling in right ventricular hypertrophy secondary to pulmonary hypertension.
This article concludes that deletion of TRPC1 may lead to striatal neuronal apoptosis by interfering many biological processes, suggesting that TRPC1 may play a special role in the mediation of striatal cellular survival and death.
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