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» Authors » David H MacLennan

David H MacLennan

Explore the profile of David H MacLennan including associated specialties, affiliations and a list of published articles. Areas
Snapshot
Articles 57
Citations 2632
Followers 0
Related Specialties
Science
Biochemistry
Cell Biology
Top 10 Co-Authors
Anthony O Gramolini
Michio Asahi
Thomas Kislinger
Elena Zvaritch
Andrew Emili
Parveen Sharma
Evangelia G Kranias
Peter H Backx
Alexander Kraev
Mitsuhiko Ikura
Published In
Proc Natl Acad Sci U S A
J Biol Chem
Anesthesiology
Biochem J
Mol Cell Proteomics
Affiliations
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Recent Articles
1.
Reduced threshold for store overload-induced Ca release is a common defect of RyR1 mutations associated with malignant hyperthermia and central core disease
Chen W, Koop A, Liu Y, Guo W, Wei J, Wang R, et al.
Biochem J . 2017 Jul; 474(16):2749-2761. PMID: 28687594
Mutations in the skeletal muscle ryanodine receptor (RyR1) cause malignant hyperthermia (MH) and central core disease (CCD), whereas mutations in the cardiac ryanodine receptor (RyR2) lead to catecholaminergic polymorphic ventricular...
2.
Metformin increases degradation of phospholamban via autophagy in cardiomyocytes
Teng A, Miyake T, Yokoe S, Zhang L, Rezende Jr L, Sharma P, et al.
Proc Natl Acad Sci U S A . 2015 Jun; 112(23):7165-70. PMID: 26040000
Phospholamban (PLN) is an effective inhibitor of the sarco(endo)plasmic reticulum Ca(2+) ATPase (SERCA). Here, we examined PLN stability and degradation in primary cultured mouse neonatal cardiomyocytes (CMNCs) and mouse hearts...
3.
Muscle spindles exhibit core lesions and extensive degeneration of intrafusal fibers in the Ryr1(I4895T/wt) mouse model of core myopathy
Zvaritch E, MacLennan D
Biochem Biophys Res Commun . 2015 Jan; 460(1):34-9. PMID: 25619131
Muscle spindles from the hind limb muscles of adult Ryr1(I4895T/wt) (IT/+) mice exhibit severe structural abnormalities. Up to 85% of the spindles are separated from skeletal muscle fascicles by a...
4.
Exome analysis identifies Brody myopathy in a family diagnosed with malignant hyperthermia susceptibility
Sambuughin N, Zvaritch E, Kraeva N, Sizova O, Sivak E, Dickson K, et al.
Mol Genet Genomic Med . 2015 Jan; 2(6):472-83. PMID: 25614869
Whole exome sequencing (WES) was used to determine the primary cause of muscle disorder in a family diagnosed with a mild, undetermined myopathy and malignant hyperthermia (MH) susceptibility (MHS). WES...
5.
Type 2 ryanodine receptor domain A contains a unique and dynamic α-helix that transitions to a β-strand in a mutant linked with a heritable cardiomyopathy
Amador F, Kimlicka L, Stathopulos P, Gasmi-Seabrook G, MacLennan D, Van Petegem F, et al.
J Mol Biol . 2013 Aug; 425(21):4034-46. PMID: 23978697
Ryanodine receptors (RyRs) are large tetrameric calcium (Ca(2+)) release channels found on the sarcoplasmic reticulum that respond to dihydropyridine receptor activity through a direct conformational interaction and/or indirect Ca(2+) sensitivity,...
6.
CASQ1 gene is an unlikely candidate for malignant hyperthermia susceptibility in the North American population
Kraeva N, Zvaritch E, Frodis W, Sizova O, Kraev A, MacLennan D, et al.
Anesthesiology . 2013 Mar; 118(2):344-9. PMID: 23460944
Background: Malignant hyperthermia (MH, MIM# 145600) is a complex pharmacogenetic disorder that is manifested in predisposed individuals as a potentially lethal reaction to volatile anesthetics and depolarizing muscle relaxants. Studies...
7.
Novel excitation-contraction uncoupled RYR1 mutations in patients with central core disease
Kraeva N, Zvaritch E, Rossi A, Goonasekera S, Zaid H, Frodis W, et al.
Neuromuscul Disord . 2012 Nov; 23(2):120-32. PMID: 23183335
Central core disease, one of the most common congenital myopathies in humans, has been linked to mutations in the RYR1 gene encoding the Ca(2+) release channel of the sarcoplasmic reticulum...
8.
Structural determination of the phosphorylation domain of the ryanodine receptor
Sharma P, Ishiyama N, Nair U, Li W, Dong A, Miyake T, et al.
FEBS J . 2012 Aug; 279(20):3952-64. PMID: 22913516
The ryanodine receptor (RyR) is a large, homotetrameric sarcoplasmic reticulum membrane protein that is essential for Ca(2+) cycling in both skeletal and cardiac muscle. Genetic mutations in RyR1 are associated...
9.
Type 1 ryanodine receptor knock-in mutation causing central core disease of skeletal muscle also displays a neuronal phenotype
De Crescenzo V, Fogarty K, Lefkowitz J, Bellve K, Zvaritch E, MacLennan D, et al.
Proc Natl Acad Sci U S A . 2011 Dec; 109(2):610-5. PMID: 22203976
The type 1 ryanodine receptor (RyR1) is expressed widely in the brain, with high levels in the cerebellum, hippocampus, and hypothalamus. We have shown that L-type Ca(2+) channels in terminals...
10.
Enhanced Ca2+ transport and muscle relaxation in skeletal muscle from sarcolipin-null mice
Tupling A, Bombardier E, Gupta S, Hussain D, Vigna C, Bloemberg D, et al.
Am J Physiol Cell Physiol . 2011 Jun; 301(4):C841-9. PMID: 21697544
Sarcolipin (SLN) inhibits sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) pumps. To evaluate the physiological significance of SLN in skeletal muscle, we compared muscle contractility and SERCA activity between Sln-null and wild-type mice....