Treatment of Postcatheterisation False Aneurysms: Ultrasound-guided Compression vs Ultrasound-guided Thrombin Injection

AbstractObjectives: to compare the efficacy and cost-effectiveness of ultrasound-guided compression (UGC) with ultrasound-guided thrombin injection (UGTI) for treatment of postcatheterisation arterial false aneurysms (cFA). Design: prospective clinical study using historical controls. Materials and Methods: we prospectively collected data on 33 consecutive patients diagnosed with cFA larger than 1.5 cm in diameter. These were treated with UGTI. We performed a retrospective review of data on a former group of 33 consecutive historical control patients that were treated by UGC. Results: the groups were similar in respect of demographic and clinical variables. Thirty patients were suitable for UGC and 33 patients were suitable for UGTI. The success rate for UGC was 26/30 (87%) compared to 33/33 (100%) for UGTI (p<0.05). Thrombosis was achieved during the first treatment session in 7/26 patients treated by UGC, compared to 26/33 in the UGTI group (p<0.0001). Four patients that failed UGC and two patients that were unsuitable for UGC required surgical repair. UGTI as compared to UGC was shorter in duration (25 vs 75 min) and required no sedation. No thromboembolic or systemic complications occurred in either group. Cost analysis revealed savings of $US 517 for each patient treated by UGTI as compared with UGC. Conclusions: in our study, UGTI is superior to UGC, and we suggest that UGTI should become the procedure of choice for the treatment of cFA

A Linear Epitope in the N-Terminal Domain of CCR5 and Its Interaction with Antibody.

The CCR5 receptor plays a role in several key physiological and pathological processes and is an important therapeutic target. Inhibition of the CCR5 axis by passive or active immunisation offers one very selective strategy for intervention. In this study we define a new linear epitope within the extracellular domain of CCR5 recognised by two independently produced monoclonal antibodies. A short peptide encoding the linear epitope can induce antibodies which recognise the intact receptor when administered colinear with a tetanus toxoid helper T cell epitope. The monoclonal antibody RoAb 13 is shown to bind to both cells and peptide with moderate to high affinity (6x10^8 and 1.2x107 M-1 respectively), and binding to the peptide is enhanced by sulfation of tyrosines at positions 10 and 14. RoAb13, which has previously been shown to block HIV infection, also blocks migration of monocytes in response to CCR5 binding chemokines and to inflammatory macrophage conditioned medium. A Fab fragment of RoAb13 has been crystallised and a structure of the antibody is reported to 2.1 angstrom resolution

Trends and Challenges in Experimental Macromolecular Crystallography

Macromolecular X-ray crystallography underpins the vigorous field of structural molecular biology having yielded many protein, nucleic acid and virus structures in fine detail. The understanding of the recognition by these macromolecules, as receptors, of their cognate ligands involves the detailed study of the structural chemistry of their molecular interactions. Also these structural details underpin the rational design of novel inhibitors in modern drug discovery in the pharmaceutical industry. Moreover, from such structures the functional details can be inferred, such as the biological chemistry of enzyme reactivity. There is then a vast number and range of types of biological macromolecules that potentially could be studied. The completion of the protein primary sequencing of the yeast genome, and the human genome sequencing project comprising some 105 proteins that is underway, raises expectations for equivalent three dimensional structural database

Interaction between Plate Make and Protein in Protein Crystallisation Screening

Background: Protein crystallisation screening involves the parallel testing of large numbers of candidate conditions with the aim of identifying conditions suitable as a starting point for the production of diffraction quality crystals. Generally, condition screening is performed in 96-well plates. While previous studies have examined the effects of protein construct, protein purity, or crystallisation condition ingredients on protein crystallisation, few have examined the effect of the crystallisation plate

On the need for an international effort to capture, share and use crystallization screening data

Development of an ontology for the description of crystallization experiments and results is proposed

Enhancement of crystallization with nucleotide ligands identified by dye-ligand affinity chromatography

Ligands interacting with Mycobacterium tuberculosis recombinant proteins were identified through use of the ability of Cibacron Blue F3GA dye to interact with nucleoside/nucleotide binding proteins, and the effects of these ligands on crystallization were examined. Co-crystallization with ligands enhanced crystallization and enabled X-ray diffraction data to be collected to a resolution of at least 2.7 Å for 5 of 10 proteins tested. Additionally, clues about individual proteins’ functions were obtained from their interactions with each of a panel of ligands