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1.
Diagn Interv Radiol ; 24(3): 158-165, 2018.
Article in English | MEDLINE | ID: mdl-29770769

ABSTRACT

PURPOSE: We aimed to assess the safety and technical outcome of computed tomography (CT) fluoroscopy-guided osteoplasty with or without prior percutaneous radiofrequency ablation (RFA) in patients with painful osteolyses. METHODS: We performed a retrospective analysis of 29 patients with painful extraspinal and spinal osteolyses (16 women, 13 men; 63.1±14.4 years) who underwent CT fluoroscopy-guided osteoplasty (10-20 mAs tube current) with or without RFA (26 and 14 lesions, respectively), in 33 consecutive procedures from 2002 to 2016. Technical success was defined as at least one complete RFA cycle and subsequent polymethyl metacrylate (PMMA) bone cement injection covering ≥75% of longest diameter of extraspinal osteolysis on axial plane or of distance between vertebral endplates. Procedure-related complications within 30 days and dose-length-product (DLP) were also evaluated. RESULTS: Osteolyses were located in the pelvis (acetabulum, n=10; iliac bone, n=4), spine (thoracic, n=6; lumbar, n=5; sacral, n=8), long bones (femur, n=3; tibia, n=1), sternum (n=2) and glenoid (n=1). Mean size of the treated osteolysis was 4.0±1.2 cm (range, 1.9-6.9 cm). Of 40 osteolyses, 31 (77.5%) abutted neighboring risk structures (spinal canal or neuroforamen, n=18; neighboring joint, n=11; other, n=8). Mean number of RFA electrode positions and complete ablation cycles was 1.5±0.9 and 2.1±1.7, respectively. Mean PMMA filling volume was 7.7±5.7 mL (range, 2-30 mL). Small asymptomatic PMMA leakages were observed in 15 lesions (37.5%). Mean total DLP was 850±653 mGy*cm. Six minor complications were observed, without any major complications. CONCLUSION: CT fluoroscopy-guided percutaneous osteoplasty with or without concomitant RFA for the treatment of painful extraspinal and spinal osteolyses can be performed with a low complication rate and high technical success.


Subject(s)
Bone Neoplasms/secondary , Bone Neoplasms/surgery , Catheter Ablation/instrumentation , Cementoplasty/instrumentation , Fluoroscopy/methods , Spine/pathology , Spine/surgery , Aged , Bone Cements/therapeutic use , Bone Neoplasms/diagnostic imaging , Bone Neoplasms/pathology , Catheter Ablation/adverse effects , Cementoplasty/adverse effects , Female , Humans , Male , Middle Aged , Neoplasm Metastasis/diagnostic imaging , Neoplasm Metastasis/pathology , Osteolysis/pathology , Osteolysis/surgery , Osteolysis/therapy , Pain/etiology , Pain/surgery , Palliative Care/methods , Pelvis/pathology , Pelvis/surgery , Polymethyl Methacrylate/administration & dosage , Polymethyl Methacrylate/adverse effects , Polymethyl Methacrylate/therapeutic use , Retrospective Studies , Spine/diagnostic imaging , Tomography, X-Ray Computed/instrumentation
2.
Mol Biol Cell ; 22(20): 3758-67, 2011 Oct.
Article in English | MEDLINE | ID: mdl-21865601

ABSTRACT

The copper chaperone for superoxide dismutase 1 (Ccs1) provides an important cellular function against oxidative stress. Ccs1 is present in the cytosol and in the intermembrane space (IMS) of mitochondria. Its import into the IMS depends on the Mia40/Erv1 disulfide relay system, although Ccs1 is, in contrast to typical substrates, a multidomain protein and lacks twin Cx(n)C motifs. We report on the molecular mechanism of the mitochondrial import of Saccharomyces cerevisiae Ccs1 as the first member of a novel class of unconventional substrates of the disulfide relay system. We show that the mitochondrial form of Ccs1 contains a stable disulfide bond between cysteine residues C27 and C64. In the absence of these cysteines, the levels of Ccs1 and Sod1 in mitochondria are strongly reduced. Furthermore, C64 of Ccs1 is required for formation of a Ccs1 disulfide intermediate with Mia40. We conclude that the Mia40/Erv1 disulfide relay system introduces a structural disulfide bond in Ccs1 between the cysteine residues C27 and C64, thereby promoting mitochondrial import of this unconventional substrate. Thus the disulfide relay system is able to form, in addition to double disulfide bonds in twin Cx(n)C motifs, single structural disulfide bonds in complex protein domains.


Subject(s)
Cysteine , Mitochondria/metabolism , Mitochondrial Membrane Transport Proteins/metabolism , Mitochondrial Membranes/metabolism , Mitochondrial Proteins/metabolism , Molecular Chaperones , Oxidoreductases Acting on Sulfur Group Donors/metabolism , Protein Transport/genetics , Saccharomyces cerevisiae Proteins/metabolism , Saccharomyces cerevisiae/metabolism , Signal Transduction/genetics , Cysteine/chemistry , Cysteine/metabolism , Cytosol/metabolism , Disulfides/metabolism , Gene Expression Regulation, Fungal , Mitochondria/genetics , Mitochondrial Membrane Transport Proteins/genetics , Mitochondrial Precursor Protein Import Complex Proteins , Mitochondrial Proteins/genetics , Models, Molecular , Molecular Chaperones/chemistry , Molecular Chaperones/genetics , Molecular Chaperones/metabolism , Mutation , Oxidation-Reduction , Oxidoreductases Acting on Sulfur Group Donors/genetics , Plasmids , Protein Folding , Protein Interaction Domains and Motifs , Saccharomyces cerevisiae/genetics , Saccharomyces cerevisiae Proteins/chemistry , Saccharomyces cerevisiae Proteins/genetics , Superoxide Dismutase/genetics , Superoxide Dismutase/metabolism , Superoxide Dismutase-1 , Transduction, Genetic
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