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1.
J Vasc Surg Cases Innov Tech ; 8(3): 494-495, 2022 Sep.
Article in English | MEDLINE | ID: mdl-36052206

ABSTRACT

The increasing use of endovascular aneurysm repair to treat abdominal aortic aneurysms has mandated solutions to the limitations of this operation, including the requirement for additional procedures. A 64-year-old man had presented with symptomatic thrombosis of the left iliac limb after endovascular aneurysm repair. We have reported the use of an innovative endovascular repair for our patient.

2.
J Am Pharm Assoc (2003) ; 60(6): 930-936.e10, 2020.
Article in English | MEDLINE | ID: mdl-32713749

ABSTRACT

OBJECTIVES: The objectives of this study were (1) to determine the rate of antibiotic prescribing at ambulatory clinics, and (2) to assess the concordance of antibiotic prescriptions with published guidelines and Food and Drug Administration-approved indications in terms of drug choices and dosing regimen. DESIGN: Cross-sectional study. SETTING AND PARTICIPANTS: Patients of all ages receiving at least 1 prescription during ambulatory visits in 2016 to 2017 were observed. OUTCOME MEASURES: For each of the 3 clinic systems included in this study, oral antibiotic prescribing rates were estimated per patient and per ambulatory visit. Then, the concordance of oral antibiotic prescribing was assessed with respect to (1) choice of agent and (2) the dosing regimen by comparing it to the recommended therapeutic regimen (RTR). RESULTS: A total of 284,348 patients receiving at least 1 prescription were included in the analysis. Between clinics, 17.4 to 43.7 per 100 patients received antibiotics. Of the antibiotics prescribed, 48.9% in Clinic A, 48.0% in Clinic B, and 60.7% in Clinic C were considered to be discordant in terms of drug choice. When the dosing regimen was taken into account in addition to the choice of agent, 72.6% in Clinic A, 76.7% in Clinic B, and 81.6% in Clinic C were discordant based on drug choice or dosing regimen. Of the prescriptions written with a discordant dosing regimen, 91.2% in Clinic A, 79.6% in Clinic B, and 91.0% in Clinic C were at a higher dosage than RTR. CONCLUSION: Antibiotic prescribing rates vary by clinics, whereas discordant prescribing is consistently prevalent across clinics. More efforts should be put into ambulatory care to address antibiotic misuse problems, and our method could improve ambulatory antimicrobial stewardship programs.


Subject(s)
Anti-Bacterial Agents , Antimicrobial Stewardship , Ambulatory Care Facilities , Anti-Bacterial Agents/therapeutic use , Cross-Sectional Studies , Humans , Practice Patterns, Physicians'
3.
Genome Res ; 29(6): 1036-1045, 2019 06.
Article in English | MEDLINE | ID: mdl-31123079

ABSTRACT

We have used RNA-seq in Caenorhabditis elegans to produce transcription profiles for seven specific embryonic cell populations from gastrulation to the onset of terminal differentiation. The expression data for these seven cell populations, covering major cell lineages and tissues in the worm, reveal the complex and dynamic changes in gene expression, both spatially and temporally. Also, within genes, start sites and exon usage can be highly differential, producing transcripts that are specific to developmental periods or cell lineages. We have also found evidence of novel exons and introns, as well as differential usage of SL1 and SL2 splice leaders. By combining this data set with the modERN ChIP-seq resource, we are able to support and predict gene regulatory relationships. The detailed information on differences and similarities between gene expression in cell lineages and tissues should be of great value to the community and provides a framework for the investigation of expression in individual cells.


Subject(s)
Alternative Splicing , Caenorhabditis elegans/genetics , Embryonic Development/genetics , Transcriptome , Animals , Caenorhabditis elegans/embryology , Computational Biology/methods , Exons , Gene Expression Profiling , Gene Expression Regulation, Developmental , Introns , Molecular Sequence Annotation , Organ Specificity , RNA Editing , RNA Splice Sites
4.
J Vis Exp ; (127)2017 09 13.
Article in English | MEDLINE | ID: mdl-28930977

ABSTRACT

This manuscript describes how to classify nematodes using temporal far-field diffraction signatures. A single C. elegans is suspended in a water column inside an optical cuvette. A 632 nm continuous wave HeNe laser is directed through the cuvette using front surface mirrors. A significant distance of at least 20-30 cm traveled after the light passes through the cuvette ensures a useful far-field (Fraunhofer) diffraction pattern. The diffraction pattern changes in real time as the nematode swims within the laser beam. The photodiode is placed off-center in the diffraction pattern. The voltage signal from the photodiode is observed in real time and recorded using a digital oscilloscope. This process is repeated for 139 wild type and 108 "roller" C. elegans. Wild type worms exhibit a rapid oscillation pattern in solution. The "roller" worms have a mutation in a key component of the cuticle that interferes with smooth locomotion. Time intervals that are not free of saturation and inactivity are discarded. It is practical to divide each average by its maximum to compare relative intensities. The signal for each worm is Fourier transformed so that the frequency pattern for each worm emerges. The signal for each type of worm is averaged. The averaged Fourier spectra for the wild type and the "roller" C. elegans are distinctly different and reveal that the dynamic worm shapes of the two different worm strains can be distinguished using Fourier analysis. The Fourier spectra of each worm strain match an approximate model using two different binary worm shapes that correspond to locomotory moments. The envelope of the averaged frequency distribution for actual and modeled worms confirms the model matches the data. This method can serve as a baseline for Fourier analysis for many microscopic species, as every microorganism will have its unique Fourier spectrum.


Subject(s)
Caenorhabditis elegans/anatomy & histology , X-Ray Diffraction/methods , Animals
5.
Mol Biol Cell ; 24(5): 601-16, 2013 Mar.
Article in English | MEDLINE | ID: mdl-23283987

ABSTRACT

We identify cpna-1 (F31D5.3) as a novel essential muscle gene in the nematode Caenorhabditis elegans. Antibodies specific to copine domain protein atypical-1 (CPNA-1), as well as a yellow fluorescent protein translational fusion, are localized to integrin attachment sites (M-lines and dense bodies) in the body-wall muscle of C. elegans. CPNA-1 contains an N-terminal predicted transmembrane domain and a C-terminal copine domain and binds to the M-line/dense body protein PAT-6 (actopaxin) and the M-line proteins UNC-89 (obscurin), LIM-9 (FHL), SCPL-1 (SCP), and UNC-96. Proper CPNA-1 localization is dependent upon PAT-6 in embryonic and adult muscle. Nematodes lacking cpna-1 arrest elongation at the twofold stage of embryogenesis and display disruption of the myofilament lattice. The thick-filament component myosin heavy chain MYO-3 and the M-line component UNC-89 are initially localized properly in cpna-1-null embryos. However, in these embryos, when contraction begins, MYO-3 and UNC-89 become mislocalized into large foci and animals die. We propose that CPNA-1 acts as a linker between an integrin-associated protein, PAT-6, and membrane-distal components of integrin adhesion complexes in the muscle of C. elegans.


Subject(s)
Caenorhabditis elegans Proteins/metabolism , Carrier Proteins/metabolism , Embryonic Development , Integrins/metabolism , Myofibrils/genetics , Actin Cytoskeleton/metabolism , Animals , Caenorhabditis elegans/genetics , Caenorhabditis elegans/growth & development , Caenorhabditis elegans/metabolism , Carrier Proteins/genetics , Gene Expression Regulation, Developmental , Muscle Development , Muscles/metabolism , Myofibrils/metabolism , Protein Binding , Protein Structure, Tertiary
6.
Pulmäo RJ ; 21(2): 33-40, 2012. tab
Article in English | LILACS | ID: lil-668386

ABSTRACT

A asma é uma doença complexa. Sua característica cardial é a inflamação crônica que leva a hiper-responsividade brônquica. Como nenhum tratamento é capaz de modificar a história natural da asma, todas as abordagens terapêuticas disponíveis devem ser consideradas com a finalidade de se atingir o controle da asma e não sua cura. O principal objetivo do controle é o tratamento efetivo da inflamação da via aérea. Na maior parte dos casos, são necessáriosagentes farmacológicos para obter o controle. Os β2-agonistas de curta duração são os medicamentos preferidos para o alívio, graças a seu início rápido de ação. Os corticosteroides inalatórios são o tratamento mais efetivo para o controle dos sintomas asmáticos em longo prazo. Entretanto, em pacientes com asma persistente moderada a grave, é necessária terapia coadjuvante. Adicionar um β2-agonista de longa duração é mais efetivo na melhora dos sintomas do que agregar um antagonista dos receptores de leucotrienos. A teofilina continua a ter um papel específico em pacientes com pouca resposta aos corticosteroides inalatórios. O papel dos anticolinérgicos está evoluindo. Aproximadamente 10% dos asmáticos têm sintomas refratáriosmesmo com a combinação de tratamentos de controle. A imunoterapia surge como uma alternativa potencial no tratamento desse grupo heterogêneo de alto risco


Subject(s)
Humans , Male , Female , Asthma/immunology , Asthma/prevention & control , Asthma/therapy , Respiratory Therapy , Respiratory Tract Diseases
7.
Mol Biol Cell ; 22(14): 2551-63, 2011 Jul 15.
Article in English | MEDLINE | ID: mdl-21633109

ABSTRACT

We have identified the gene C28H8.6 (pxl-1) as the Caenorhabditis elegans orthologue of vertebrate paxillin. PXL-1 contains the four C-terminal LIM domains conserved in paxillin across all species and three of the five LD motifs found in the N-terminal half of most paxillins. In body wall muscle, PXL-1 antibodies and a full-length green fluorescent protein translational fusion localize to adhesion sites in the sarcomere, the functional repeat unit in muscle responsible for contraction. PXL-1 also localizes to ring-shaped structures near the sarcolemma in pharyngeal muscle corresponding to podosome-like sites of actin attachment. Our analysis of a loss-of-function allele of pxl-1, ok1483, shows that loss of paxillin leads to early larval arrested animals with paralyzed pharyngeal muscles and eventual lethality, presumably due to an inability to feed. We rescued the mutant phenotype by expressing paxillin solely in the pharynx and found that these animals survived and are essentially wild type in movement and body wall muscle structure. This indicates a differential requirement for paxillin in these two types of muscle. In pharyngeal muscle it is essential for contraction, whereas in body wall muscle it is dispensable for filament assembly, sarcomere stability, and ultimately movement.


Subject(s)
Caenorhabditis elegans/physiology , Muscle Contraction , Paxillin/physiology , Pharyngeal Muscles/physiology , Actin Cytoskeleton/ultrastructure , Amino Acid Motifs , Amino Acid Sequence , Animals , Caenorhabditis elegans/genetics , Caenorhabditis elegans/metabolism , Caenorhabditis elegans Proteins/metabolism , Carrier Proteins/metabolism , Cell Survival/genetics , Genes, Lethal , Intracellular Signaling Peptides and Proteins , Larva/genetics , Larva/physiology , Molecular Sequence Data , Mutation , Paxillin/genetics , Pharyngeal Muscles/metabolism , Phenotype , Protein Isoforms/genetics , Protein Structure, Tertiary , Sarcomeres/physiology
8.
PLoS One ; 6(5): e19937, 2011.
Article in English | MEDLINE | ID: mdl-21611156

ABSTRACT

Determining the sub-cellular localization of a protein within a cell is often an essential step towards understanding its function. In Caenorhabditis elegans, the relatively large size of the body wall muscle cells and the exquisite organization of their sarcomeres offer an opportunity to identify the precise position of proteins within cell substructures. Our goal in this study is to generate a comprehensive "localizome" for C. elegans body wall muscle by GFP-tagging proteins expressed in muscle and determining their location within the cell. For this project, we focused on proteins that we know are expressed in muscle and are orthologs or at least homologs of human proteins. To date we have analyzed the expression of about 227 GFP-tagged proteins that show localized expression in the body wall muscle of this nematode (e.g. dense bodies, M-lines, myofilaments, mitochondria, cell membrane, nucleus or nucleolus). For most proteins analyzed in this study no prior data on sub-cellular localization was available. In addition to discrete sub-cellular localization we observe overlapping patterns of localization including the presence of a protein in the dense body and the nucleus, or the dense body and the M-lines. In total we discern more than 14 sub-cellular localization patterns within nematode body wall muscle. The localization of this large set of proteins within a muscle cell will serve as an invaluable resource in our investigation of muscle sarcomere assembly and function.


Subject(s)
Caenorhabditis elegans Proteins/metabolism , Caenorhabditis elegans/metabolism , Muscles/metabolism , Animals , Caenorhabditis elegans/cytology , Cloning, Molecular , Genome/genetics , Green Fluorescent Proteins/metabolism , Humans , Mitochondrial Proteins/metabolism , Muscles/cytology , Open Reading Frames/genetics , Phenotype , Protein Transport , RNA Interference , Recombinant Fusion Proteins/metabolism , Subcellular Fractions/metabolism
9.
PLoS Genet ; 5(6): e1000537, 2009 Jun.
Article in English | MEDLINE | ID: mdl-19557190

ABSTRACT

A crucial step in the development of muscle cells in all metazoan animals is the assembly and anchorage of the sarcomere, the essential repeat unit responsible for muscle contraction. In Caenorhabditis elegans, many of the critical proteins involved in this process have been uncovered through mutational screens focusing on uncoordinated movement and embryonic arrest phenotypes. We propose that additional sarcomeric proteins exist for which there is a less severe, or entirely different, mutant phenotype produced in their absence. We have used Serial Analysis of Gene Expression (SAGE) to generate a comprehensive profile of late embryonic muscle gene expression. We generated two replicate long SAGE libraries for sorted embryonic muscle cells, identifying 7,974 protein-coding genes. A refined list of 3,577 genes expressed in muscle cells was compiled from the overlap between our SAGE data and available microarray data. Using the genes in our refined list, we have performed two separate RNA interference (RNAi) screens to identify novel genes that play a role in sarcomere assembly and/or maintenance in either embryonic or adult muscle. To identify muscle defects in embryos, we screened specifically for the Pat embryonic arrest phenotype. To visualize muscle defects in adult animals, we fed dsRNA to worms producing a GFP-tagged myosin protein, thus allowing us to analyze their myofilament organization under gene knockdown conditions using fluorescence microscopy. By eliminating or severely reducing the expression of 3,300 genes using RNAi, we identified 122 genes necessary for proper myofilament organization, 108 of which are genes without a previously characterized role in muscle. Many of the genes affecting sarcomere integrity have human homologs for which little or nothing is known.


Subject(s)
Actin Cytoskeleton/chemistry , Caenorhabditis elegans/genetics , Gene Expression Profiling/methods , Muscle Development , Actin Cytoskeleton/genetics , Actin Cytoskeleton/metabolism , Animals , Caenorhabditis elegans/chemistry , Caenorhabditis elegans/embryology , Caenorhabditis elegans/metabolism , Caenorhabditis elegans Proteins/genetics , Caenorhabditis elegans Proteins/metabolism , Gene Expression Regulation, Developmental , Muscles/chemistry , Muscles/embryology , Muscles/metabolism , Sarcomeres/genetics , Sarcomeres/metabolism
10.
Dev Biol ; 327(2): 551-65, 2009 Mar 15.
Article in English | MEDLINE | ID: mdl-19111532

ABSTRACT

Starting with SAGE-libraries prepared from C. elegans FAC-sorted embryonic intestine cells (8E-16E cell stage), from total embryos and from purified oocytes, and taking advantage of the NextDB in situ hybridization data base, we define sets of genes highly expressed from the zygotic genome, and expressed either exclusively or preferentially in the embryonic intestine or in the intestine of newly hatched larvae; we had previously defined a similarly expressed set of genes from the adult intestine. We show that an extended TGATAA-like sequence is essentially the only candidate for a cis-acting regulatory motif common to intestine genes expressed at all stages. This sequence is a strong ELT-2 binding site and matches the sequence of GATA-like sites found to be important for the expression of every intestinal gene so far analyzed experimentally. We show that the majority of these three sets of highly expressed intestinal-specific/intestinal-enriched genes respond strongly to ectopic expression of ELT-2 within the embryo. By flow-sorting elt-2(null) larvae from elt-2(+) larvae and then preparing Solexa/Illumina-SAGE libraries, we show that the majority of these genes also respond strongly to loss-of-function of ELT-2. To test the consequences of loss of other transcription factors identified in the embryonic intestine, we develop a strain of worms that is RNAi-sensitive only in the intestine; however, we are unable (with one possible exception) to identify any other transcription factor whose intestinal loss-of-function causes a phenotype of comparable severity to the phenotype caused by loss of ELT-2. Overall, our results support a model in which ELT-2 is the predominant transcription factor in the post-specification C. elegans intestine and participates directly in the transcriptional regulation of the majority (>80%) of intestinal genes. We present evidence that ELT-2 plays a central role in most aspects of C. elegans intestinal physiology: establishing the structure of the enterocyte, regulating enzymes and transporters involved in digestion and nutrition, responding to environmental toxins and pathogenic infections, and regulating the downstream intestinal components of the daf-2/daf-16 pathway influencing aging and longevity.


Subject(s)
Caenorhabditis elegans Proteins/metabolism , Caenorhabditis elegans , GATA Transcription Factors/metabolism , Gene Expression Regulation, Developmental , Intestines/physiology , Animals , Base Sequence , Caenorhabditis elegans/anatomy & histology , Caenorhabditis elegans/embryology , Caenorhabditis elegans/growth & development , Caenorhabditis elegans Proteins/genetics , Computational Biology , GATA Transcription Factors/genetics , Intestines/anatomy & histology , Molecular Sequence Data , Phenotype , Promoter Regions, Genetic , RNA Interference , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Signal Transduction/physiology
11.
Curr Biol ; 15(10): 935-41, 2005 May 24.
Article in English | MEDLINE | ID: mdl-15916950

ABSTRACT

Cilia and flagella play important roles in many physiological processes, including cell and fluid movement, sensory perception, and development. The biogenesis and maintenance of cilia depend on intraflagellar transport (IFT), a motility process that operates bidirectionally along the ciliary axoneme. Disruption in IFT and cilia function causes several human disorders, including polycystic kidneys, retinal dystrophy, neurosensory impairment, and Bardet-Biedl syndrome (BBS). To uncover new ciliary components, including IFT proteins, we compared C. elegans ciliated neuronal and nonciliated cells through serial analysis of gene expression (SAGE) and screened for genes potentially regulated by the ciliogenic transcription factor, DAF-19. Using these complementary approaches, we identified numerous candidate ciliary genes and confirmed the ciliated-cell-specific expression of 14 novel genes. One of these, C27H5.7a, encodes a ciliary protein that undergoes IFT. As with other IFT proteins, its ciliary localization and transport is disrupted by mutations in IFT and bbs genes. Furthermore, we demonstrate that the ciliary structural defect of C. elegans dyf-13(mn396) mutants is caused by a mutation in C27H5.7a. Together, our findings help define a ciliary transcriptome and suggest that DYF-13, an evolutionarily conserved protein, is a novel core IFT component required for cilia function.


Subject(s)
Caenorhabditis elegans/genetics , Cilia/genetics , Gene Expression Profiling , Neurons/metabolism , Animals , Base Sequence , Caenorhabditis elegans Proteins/metabolism , Cilia/metabolism , Computational Biology , Genomics/methods , Green Fluorescent Proteins , Mutation/genetics , Protein Transport/physiology , Sequence Analysis, DNA , Transcription Factors/metabolism
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