Mus musculus
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ABSTRACT:
PROVIDER: PRJNA152089 | ENA |
REPOSITORIES: ENA
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Project description:To elucidate the genome-wide role of Ca2+/ calmodulin inhibition of E2A in regulation of BCR activation, we performed DNA microarray analysis of activated splenic B cells expressing wildtype or CaM-resistant E12 mutant m8N47 with and without anti-IgM treatment for 3 hour.The expression of a remarkably large set of genes differed significantly.
2012-07-11 | GSE35747 | GEO
Project description:To elucidate the genome-wide role of Ca2+/ calmodulin inhibition of E2A in regulation of BCR activation, we performed DNA microarray analysis of activated splenic B cells expressing wildtype or CaM-resistant E12 mutant m8N47 with and without anti-IgM treatment for 3 hour.The expression of a remarkably large set of genes differed significantly. Primary splenic B-lymphocytes were purified from mice heterozygous for the deletion of E2A gene and infected with retroviruses expressing either wildtype or mutant E12 after activation with CD40L plus IL-4 for 14 h. After 12 h incubation, the infection was repeated for 12 h, followed by incubation for a further 22 h post-infection in fresh complete medium with the stimulants to allow expression of GFP and E12. In addition to CD40L plus IL-4, the medium was supplemented with LPS (200 ng/ml) during retroviral infection incubations to improve infection efficiency. To study gene expression following B-cell receptor activation, anti-mouse IgM (2.5 M-NM-<g/ml) was added for 3 hour. For DNA microarray analysis of infected B-lymphocytes, the infected cells were purified with a FACSAria cell sorter instrument (BD Biosciences) using their green fluorescence from expression of the GFP.
2012-07-10 | E-GEOD-35747 | biostudies-arrayexpress
Project description:Toxoplasma gondii is an apicomplexan parasite infecting human and animals, causing huge health concerns and economic losses. Calcium ion, a critical second messenger in cells, can regulate related vital activities, particularly in parasite invasion and escape processes. Calmodulin (CaM) is a short, highly conserved Ca2+ binding protein found in all eukaryotic cells, including apicomplexan parasites. After binding to Ca2+, CaM can be activated to interact with a variety of proteins (such as enzymes). Since direct destruction of CaM is impossible, few studies have been conducted on the function of CaM in T. gondii. We generated the CaM indirect knockout strain (iCaM) using a tetracycline-off system with CaM promoter sequence in T. gondii TATI strain, and compared the transcriptomes of tachyzoites with and without Calmodulin.
2022-04-14 | GSE198001 | GEO
Project description:Heterozygosity for missense mutations in one of 3 seemingly redundant calmodulin (CaM)-encoding genes can cause life-threatening ventricular arrhythmias, suggesting that small fractions of mutant CaM protein suffice to cause a severe phenotype. However, the exact molar ratios of wildtype to mutant CaM protein in calmodulinopathy hearts remain unknown. The aim of the present study was to directly quantitate mutant versus wildtype CaM transcript and protein levels in hearts of knock-in mice harboring the p.N98S mutation in the Calm1 gene. We found that the transcripts from the mutant Calm1 allele were the least abundantly expressed Calm transcripts in both hetero- and homozygous mutant hearts, while mutant hearts accumulate high levels of N98S-CaM protein in a Calm1N98S allele dosage-dependent manner, exceeding those of wildtype CaM protein. We further show that the severity of the electrophysiological phenotype incrementally increases with the graded increase in the mutant-to-wildtype CaM protein expression ratio seen in homozygous versus heterozygous mutant mice. We finally show a decrease in N98S-CaM protein degradation, suggesting that mutant CaM stabilization contributed to its enrichment in the heart. Our results support a novel mechanism by which a mutation in a single Calm gene can give rise to a severe phenotype.
2025-07-16 | GSE301709 | GEO
Project description:Toxoplasma gondii is an apicomplexan parasite infecting human and animals, causing huge health concerns and economic losses. Calcium ion, a critical second messenger in cells, can regulate related vital activities, particularly in parasite invasion and escape processes. Calmodulin (CaM) is a short, highly conserved Ca2+ binding protein found in all eukaryotic cells, including apicomplexan parasites. After binding to Ca2+, CaM can be activated to interact with a variety of proteins (such as enzymes). Nevertheless, CaM-interacting proteins have not been identified in T. gondii. We report here the use of T. gondii strain RH△hxgprt expressing the proximity-labeling enzyme BirA* fused to CaM, in combination with LC-MS/MS to specifically identify CaM-interacting proteins. Our study revealed over three hundred of CaM’s proximal interacting proteins in T. gondii. These CaM partners were broadly dispersed throughout the parasite. The majority of their CRISPR fitness scores were below zero, indicating CaM's essential functions in parasites.
2022-09-25 | PXD032102 | Pride
Project description:Calmodulinopathies are rare inherited arrhythmia syndromes caused by dominant gain of function variants in one of three genes, CALM1, CALM2, and CALM3, which each encode the identical calmodulin (CaM) protein. We hypothesized that antisense oligonucleotide (ASO)-mediated depletion of an affected calmodulin gene would ameliorate disease manifestations, while the other two calmodulin genes would preserve CaM level and function. Here we tested this hypothesis using human induced pluripotent stem cell-derived cardiomyocyte (iPSC-CM) and mouse models of CALM1 pathogenic variants. Human CALM1F142L/+ iPSC-CMs exhibited prolonged action potentials, modeling congenital long QT syndrome. CALM1-depleting ASOs did not alter CaM protein level and normalized repolarization of CALM1F142L/+ iPSC-CMs. Similarly, an ASO targeting murine Calm1 depleted Calm1 transcript without affecting CaM protein level. This ASO alleviated drug-induced arrhythmia in CalmN98S/+ mice without causing observable toxicity. These results provide proof-of-concept that ASOs targeting individual calmodulin genes are potentially effective and safe therapies for calmodulinopathies.
2024-06-13 | GSE245945 | GEO
Project description:We have employed whole genome microarray expression profiling to identify genes conferring induction of pistillody, homeotic transformation of stamens into pistil-like structures. As a result, we identified five genes which show higher expression levels in pistillody line compared with normal line. Quantitative expression analysis using real-time PCR indicated that among five genes a calmodulin (CaM)-binding protein gene, WCBP1 (wheat calmodulin-binding protein 1), is obviously up-regulated in the young spikes of the pistillody line. The full-length cDNA sequence for WCBP1 showed it is a member of the ACBP60 family CaM-binding protein.
2012-12-31 | GSE37486 | GEO
Project description:Whole genome transcription profile of antigen receptor activated B cells
| PRJNA115731 | ENA
Project description:We have employed whole genome microarray expression profiling to identify genes conferring induction of pistillody, homeotic transformation of stamens into pistil-like structures. As a result, we identified five genes which show higher expression levels in pistillody line compared with normal line. Quantitative expression analysis using real-time PCR indicated that among five genes a calmodulin (CaM)-binding protein gene, WCBP1 (wheat calmodulin-binding protein 1), is obviously up-regulated in the young spikes of the pistillody line. The full-length cDNA sequence for WCBP1 showed it is a member of the ACBP60 family CaM-binding protein. Expression patterns were compared between the pistillody line and normal line. Total RNA samples were isolated from young spikes (3-10mm in length) at floret differentiation stage. Two independent experiments were conducted in each experiments.
2012-12-31 | E-GEOD-37486 | biostudies-arrayexpress
Project description:Purpose: Cardiac hypertrophy is a well-known major risk factor for poor prognosis in patients with cardiovascular diseases. Dysregulation of intracellular Ca2+ is involved in the pathogenesis of cardiac hypertrophy. However, the precise mechanism underlying cardiac hypertrophy remains elusive. Here, we investigated whether pressure-overload induced hypertrophy can be induced by destabilization of cardiac ryanodine receptor (RyR2) through calmodulin (CaM) dissociation and subsequent Ca2+ leakage, and whether it can be genetically rescued by enhancing the binding affinity of CaM to RyR2. Methods: To examine the role of CaM-RyR2 complex in the development of pressure-overload induced cardiac hypertrophy, whole transcriptome analysis using RNA-seq analysis in the hearts from WT and homozygous RyR2V3599K/V3599K (V3599K) mice with or without transverse aortic constriction (TAC) was performed to elucidate the RyR2 signaling pathway in the heart. Results: Gene expression increased in WT (+TAC) hearts compared to WT (-TAC) hearts; however, this increase was not observed in V3599K (+TAC) hearts. Conclusions: Enhanced CaM binding to RyR2 decreased expression of hypertrophy-related genes.
2020-10-07 | GSE158536 | GEO