WordNet

the 3rd letter of the Roman alphabet (同)c
(music) the keynote of the scale of C major
a general-purpose programing language closely associated with the UNIX operating system
an object shaped like an equilateral triangle
a low triangular area of alluvial deposits where a river divides before entering a larger body of water; "the Mississippi River delta"; "the Nile delta"
the 4th letter of the Greek alphabet

PrepTutorEJDIC

carbonの化学記号
デルタ(ギリシア語アルファベットの第4字Δ,δ;英語D,dに相当) / (河口の)三角州,デルタ / 三角形をしたもの
cesiumの化学記号
cadmiumの化学記号

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1. 寒冷蕁麻疹 cold urticaria
2. 爪疾患の概要 overview of nail disorders
3. 血小板生物学 platelet biology
4. ペプチドホルモンのシグナル伝達および調節 peptide hormone signal transduction and regulation
5. 先天性乳児ネフローゼ症候群 congenital and infantile nephrotic syndrome

English Journal

Ca2+-independent binding of anionic phospholipids by phospholipase C δ1 EF-hand domain.

Cai J1, Guo S, Lomasney JW, Roberts MF.Author information 1From the Department of Chemistry, Boston College, Chestnut Hill, Massachusetts 02467 and.AbstractRecombinant EF-hand domain of phospholipase C δ1 has a moderate affinity for anionic phospholipids in the absence of Ca(2+) that is driven by interactions of cationic and hydrophobic residues in the first EF-hand sequence. This region of PLC δ1 is missing in the crystal structure. The relative orientation of recombinant EF with respect to the bilayer, established with NMR methods, shows that the N-terminal helix of EF-1 is close to the membrane interface. Specific mutations of EF-1 residues in full-length PLC δ1 reduce enzyme activity but not because of disturbing partitioning of the protein onto vesicles. The reduction in enzymatic activity coupled with vesicle binding studies are consistent with a role for this domain in aiding substrate binding in the active site once the protein is transiently anchored at its target membrane.
The Journal of biological chemistry.J Biol Chem.2013 Dec 27;288(52):37277-88. doi: 10.1074/jbc.M113.512186. Epub 2013 Nov 14.
Recombinant EF-hand domain of phospholipase C δ1 has a moderate affinity for anionic phospholipids in the absence of Ca(2+) that is driven by interactions of cationic and hydrophobic residues in the first EF-hand sequence. This region of PLC δ1 is missing in the crystal structure. The relative ori
PMID 24235144

Genetic ablation of phospholipase C delta 1 increases survival in SOD1(G93A) mice.

Staats KA1, Van Helleputte L, Jones AR, Bento-Abreu A, Van Hoecke A, Shatunov A, Simpson CL, Lemmens R, Jaspers T, Fukami K, Nakamura Y, Brown RH Jr, Van Damme P, Liston A, Robberecht W, Al-Chalabi A, Van Den Bosch L.Author information 1Laboratory of Neurobiology, Belgium; Leuven Research Institute of Neuroscience and Disease (LIND), KU Leuven, Belgium; Vesalius Research Center, VIB, Belgium. Electronic address: kim.staats@vib-kuleuven.be.AbstractAmyotrophic Lateral Sclerosis (ALS) is a devastating progressive neurodegenerative disease, resulting in selective motor neuron degeneration and paralysis. Patients die approximately 3-5 years after diagnosis. Disease pathophysiology is multifactorial, including excitotoxicity, but is not yet fully understood. Genetic analysis has proven fruitful in the past to further understand genes modulating the disease and increase knowledge of disease mechanisms. Here, we revisit a previously performed microsatellite analysis in ALS and focus on another hit, PLCD1, encoding phospholipase C delta 1 (PLCδ1), to investigate its role in ALS. PLCδ1 may contribute to excitotoxicity as it increases inositol 1,4,5-trisphosphate (IP3) formation, which releases calcium from the endoplasmic reticulum through IP3 receptors. We find that expression of PLCδ1 is increased in ALS mouse spinal cord and in neurons from ALS mice. Furthermore, genetic ablation of this protein in ALS mice significantly increases survival, but does not affect astrogliosis, microgliosis, aggregation or the amount of motor neurons at end stage compared to ALS mice with PLCδ1. Interestingly, genetic ablation of PLCδ1 prevents nuclear shrinkage of motor neurons in ALS mice at end stage. These results indicate that PLCD1 contributes to ALS and that PLCδ1 may be a new target for future studies.
Neurobiology of disease.Neurobiol Dis.2013 Dec;60:11-7. doi: 10.1016/j.nbd.2013.08.006. Epub 2013 Aug 19.
Amyotrophic Lateral Sclerosis (ALS) is a devastating progressive neurodegenerative disease, resulting in selective motor neuron degeneration and paralysis. Patients die approximately 3-5 years after diagnosis. Disease pathophysiology is multifactorial, including excitotoxicity, but is not yet fully
PMID 23969236

PLC-δ1-Lf, a novel N-terminal extended phospholipase C-δ1.

Kim NY1, Ahn SJ, Kim MS, Seo JS, Kim BS, Bak HJ, Lee JY, Park MA, Park JH, Lee HH, Chung JK.Author information 1Department of Aquatic Life Medicine, Pukyong National University, Busan 608-737, South Korea.AbstractPhospholipase C-δ (PLC-δ), a key enzyme in phosphoinositide turnover, is involved in a variety of physiological functions. The widely expressed PLC-δ1 isoform is the best characterized and the most well understood phospholipase family member. However, the functional and molecular mechanisms of PLC-δ1 remain obscure. Here, we identified that the N-terminal region of mouse PLC-δ1 gene has two variants, a novel alternative splicing form, named as long form (mPLC-δ1-Lf) and the previously reported short form (mPLC-δ1-Sf), having exon 2 and exon 1, respectively, while both the gene variants share exons 3-16 for RNA transcription. Furthermore, the expression, identification and enzymatic characterization of the two types of PLC-δ1 genes were compared. Expression of mPLC-δ1-Lf was found to be tissue specific, whereas mPLC-δ1-Sf was widely distributed. The recombinant mPLC-δ1-Sf protein exhibited higher activity than recombinant mPLC-δ1-Lf protein. Although, the general catalytic and regulatory properties of mPLC-δ1-Lf are similar to those of PLC-δ1-Sf isozyme, the mPLC-δ1-Lf showed some distinct regulatory properties, such as tissue-specific expression and lipid binding specificity, particularly for phosphatidylserine.
Gene.Gene.2013 Oct 10;528(2):170-7. doi: 10.1016/j.gene.2013.07.022. Epub 2013 Jul 25.
Phospholipase C-δ (PLC-δ), a key enzyme in phosphoinositide turnover, is involved in a variety of physiological functions. The widely expressed PLC-δ1 isoform is the best characterized and the most well understood phospholipase family member. However, the functional and molecular mechanisms of PL
PMID 23892088