ABSTRACT
The diagnostic time required for a full, 8-hour video capsule endoscopy is usually between 45 and 120 min. The aim of this work is to evaluate the diagnostic time required when applying a method that adaptively controlls the image display rate. The advantage of the method is that the sequence can be played at high speed in stable smooth sequences to save time and then decreased at sequences where there are sudden rough changes, in order to assess suspicious findings detail. In this paper, this method is examined under real conditions: 10 sequences were independently evaluated by 4 medical doctors. The methods of evaluation include: 1) the time required for reading a sequence, 2) the percentage of abnormal regions accurately found, and 3) the manipulations of the evaluating physicians. The results indicate that the proposed method reduces diagnostic time to around 10 +/- 1.5% length of the sequence and is of valuable assistance to medical doctors.
Subject(s)
Capsule Endoscopy/methods , Image Interpretation, Computer-Assisted/methods , Intestinal Diseases/diagnosis , Intestine, Small/pathology , Humans , Physicians , Sensitivity and Specificity , Time Factors , Video RecordingABSTRACT
BACKGROUND: Fractalkine expressed on endothelial cells mediates activation and adhesion of leucocytes expressing its receptor, CX(3)CR1. Soluble fractalkine exhibits chemotactic activity for leucocytes expressing CX(3)CR1. OBJECTIVE: To determine the role of fractalkine and its receptor in systemic sclerosis (SSc) by assessing their expression levels in patients with this disease. METHODS: The expression of fractalkine and CX(3)CR1 in the skin and lung tissues was immunohistochemically examined. Circulating soluble fractalkine levels were examined by enzyme linked immunosorbent assay (ELISA). Blood samples from patients with SSc were stained for CX(3)CR1 with flow cytometric analysis. RESULTS: CX(3)CR1 levels on peripheral monocytes/macrophages and T cells were found to be raised in patients with diffuse cutaneous SSc. The numbers of cells expressing CX(3)CR1, including monocytes/macrophages, were increased in the lesional skin and lung tissues from patients with diffuse cutaneous SSc. Fractalkine was strongly expressed on endothelial cells in the affected skin and lung tissues. Soluble fractalkine levels were significantly raised in sera and were associated with raised erythrocyte sedimentation rates, digital ischaemia, and severity of pulmonary fibrosis. CONCLUSIONS: Up regulated expression of fractalkine and CX(3)CR1 cooperatively augments the recruitment of mononuclear cells expressing CX(3)CR1 into the affected tissue of SSc, leading to inflammation and vascular injury.
Subject(s)
Chemokines, CX3C/metabolism , Membrane Proteins/metabolism , Receptors, Cytokine/metabolism , Receptors, HIV/metabolism , Scleroderma, Systemic/metabolism , Up-Regulation , Adult , Aged , CX3C Chemokine Receptor 1 , Chemokine CX3CL1 , Chemokines, CX3C/blood , Enzyme-Linked Immunosorbent Assay , Female , Humans , Immunoenzyme Techniques , Lung/metabolism , Male , Membrane Proteins/blood , Middle Aged , Pulmonary Fibrosis/metabolism , Receptors, Cytokine/blood , Receptors, HIV/blood , Scleroderma, Systemic/blood , Scleroderma, Systemic/pathology , Skin/metabolismABSTRACT
A 68-year-old woman who had been diagnosed with sarcoidosis presented with acral lentiginous melanoma (Breslow's tumour thickness, 2.6 mm; Clark's level IV) on her right heel. She underwent surgery for excision of the primary tumour and sentinel lymph node biopsy. The two sentinel lymph nodes revealed numerous sarcoidal granulomas and small nests of metastatic melanoma cells in the subcapuslar lesions. She subsequently underwent ilio-inguinal lymph node dissection. Surprisingly, all of the nine dissected nodes were mostly replaced by sarcoidal granulomas and contained melanoma micrometastases.
Subject(s)
Granuloma/complications , Melanoma/complications , Skin Neoplasms/complications , Aged , Female , Granuloma/pathology , Humans , Lymphatic Metastasis , Melanoma/secondary , Sarcoidosis/complications , Sarcoidosis/pathology , Sentinel Lymph Node Biopsy/methods , Skin Neoplasms/pathologyABSTRACT
BACKGROUND: Aneurysms of the proximal segment of anterior cerebral artery (A1) are uncommon, but present a unique challenge to surgeons because of the risk of injury to the nearby perforating arteries. Surgical issues and treatment options, however, have not been detailed in the previous literature. METHOD: We report a consecutive series of 11 patients with A1 aneurysms focusing on the surgical considerations. The A1 aneurysms represented 3.4% of the 322 cerebral aneurysms treated in our hospital in the last 6 years. All patients presented with subarachnoid hemorrhage, and 8 patients (73%) had multiple aneurysms. FINDINGS: All aneurysms were secured by neck clipping via pterional craniotomy without any surgery-related morbidity. All of the aneurysms projected superiorly or posteriorly from the origin of the perforating artery of the A1 segment. The aneurysm dome was tightly adherent to the perforating arteries in 7 cases (64%) and the base extended broadly along the axis of the parent artery in 4 cases (36%). INTERPRETATION: Separating the perforating arteries from the neck or dome of the A1 aneurysm and preserving the vessel presents a substantial challenge to the surgeon, because the aneurysm is almost always behind the parent artery in the surgical field, making it difficult to achieve good access for this particular type of dissection. Consideration should be given to additional orbitotomy, wide opening of the Sylvian fissure, mobilization of the MCA and ICA, selection of aperture clip and intra-operative shortening of the clip blades.
Subject(s)
Anterior Cerebral Artery/surgery , Intracranial Aneurysm/surgery , Adult , Aged , Angiography, Digital Subtraction , Anterior Cerebral Artery/diagnostic imaging , Female , Glasgow Outcome Scale , Humans , Intracranial Aneurysm/diagnostic imaging , Male , Middle Aged , Tomography, X-Ray ComputedSubject(s)
Escherichia coli/enzymology , Peptides/chemical synthesis , gamma-Glutamyltransferase/metabolism , Animals , Cloning, Molecular/methods , Escherichia coli/genetics , Genes, Bacterial , Humans , Kinetics , Recombinant Proteins/isolation & purification , Recombinant Proteins/metabolism , Substrate Specificity , gamma-Glutamyltransferase/genetics , gamma-Glutamyltransferase/isolation & purificationABSTRACT
The DNA sequence of ggt, the gene that codes for gamma-glutamyltranspeptidase (EC 2.3.2.2) of Escherichia coli K-12, has been determined. The sequence contains a single open reading frame encoding the signal peptide and large and small subunits, in that order. This result suggests that E. coli gamma-glutamyltranspeptidase is processed posttranslationally.
Subject(s)
DNA, Bacterial/genetics , Escherichia coli/genetics , Genes, Bacterial , Genes , gamma-Glutamyltransferase/genetics , Amino Acid Sequence , Animals , Base Sequence , Escherichia coli/enzymology , Humans , Kidney/enzymology , Liver/enzymology , Molecular Sequence Data , Rats , Sequence Homology, Nucleic AcidABSTRACT
Based on the results of mapping of ggt, eight strains were selected from a gene library of E. coli. One of the strains harboring pLC9-12 was found to show 14 times higher gamma-glutamyltranspeptidase activity per cell than the wild type strain. The ggt was subcloned to the BamHI site of pUC18 and the recombinant plasmid pSH101 was obtained. Ggt- phenotype of gamma-glutamyltranspeptidase-deficient mutants was complemented by pSH101. The specific activity of the enzyme in cells harboring pSH101 was 37-fold higher than that in the wild type cells. gamma-Glutamyltranspeptidase was isolated from the periplasmic fraction of the cells by simple two steps and crystallized.
