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Calcium channel, voltage-dependent, L type, alpha 1S subunit

dihydropyridine receptor, CACNA1S, CACNL1A3, MHS-5
This gene encodes one of the five subunits of the slowly inactivating L-type voltage-dependent calcium channel in skeletal muscle cells. Mutations in this gene have been associated with hypokalemic periodic paralysis, thyrotoxic periodic paralysis and malignant hyperthermia susceptibility. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: dihydropteridine reductase, HAD, CAN, ACID, ATPase
Papers on dihydropyridine receptor
Membrane depolarization increases ryanodine sensitivity to Ca2+ release to the cytosol in L6 skeletal muscle cells: Implications for excitation-contraction coupling.
Ochs et al., United States. In Exp Biol Med (maywood), Jan 2016
UNASSIGNED: The dihydropyridine receptor in the plasma membrane and the ryanodine receptor in the sarcoplasmic reticulum are known to physically interact in the process of excitation-contraction coupling.
The R900S mutation in CACNA1S associated with hypokalemic periodic paralysis.
Qi et al., Hangzhou, China. In Neuromuscul Disord, Dec 2015
We used whole-exome next-generation sequencing to identify a mutation in the calcium channel, voltage-dependent, L type, alpha subunit gene (CACNA1S), R900S, which is a rare mutation associated with hypokalemic periodic paralysis.
Effect of sophoridine on Ca(2+) induced Ca(2+) release during heart failure.
Yang et al., Yinchuan, China. In Physiol Res, Dec 2015
We investigated the Ca(2+) induced Ca(2+) transients and assessed the expression of ryanodine receptor (RyR2) and L-type Ca(2+) channel (dihydropyridine receptor, DHPR).
Mutation analysis of CACNA1S and SCN4A in patients with hypokalemic periodic paralysis.
Yao et al., Beijing, China. In Mol Med Report, Oct 2015
Mutations in CACNA1S (calcium channel, voltage‑dependent, L type, alpha 1S subunit) and SCN4A (sodium channel, voltage‑gated, type IV, alpha subunit) are associated with hypokalemic periodic paralysis (HPP).
Novel pathogenic variants and genes for myopathies identified by whole exome sequencing.
Baumbach-Reardon et al., Vancouver, Canada. In Mol Genet Genomic Med, Jul 2015
Finally, we classify two cases as calcium channelopathies with identification of novel pathogenic variants in RYR1 and CACNA1S.
Mutations of SCN4A gene cause different diseases: 2 case reports and literature review.
Cao et al., Shanghai, China. In Channels (austin), 2014
Genomic DNA was extracted from peripheral blood leukocytes, followed by polymerase chain reaction and DNA sequencing of candidate genes, including SCN4A and CACNA1S.
Malignant hyperthermia: a review.
Stowell et al., Livingston, United States. In Orphanet J Rare Dis, 2014
Less than 1 % of variants have been found in CACNA1S but not all of these are causal.
Skeletal muscle excitation-contraction coupling: who are the dancing partners?
Dulhunty et al., Canberra, Australia. In Int J Biochem Cell Biol, 2014
There is an overwhelming body of work supporting the idea that excitation-contraction coupling in skeletal muscle depends on a physical interaction between the skeletal muscle isoform of the dihydropyridine receptor L-type Ca(2+) channel and the skeletal isoform of the ryanodine receptor Ca(2+) release channel.
DNA testing for malignant hyperthermia: the reality and the dream.
Stowell, Palmerston North, New Zealand. In Anesth Analg, 2014
In 1994, a single point mutation in the α 1 subunit of the dihydropyridine receptor gene (CACNA1S) was identified and also subsequently shown to be causative of MH.
Genotype and phenotype analysis of patients with sporadic periodic paralysis.
Lin et al., Taipei, Taiwan. In Am J Med Sci, 2012
All familial periodic paralysis patients studied have mutations in either CACNA1S or SCN4A, but only 4 sporadic periodic paralysis patients have de novo mutations in CACNA1S (R1239H) and SCN4A (R669x2, R1135H).
Muscle weakness in myotonic dystrophy associated with misregulated splicing and altered gating of Ca(V)1.1 calcium channel.
Thornton et al., Rochester, United States. In Hum Mol Genet, 2012
Misregulated splicing and altered gating of Ca(V)1.1 calcium channel is associated with muscle weakness in myotonic dystrophy.
A novel mutation in CACNA1S gene associated with hypokalemic periodic paralysis which has a gender difference in the penetrance.
Liu et al., Harbin, China. In J Mol Neurosci, 2012
Affected members of a 5-generation Chinese family with hypokalemic periodic paralysis patients had a novel His916Gln mutation in all male HypoPP patients of the family. Penetrance of the mutation was complete in male carriers, but not female carriers.
Novel insights into the pathomechanisms of skeletal muscle channelopathies.
Hanna et al., London, United Kingdom. In Curr Neurol Neurosci Rep, 2012
Recent detailed characterizations of human genetic mutations in voltage-gated muscle sodium (gene: SCN4A), chloride (gene: CLCN1), calcium (gene: CACNA1S), and inward rectifier potassium (genes: KCNJ2, KCNJ18) channels have resulted in new insights into disease mechanisms, clinical phenotypic variation, and therapeutic options.
A novel mutation in the calcium channel gene in a family with hypokalemic periodic paralysis.
Takahashi et al., Sakai, Japan. In J Neurol Sci, 2011
A novel mutation in the CACNA1S gene--p.Arg900Gly--is found in a patient with hypokalemic periodic paralysis; this mutation is subsequently found to affect some of the patient's other family members.
[The relationships between the single nueleotide polymorphisms of CACNA1S gene 11 exon and thyrotoxic hypokalemic periodic paralysis in the people of Han Nationality in Sichuan Province, China].
Tian et al., Chengdu, China. In Sheng Wu Yi Xue Gong Cheng Xue Za Zhi, 2011
Three SNPs of CACNA1S gene exon 11 were found but could not be associated with thyrotoxic hypokalemic periodic paralysis in people of Han Nationality in Sichuan.
Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor.
Allen et al., Kyoto, Japan. In Nature, 1996
The skeletal isoform of the ryanodine receptor (RyR-1) functions as the Ca2+-release channel and the dihydropyridine receptor (DHPR) functions as the voltage sensor and also as an L-type Ca2+ channel.
Mapping of the hypokalaemic periodic paralysis (HypoPP) locus to chromosome 1q31-32 in three European families.
Weissenbach et al., Paris, France. In Nat Genet, 1994
Using an intragenic microsatellite, we also demonstrate that the gene encoding the muscle DHP-sensitive calcium channel alpha 1 subunit (CACNL1A3) maps to the same region, sharing a 5 centiMorgan (cM) interval with the HypoPP locus.
Restoration of normal function in genetically defective myotubes by spontaneous fusion with fibroblasts.
Beam et al., Fort Collins, United States. In Nature, 1989
The deficiency results from mutation of the gene for the skeletal muscle dihydropyridine receptor, an essential sarcolemmal component both of excitation-contraction coupling and of the slow calcium-ion channel.
Restoration of excitation-contraction coupling and slow calcium current in dysgenic muscle by dihydropyridine receptor complementary DNA.
Numa et al., Kyoto, Japan. In Nature, 1988
This suggests that the dihydropyridine receptor in the transverse tubule membrane of skeletal muscle functions both as the voltage sensor for excitation-contraction coupling and as the slow calcium channel.
Primary structure of the receptor for calcium channel blockers from skeletal muscle.
Numa et al., In Nature, 1987
Structural and sequence similarities to the voltage-dependent sodium channel suggest that in the transverse tubule membrane of skeletal muscle the dihydropyridine receptor may act both as voltage sensor in excitation-contraction coupling and as a calcium channel.
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