CM8, a human sequence with putative centromeric function, does not map to the centromere but is present in one to two copies at 9qter

1992 ◽  
Vol 1 (9) ◽  
pp. 749-751 ◽  
Author(s):  
N. I. McGill ◽  
J. Fantes ◽  
H. Cooke
Keyword(s):  
Human Sequence ◽  
Centromeric Function

Electron-Microscopic localization of biotinylated gastrin bound to eosinophils in the rat stomach

1994 ◽  
Vol 52 ◽  
pp. 300-301
Author(s):  
Caroline A. Miller ◽  
David H. Nichols ◽  
Richard F. Murphy
Keyword(s):  
Electron Microscope ◽  
Phosphate Buffer ◽  
Uranyl Acetate ◽  
List Type ◽  
Cerium Chloride ◽  
Rat Stomach ◽  
Electron Microscopic ◽  
Human Sequence ◽  
Acetate Lead ◽  
Microscope Slides

Gastrin is a small peptide capable of both stimulating gastric acid secretion and acting as an enteric growth factor. Known functions of eosinophils in the rat stomach are related to immunological defense. Here we demonstrate the binding of biotinylated gastrin to rat stomach eosinophils in the electron microscope. Small pieces of stomach were fixed by immersion in 4% paraformaldehyde/0.1% glutaraldehyde in 0.1 M phosphate buffer, pH 7.4 for 1 hour. The tissue was then cryoprotected in 30% sucrose/0.1 M phosphate buffer, transferred to Tissue Tek OCT compound and frozen in isopentane cooled with liquid nitrogen. Transverse cryostat sections were cut at 25 μm, thawed in PBS and free floating sections exposed to 10−5 M biotinylated 1-17 gastrin (human sequence; Peninsula Labs) for 1 hour. Controls omitted the biotinylated gastrin from this step. Sections were then rinsed 3X in PBS and exposed to either:1).a 1:50 dilution of 10 nm Extravidin colloidal gold (Sigma) for 2 hours, or2).an avidin-biotin-alkaline phosphatase complex (ABC-AP;Vector) for 1 hour. A substrate solution containing cerium chloride was used to generate an electron dense reaction product.Sections from both procedures were postfixed in 1% OsO4 in 0.1 M phosphate buffer, rinsed and dehydrated. These were then flat embedded in EMbed 812 between two microscope slides coated with Liquid Release (both from Electron Microscopy Sciences).Polymerized sections were adhered to resin blocks using super glue, cut at 70-90 nm, stained with uranyl acetate/lead citrate and observed in a Philips CM-10 electron microscope.

scholarly journals Altered toxicity of the prion protein peptide PrP106–126 carrying the Ala117→Val mutation

2000 ◽  
Vol 346 (3) ◽  
pp. 785-791 ◽  
Author(s):  
David R. BROWN
Keyword(s):  
Point Mutation ◽  
Prion Protein ◽  
Prion Diseases ◽  
Point Mutations ◽  
Human Sequence ◽  
Gene Coding ◽  
Normal Human ◽  
Microtubule Formation ◽  
Β Sheet ◽  
Prion Protein Peptide

The inherited prion diseases such as Gerstmann-Sträussler-Scheinker syndrome (GSS) are linked to point mutations in the gene coding for the cellular isoform of the prion protein (PrPC). One particular point mutation A117V (Ala117 → Val) is linked to a variable pathology that usually includes deposition of neurofibrillary tangles. A prion protein peptide carrying this point mutation [PrP106-126(117V)] was generated and compared with a peptide based on the normal human sequence [PrP106-126(117A)]. The inclusion of this point mutation increased the toxicity of PrP106-126 which could be linked to an increased β-sheet content. An assay of microtubule formation in the presence of tau indicated that PrP106-126 decreased the rate of microtubule formation that could be related to the displacement of tau. PrP106-126 carrying the 117 mutation was more efficient at inhibiting microtubule formation. These results suggest a possible mechanism of toxicity for protein carrying this mutation via destabilization of the cytoskeleton and deposition of tau in filaments, as observed in GSS.

The revised 8307 base pair coding sequence of human thyroglobulin transiently expressed in eukaryotic cells

1997 ◽  
Vol 136 (5) ◽  
pp. 508-515 ◽  
Author(s):  
Simone A R van de Graaf ◽  
Erwin Pauws ◽  
Jan J M de Vijlder ◽  
Carrie Ris-Stalpers
Keyword(s):  
Nucleotide Sequence ◽  
Expression System ◽  
Thyroid Tissue ◽  
Initiation Site ◽  
Human Thyroid ◽  
Translation Initiation Site ◽  
Thyroid Cells ◽  
Coding Sequence ◽  
Reverse Transcription Pcr ◽  
Human Sequence

Abstract We developed a transient transfection system for human thyroglobulin (TG) cDNA in both human thyroid cells and in COS-1 cells. Four overlapping TG cDNA fragments were amplified by reverse transcription-PCR from RNA of normal thyroid tissue. The most 5′ fragment includes the natural translation initiation site and the sequence encoding the signal peptide (SP). After subcloning, the nucleotide sequence was determined and compared with the published human sequence, resulting in the detection of 30 nucleotide variations. For validation purposes, all variations were screened in 6–12 normal human alleles. Twenty-one were present in all screened alleles and have to be revised in the published nucleotide sequence. Since one variation concerns a triplet insertion, the coding sequence of the mature human thyroglobulin is 8307 nucleotides encoding 2750 amino acids. The TG cDNA constructs were transiently transfected in HTori 3 and COS-1 cells and protein expression was detected using a polyclonal anti-human-TG on fixed cells and after SDS-PAGE. In both cell-lines all four TG protein fragments were expressed. The mannose structures detected on the proteins by lectins and localization after expression in the cells suggest that only the N-terminal TG fragment (containing the SP) is directed to the endoplasmatic reticulum but is unable to reach the Golgi complex. The described expression system in human thyrocytes will be a helpful tool in studying the structure–function relationship of human TG in thyroid hormonogenesis. European Journal of Endocrinology 136 508–515

Regulation of apo A-IV transcription by lipid in newborn swine is associated with a promoter DNA-binding protein

2003 ◽  
Vol 284 (2) ◽  
pp. G248-G254 ◽  
Author(s):  
Song Lu ◽  
Ying Yao ◽  
Heng Wang ◽  
Songmei Meng ◽  
Xiangying Cheng ◽  
...  
Keyword(s):  
Transcriptional Activation ◽  
Promoter Sequence ◽  
Dietary Lipid ◽  
Lipid Absorption ◽  
Proximal Promoter ◽  
Significant Shift ◽  
Human Sequence ◽  
Nuclear Extracts ◽  
Promoter Dna ◽  
Isocaloric Diets

Dietary lipid acutely upregulates apolipoprotein (apo) A-IV expression by sevenfold at the pretranslational level in neonatal swine jejunum. To determine the mechanism of this regulation, two-day-old female swine received intraduodenal infusions of low- and high-triacylglycerol (TG) isocaloric diets for 24 h. Nuclear runoff assay confirmed apo A-IV gene transcriptional regulation by the high-TG diet. Footprinting analysis using the swine apo A-IV proximal promoter sequence (+14 to −246 bp) demonstrated three regions protected by the low-TG extracts. Of these three motifs, only ACCTTC showed 100% homology to the human sequence and was further studied. EMSA was performed using probes containing wild-type (WT) and mutant (M) motifs. A shift was noted with the low-TG nuclear extracts with the WT probe but not with the M probe. Excess unlabeled free WT probe competed out the shift, whereas the M probe did not. No significant shift occurred with either probe using high-TG extracts. These results suggest that a repressor protein binds to the ACCTTC motif and becomes unbound during lipid absorption, allowing transcriptional activation of the apo A-IV gene in newborn swine small intestine.

Vaccination with a non-human sequence amyloid oligomer mimic results in improved cognitive function and reduced plaque deposition in Tg2576 mice

2011 ◽  
Vol 71 ◽  
pp. e85-e86
Author(s):  
Suhail Rasool ◽  
Hilda Martinez Coria ◽  
Leonoid Breydo ◽  
Jessica Wu ◽  
Saskia Milton ◽  
...  
Keyword(s):  
Cognitive Function ◽  
Plaque Deposition ◽  
Human Sequence ◽  
Tg2576 Mice ◽  
Amyloid Oligomer

scholarly journals Urotensin receptor (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

2019 ◽  
Vol 2019 (4) ◽  
Author(s):  
Anthony P. Davenport ◽  
Stephen A. Douglas ◽  
Alain Fournier ◽  
Adel Giaid ◽  
Henry Krum ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Neurosecretory System ◽  
Urotensin Ii ◽  
High Sequence Identity ◽  
Caudal Neurosecretory System ◽  
Amino Acid Peptide ◽  
Related Peptide ◽  
Human Sequence ◽  
Mature Mouse

The urotensin-II (U-II) receptor (UT, nomenclature as agreed by the NC-IUPHAR Subcommittee on the Urotensin receptor [26, 36, 89]) is activated by the endogenous dodecapeptide urotensin-II, originally isolated from the urophysis, the endocrine organ of the caudal neurosecretory system of teleost fish [7, 88]. Several structural forms of U-II exist in fish and amphibians. The goby orthologue was used to identify U-II as the cognate ligand for the predicted receptor encoded by the rat gene gpr14 [20, 62, 68, 70]. Human urotensin-II, an 11-amino-acid peptide [20], retains the cyclohexapeptide sequence of goby U-II that is thought to be important in ligand binding [53, 11]. This sequence is also conserved in the deduced amino-acid sequence of rat urotensin-II (14 amino-acids) and mouse urotensin-II (14 amino-acids), although the N-terminal is more divergent from the human sequence [19]. A second endogenous ligand for the UT has been discovered in rat [83]. This is the urotensin II-related peptide, an octapeptide that is derived from a different gene, but shares the C-terminal sequence (CFWKYCV) common to U-II from other species. Identical sequences to rat urotensin II-related peptide are predicted for the mature mouse and human peptides [32]. UT exhibits relatively high sequence identity with somatostatin, opioid and galanin receptors [89].

scholarly journals Taenia larvae possess distinct acetylcholinesterase profiles with implications for host cholinergic signalling

2020 ◽  
Vol 14 (12) ◽  
pp. e0008966
Author(s):  
Anja de Lange ◽  
Ulrich Fabien Prodjinotho ◽  
Hayley Tomes ◽  
Jana Hagen ◽  
Brittany-Amber Jacobs ◽  
...  
Keyword(s):  
Membrane Surface ◽  
Taenia Solium ◽  
Acetylcholinesterase Activity ◽  
Bioinformatic Analysis ◽  
Functional Protein ◽  
Taenia Crassiceps ◽  
Human Sequence ◽  
Neuronal Signalling ◽  
Whole Cell Patch Clamp ◽  
Acquired Epilepsy

Larvae of the cestodes Taenia solium and Taenia crassiceps infect the central nervous system of humans. Taenia solium larvae in the brain cause neurocysticercosis, the leading cause of adult-acquired epilepsy worldwide. Relatively little is understood about how cestode-derived products modulate host neural and immune signalling. Acetylcholinesterases, a class of enzyme that breaks down acetylcholine, are produced by a host of parasitic worms to aid their survival in the host. Acetylcholine is an important signalling molecule in both the human nervous and immune systems, with powerful modulatory effects on the excitability of cortical networks. Therefore, it is important to establish whether cestode derived acetylcholinesterases may alter host neuronal cholinergic signalling. Here we make use of multiple techniques to profile acetylcholinesterase activity in different extracts of both Taenia crassiceps and Taenia solium larvae. We find that the larvae of both species contain substantial acetylcholinesterase activity. However, acetylcholinesterase activity is lower in Taenia solium as compared to Taenia crassiceps larvae. Further, whilst we observed acetylcholinesterase activity in all fractions of Taenia crassiceps larvae, including on the membrane surface and in the excreted/secreted extracts, we could not identify acetylcholinesterases on the membrane surface or in the excreted/secreted extracts of Taenia solium larvae. Bioinformatic analysis revealed conservation of the functional protein domains in the Taenia solium acetylcholinesterases, when compared to the homologous human sequence. Finally, using whole-cell patch clamp recordings in rat hippocampal brain slice cultures, we demonstrate that Taenia larval derived acetylcholinesterases can break down acetylcholine at a concentration which induces changes in neuronal signalling. Together, these findings highlight the possibility that Taenia larval acetylcholinesterases can interfere with cholinergic signalling in the host, potentially contributing to pathogenesis in neurocysticercosis.

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