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provides coniferyl ferulate(CAS#:508-79-2) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
The α1 and β1a subunits of the skeletal muscle calcium channel, Cav1.1, as well as the Ca2+ release channel, ryanodine receptor (RyR1), are essential for excitation-contraction coupling. RyR1 channel activity is modulated by the β1a subunit and this effect can be mimicked by a peptide (β1a490-524) corresponding to the 35-residue C-terminal tail of the β1a subunit. Protein-protein interaction assays confirmed a high-affinity interaction between the C-terminal tail of the β1a and RyR1. Based on previous results using overlapping peptides tested on isolated RyR1, we hypothesized that a 19-amino-acid residue peptide (β1a490-508) is sufficient to reproduce activating effects of β1a490-524. Here we examined the effects of β1a490-508 on Ca2+ release and Ca2+ currents in adult skeletal muscle fibers subjected to voltage-clamp and on RyR1 channel activity after incorporating sarcoplasmic reticulum vesicles into lipid bilayers. β1a490-508 (25 nM) increased the peak Ca2+ release flux by 49% in muscle fibers. Considerably fewer activating effects were observed using 6.25, 100, and 400 nM of β1a490-508 in fibers. β1a490-508 also increased RyR1 channel activity in bilayers and Cav1.1 currents in fibers. A scrambled form of β1a490-508 peptide was used as negative control and produced negligible effects on Ca2+ release flux and RyR1 activity. Our results show that the β1a490-508 peptide contains molecular components sufficient to modulate excitation-contraction coupling in adult muscle fibers.
β1a490-508, a 19-Residue Peptide from C-Terminal Tail of Cav1.1 β1a Subunit, Potentiates Voltage-Dependent Calcium Release in Adult Skeletal Muscle Fibers
Erick O. Hernandez-Ochoa,† Rotimi O. Olojo,† Robyn T. Rebbeck,‡ Angela F. Dulhunty,‡ and Martin F. Schneider†∗
2014 Feb 4;
Ideally, CD8+ T-cell responses against virally infected or malignant cells are defined at the level of the specific peptide and restricting MHC class I element, a determination not yet made in the dog. To advance the discovery of canine CTL epitopes, we sought to determine whether a putative classical MHC class Ia gene, Dog Leukocyte Antigen (DLA)-88, presents peptides from a viral pathogen, canine distemper virus (CDV). To investigate this possibility, DLA-88*508:01, an allele prevalent in Golden Retrievers, was expressed as a FLAG-tagged construct in canine histiocytic cells to allow affinity purification of peptide-DLA-88 complexes and subsequent elution of bound peptides. Pattern analysis of self peptide sequences, which were determined by liquid chromatography-tandem mass spectrometry (LC-MS/MS), permitted binding preferences to be inferred. DLA-88*508:01 binds peptides that are 9-to-12 amino acids in length, with a modest preference for 9- and 11-mers. Hydrophobic residues are favored at positions 2 and 3, as are K, R or F residues at the C-terminus. Testing motif-matched and -unmatched synthetic peptides via peptide-MHC surface stabilization assay using a DLA-88*508:01-transfected, TAP-deficient RMA-S line supported these conclusions. With CDV infection, 22 viral peptides ranging from 9-to-12 residues in length were identified in DLA-88*508:01 eluates by LC-MS/MS. Combined motif analysis and surface stabilization assay data suggested that 11 of these 22 peptides, derived from CDV fusion, hemagglutinin, large polymerase, matrix, nucleocapsid, phosphoprotein, and V proteins, were processed and presented, and thus, potential targets of anti-viral CTL in DLA-88*508:01-bearing dogs. The presentation of diverse self and viral peptides indicates that DLA-88 is a classical MHC class Ia gene.
Canine Distemper Virus, CD8+ T Lymphocytes, MHC, Peptides/Epitopes, Retrovirus
The canine MHC class Ia allele DLA-88*508:01 presents diverse self-and canine distemper virus-origin peptides of varying length that have a conserved binding motif
Peter Ross,a,1 Paige S. Nemec,a Alexander Kapatos,a Keith R. Miller,c Jennifer C. Holmes,a Steven E. Suter,a Adam S. Buntzman,b Erik J. Soderblom,e Edward J. Collins,c,d,2 and Paul R. Hessa,*
2019 Mar 1.
Clear cell renal cell carcinoma (ccRCC), the most common subtype, accounts for approximately 80% of all RCC cases. ccRCC patients typically present with an advanced stage at the time of diagnosis resulting in a poor patient prognosis. The present study aimed to identify novel potential microRNAs (miRNAs or miRs) in peripheral blood as biomarkers for the detection of ccRCC. Candidate miRNAs were selected through integrated analysis of the Gene Expression Omnibus (GEO) database, The Cancer Genome Atlas (TCGA) database, and from clinical samples. The expression levels of miRNAs were quantified using reverse transcription-quantitative PCR. Receiver operating characteristic (ROC) curve analysis was used to explore the diagnostic values of the miRNAs. Bioinformatic analysis of candidate miRNAs was conducted by using the STRING database. After an integrated analysis of the GEO and TCGA databases, four miRNAs were found to be consistently dysregulated in ccRCC tissues. Then, their expression levels in serum and diagnostic utilities were further explored. We discovered that serum miR-508-3p and miR-885-5p were significantly dysregulated in ccRCC patients with marked diagnostic values. The area under the ROC curve (AUC) of serum miR-508-3p and miR-885-5p was 0.80 (95% CI, 0.73-0.87) and 0.87 (95% CI, 0.79-0.95), respectively. Functional enrichment analysis revealed that both miR-508-3p and miR-885-5p were closely associated with cellular metabolic processes. In conclusion, serum miR-508-3p and miR-885-5p are novel potential biomarkers for the diagnosis of ccRCC.
clear cell renal cell carcinoma, miRNA, biomarker, serum, bioinformatic analysis
Identification of dysregulated serum miR-508-3p and miR-885-5p as potential diagnostic biomarkers of clear cell renal carcinoma
Siming Liu,1,* Xiaojun Deng,1,* and Jiong Zhang2