24 research outputs found

    Diagnosis and Management of Atypical Mycobacterial Infection after Laparoscopic Surgery

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    Atypical mycobacterial infections at the laparoscopic port site are a frequent problem encountered in patients undergoing laparoscopic surgery. In this study we concentrate on the clinical diagnosis, management and prevention of this problem. In this series we assess 19 patients presenting with port hole infections after laparoscopic surgery and were treated with a combination of oral clarithromycin and ciprofloxacin. Seven patients who had persistent nodules were given injections of amikacin directly into the infection foci along with standard oral therapy. Most of the patients treated with standard oral therapy for 28 days showed recovery. The patients with persistent nodules 4 weeks after completion of therapy were treated with injections of amikacin directly into the nodule which lead to resolution of symptoms. For prevention of infection, proper sterilization and storage of instruments is recommended. Laparoscopic port hole infections is a preventable problem and can also be treated by nonsurgical method

    Structure and functional analysis of the IGF-II/IGF2R interaction

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    Embryonic development and normal growth require exquisite control of insulin-like growth factors (IGFs). In mammals the extracellular region of the cation-independent mannose-6-phosphate receptor has gained an IGF-II-binding function and is termed type II IGF receptor (IGF2R). IGF2R sequesters IGF-II; imbalances occur in cancers and IGF2R is implicated in tumour suppression. We report crystal structures of IGF2R domains 11–12, 11–12–13–14 and domains 11–12–13/IGF-II complex. A distinctive juxtaposition of these domains provides the IGF-II-binding unit, with domain 11 directly interacting with IGF-II and domain 13 modulating binding site flexibility. Our complex shows that Phe19 and Leu53 of IGF-II lock into a hydrophobic pocket unique to domain 11 of mammalian IGF2Rs. Mutagenesis analyses confirm this IGF-II ‘binding-hotspot', revealing that IGF-binding proteins and IGF2R have converged on the same high-affinity site
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