1.Management of Persistent Cerebrospinal Fluid Leakage Following Thoraco-lumbar Surgery.
Bilgehan TOSUN ; Konuralp ILBAY ; Michael Sun Min KIM ; Ozgur SELEK
Asian Spine Journal 2012;6(3):157-162
STUDY DESIGN: This was a retrospective study of patients who had developed a dural tear after thoracic and lumbar spine surgery that was not recognized during the surgery, and was treated either by lumbar drainage or over-sewing of the wounds. PURPOSE: To revisit the treatment strategies in postoperative dural leaks and present our experience with over-sewing of the wound and lumbar drainage. OVERVIEW OF LITERATURE: Unintended durotomy is a frequent complication of spinal surgery. Management of subsequent cerebrospinal fluid leakage remains controversial. There is no distinct treatment guideline according to the etiology in the current literature. METHODS: The records of 368 consecutive patients who underwent thoracic and/or lumbar spine surgery from 2006 throug h 2010 were retrospectively reviewed. Seven cerebrospinal fluid fistulas and five pseudomeningoceles were noted in 12 (3.2%) procedures. Cerebrospinal fluid diversion by lumbar drainage in five pseudomeningoceles and over-sewing of wounds in seven cerebrospinal fluid fistulas employed in 12 patients. Clinical grading was evaluated by Wang. RESULTS: Of the 12 patients who had a dural tear, 5 were managed successfully with lumbar drainage, and 7 with oversewing of the wound. The clinical outcomes were excellent in 9 patients, good in 2, and poor in 1. Complications such as neurological deficits, or superficial or deep wound infections did not develop. A recurrence of the fistula or pseudomeningocele after the treatment was not seen in any of our patients. CONCLUSIONS: Pseudomeningoceles respond well to lumbar drainage, whereas over-sewing of the wound is an alternative treatment option in cerebrospinal fluid fistulas without neurological compromise.
Drainage
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Fistula
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Humans
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Recurrence
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Retrospective Studies
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Spine
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Wound Healing
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Wound Infection
2.Amplification of distinct α-synuclein fibril conformers through protein misfolding cyclic amplification.
Byung Chul JUNG ; Yoon Ju LIM ; Eun Jin BAE ; Jun Sung LEE ; Min Sun CHOI ; Michael K LEE ; He Jin LEE ; Yoon Suk KIM ; Seung Jae LEE
Experimental & Molecular Medicine 2017;49(4):e314-
Amyloid fibril formation has been implicated in the pathogenesis of neurodegenerative diseases. Fibrillation generates numerous conformers. Presumably, the conformers may possess specific biological properties, thus providing a biochemical framework for strains of prions. However, the precise relationship between various fibril conformers and their pathogenic functions has not been determined because of limited accessibility to adequate amounts of fibrils from tissue samples. α-Synuclein is one such protein, and it has been implicated in Parkinson disease. Using a technique known as protein misfolding cyclic amplification, originally developed for amplifying prions, we established a procedure through which the amplification of α-synuclein fibrils is possible. With a trace amount of seeds, we succeeded in amplifying α-synuclein fibrils. The replication of the seeds was faithful in terms of conformation even after multiple rounds of cyclic amplification. Moreover, two transgenic mouse strains each representing a distinct synucleinopathy were used to investigate different conformers by using this technique. The amplified α-synuclein fibrils derived from the tissue extracts of these two strains led to the production of two different fibril conformers with distinct proteinase K digestion profiles. Together, our results demonstrated that a trace amount of α-synuclein fibrils in tissue extracts could be amplified with their conformations conserved. This procedure should be useful in amplifying α-synuclein fibrils from the brains and body fluids of patients afflicted with synucleinopathies and may serve as a potential diagnostic tool for Parkinson disease and other synucleinopathies.
Amyloid
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Animals
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Body Fluids
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Brain
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Digestion
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Endopeptidase K
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Humans
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Mice
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Mice, Transgenic
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Neurodegenerative Diseases
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Parkinson Disease
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Prions
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Tissue Extracts