scholarly journals Transcriptome analysis identified long non-coding RNAs involved in the adaption of yak to high-altitude environments

2020 ◽  
Vol 7 (9) ◽  
pp. 200625
Author(s):  
Jin-Wei Xin ◽  
Zhi-Xin Chai ◽  
Cheng-Fu Zhang ◽  
Yu-Mei Yang ◽  
Qiang Zhang ◽  
...  
Keyword(s):  
Muscle Contraction ◽  
High Altitude ◽  
Target Genes ◽  
Calcium Release ◽  
Phosphoglycerate Mutase ◽  
Acid Oxidation ◽  
Transcriptional Level ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Kegg Pathways

The mechanisms underlying yak adaptation to high-altitude environments have been investigated using various methods, but no report has focused on long non-coding RNA (lncRNA). In the present study, lncRNAs were screened from the gluteus transcriptomes of yak and their transcriptional levels were compared with those in Sanjiang cattle, Holstein cattle and Tibetan cattle. The potential target genes of the differentially expressed lncRNAs between species/strains were predicted using cis and trans models. Based on cis -regulated target genes, no KEGG pathway was significantly enriched. Based on trans -regulated target genes, 11 KEGG pathways in relation to energy metabolism and three KEGG pathways associated with muscle contraction were significantly enriched. Compared with cattle strains, transcriptional levels of acyl-CoA dehydrogenase, acyl-CoA-binding protein, 3-hydroxyacyl-CoA dehydrogenase were relatively higher and those of glyceraldehyde 3-phosphate dehydrogenase, phosphoglycerate mutase 1, pyruvate kinase and lactate/malate dehydrogenase were relatively lower in yak, suggesting that yaks activated fatty acid oxidation but inhibited glucose oxidation and glycolysis. Besides, NADH dehydrogenase and ATP synthase showed lower transcriptional levels in yak than in cattle, which might protect muscle tissues from deterioration caused by reactive oxygen species (ROS). Compared with cattle strains, the higher transcriptional level of glyoxalase in yak might contribute to dicarbonyl stress resistance. Voltage-dependent calcium channel/calcium release channel showed a lower level in yak than in cattle strains, which could reduce the Ca 2+ influx and subsequently decrease the risk of hypertension. However, levels of EF-hand and myosin were higher in yak than in cattle strains, which might enhance the negative effects of reduced Ca 2+ on muscle contraction. Overall, the present study identified lncRNAs and proposed their potential regulatory functions in yak.

scholarly journals TET1-DNA Hydroxymethylation Mediated Oligodendrocyte Homeostasis is Required for CNS Myelination and Remyelination

2019 ◽  
Author(s):  
Ming Zhang ◽  
Jian Wang ◽  
Kaixiang Zhang ◽  
Guozhen Lu ◽  
Keke Ren ◽  
...  
Keyword(s):  
Target Genes ◽  
Calcium Release ◽  
System Development ◽  
Nervous System Development ◽  
Oligodendrocyte Differentiation ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Dna Hydroxymethylation ◽  
Adult Mice ◽  
A Genome

AbstractTen-eleven translocation (TET) proteins, encoding dioxygenase for DNA hydroxymethylation, are important players in nervous system development and diseases. However, their role in oligodendrocyte homeostasis, myelination and remyelination remains elusive. Here, we detected a genome-wide and locus-specific DNA hydroxymethylation landscape shift during oligodendrocyte-progenitor (OPC) differentiation. Ablation of Tet1, but not Tet3, results in stage-dependent defects in oligodendrocyte development and myelination in the brain. The mice lacking Tet1 in the oligodendrocyte lineage develop schizophrenia-like behaviors. We further show that TET1 is also required for proper remyelination after demyelination injury in the adult mice. Transcriptomic and DNA hydroxymethylation profiling revealed a critical TET1-regulated epigenetic program for oligodendrocyte differentiation and identified a set of TET1-5hmC target genes associated with myelination, cell division, and calcium transport. Tet1-deficient OPCs exhibited reduced calcium activity in response to stimulus in culture. Moreover, deletion of a TET1-5hmC target gene, Itpr2, an oligodendrocyte-enriched intracellular calcium-release channel, significantly impaired the onset of oligodendrocyte differentiation. Together, our results suggest that stage-specific TET1-mediated epigenetic programming and oligodendrocyte homeostasis is required for proper myelination and repair.

scholarly journals David Herman Maclennan. 3 July 1937—24 June 2020

2021 ◽  
Author(s):  
Reinhart Reithmeier
Keyword(s):  
Muscle Contraction ◽  
Molecular Mechanisms ◽  
Calcium Release ◽  
New Technologies ◽  
Muscle Disease ◽  
Mitochondrial Atpase ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Isolation And Characterization ◽  
The University

David Herman MacLennan, one of Canada's foremost biomedical scientists, was known internationally for his research on the molecular mechanism of muscle contraction in human health and disease. David was born on 3 July 1937 in Swan River, Manitoba, and grew up in farm country. After obtaining a BS (Agriculture) in plant science from the University of Manitoba in 1959, David completed his MSc (1961) and PhD (1963) in biology at Purdue. A post-doctoral fellowship at the Enzyme Institute at the University of Wisconsin followed, where he was appointed as an assistant professor (1964–1968). At Wisconsin David published a series of elegant papers on the isolation and characterization of the mitochondrial ATPase and protein components of the electron transfer system. In 1969 he was recruited back to Canada as an associate professor in the Banting and Best Department of Medical Research at the University of Toronto, where he spent the rest of his illustrious career. Here, David shifted his focus to determine how calcium regulates muscle contraction, with a focus on the role of the sarcoplasmic reticulum (SR). David was a scientist who knew where a field was going and he often got there first, incorporating new technologies along the way. His early discovery of the Ca 2+ ATPase pump that controls calcium uptake into the SR was the key to muscle relaxation. His lab systematically characterized the components of the SR, including the ryanodine receptor which acts as a calcium release channel to allow muscle contraction. David's discoveries of these molecular mechanisms and their application to debilitating muscle disease are an inspiring scientific legacy. Although David published hundreds of papers, many cited hundreds of times, gave hundreds of invited seminars and won many prestigious awards, including Fellow of the Royal Society of London in 1994, his greatest legacy is the people he trained, many of whom went on to leadership positions in research and at universities around the world.

scholarly journals Unravelling calcium-release channel gating: clues from a hot disease

2004 ◽  
Vol 380 (1) ◽  
pp. e1-e3 ◽  
Author(s):  
Tommie V. McCARTHY ◽  
John J. MACKRILL
Keyword(s):  
Calcium Release ◽  
Distinct Point ◽  
Ryanodine Receptors ◽  
Point Mutations ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Present Evidence ◽  
Gating Mechanism ◽  
Biochemical Journal ◽  
Interdomain Interactions

Ryanodine receptors (RyRs) are a family of intracellular channels that mediate Ca2+ release from the endoplasmic and sarcoplasmic reticulum. More than 50 distinct point mutations in one member of this family, RyR1, cause malignant hyperthermia, a potentially lethal pharmacogenetic disorder of skeletal muscle. These mutations are not randomly distributed throughout the primary structure of RyR1, but are grouped in three discrete clusters. In this issue of the Biochemical Journal, Kobayashi et al. present evidence that interdomain interactions between two of these mutation-enriched regions play a key role in the gating mechanism of RyR1.

scholarly journals Protein Kinase A Phosphorylation of the Cardiac Calcium Release Channel (Ryanodine Receptor) in Normal and Failing Hearts

2002 ◽  
Vol 278 (1) ◽  
pp. 444-453 ◽  
Author(s):  
Steven Reiken ◽  
Marta Gaburjakova ◽  
Silvia Guatimosim ◽  
Ana M. Gomez ◽  
Jeanine D'Armiento ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Kinase A

scholarly journals Calcium channel ITPR2 and mitochondria–ER contacts promote cellular senescence and aging

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Dorian V. Ziegler ◽  
David Vindrieux ◽  
Delphine Goehrig ◽  
Sara Jaber ◽  
Guillaume Collin ◽  
...  
Keyword(s):  
Cellular Senescence ◽  
Calcium Release ◽  
Liver Steatosis ◽  
Metabolic Stress ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Age Related ◽  
Trisphosphate Receptor

AbstractCellular senescence is induced by stresses and results in a stable proliferation arrest accompanied by a pro-inflammatory secretome. Senescent cells accumulate during aging, promoting various age-related pathologies and limiting lifespan. The endoplasmic reticulum (ER) inositol 1,4,5-trisphosphate receptor, type 2 (ITPR2) calcium-release channel and calcium fluxes from the ER to the mitochondria are drivers of senescence in human cells. Here we show that Itpr2 knockout (KO) mice display improved aging such as increased lifespan, a better response to metabolic stress, less immunosenescence, as well as less liver steatosis and fibrosis. Cellular senescence, which is known to promote these alterations, is decreased in Itpr2 KO mice and Itpr2 KO embryo-derived cells. Interestingly, ablation of ITPR2 in vivo and in vitro decreases the number of contacts between the mitochondria and the ER and their forced contacts induce premature senescence. These findings shed light on the role of contacts and facilitated exchanges between the ER and the mitochondria through ITPR2 in regulating senescence and aging.

scholarly journals Electron Cryomicroscopy of IP3R1 Calcium Release Channel

2009 ◽  
Vol 96 (3) ◽  
pp. 96a ◽  
Author(s):  
Que T. Ngo ◽  
Joshua T. Maxwell ◽  
Gregory A. Mignery ◽  
Wah Chiu ◽  
Steven J. Ludtke ◽  
...  
Keyword(s):  
Calcium Release ◽  
Electron Cryomicroscopy ◽  
Calcium Release Channel ◽  
Release Channel

scholarly journals A minimal gating model for the cardiac calcium release channel

1996 ◽  
Vol 71 (6) ◽  
pp. 2996-3012 ◽  
Author(s):  
A. Zahradníková ◽  
I. Zahradník
Keyword(s):  
Calcium Release ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Gating Model
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