Extralesional cryotherapy combined with intralesional triamcinolone injections after keloid excision

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Use of Topical Rapamycin as Maintenance Treatment after a Single Session of Fractionated CO2 Laser Ablation: A Method to Enhance Percutaneous Drug Delivery

Tuberous sclerosis complex (TSC) is an autosomal dominant neurocutaneous disorder with an incidence of approximately 1 in 5,000 to 10,000 live births. TSC has various clinical manifestations such as multiple hamartomas in systemic organs, including the skin. Angiofibromas are the most common skin lesions in patients with TSC. Although benign, angiofibromas develop in childhood and puberty, and can be psychosocially disfiguring for patients. Skin lesions in TSC, specifically angiofibromas, have no significant risk of malignant transformation after puberty; thus, they require no treatment if not prominent. However, the presentation of TSC is important owing to its impact on patient cosmesis. Surgical treatment and laser therapy are the mainstream treatments for angiofibromas. Although the evidence is limited, topical mammalian target of rapamycin inhibitors such as sirolimus (rapamycin) are effective in facial angiofibroma treatment. We describe an adult patient with an angiofibroma who had an excellent response to treatment with topical rapamycin after a single session of carbon dioxide (CO2) laser ablation. The patient showed no sign of relapse or recurring lesions for a year. CO2 laser ablation may serve as a new paradigm of treatment for angiofibromas in TSC. Since the selection of laser devices can be limited for some institutions, we suggest a rather basic but highly effective approach for angiofibroma treatment that can be generally applied with the classic CO2 device.ope

Dual cortical tunneling method for endoscopic forehead lift

Background Endoscopic forehead lift with cortical tunneling is an effective option for rejuvenation of the upper third of the face. Although it has been considered safe and reliable, with relatively consistent long-term results, relapse and weakening of adhesion have been common problems. Methods We suggest the dual-tunneling method for overcoming these limitations. A total of 100 patients aged 17 to 65 years underwent forehead lifting with cortical tunneling by the senior author from August 2016 to December 2017. The single-tunnel method was applied in one half of the patients and the dual-tunnel method in the other half. Bilateral brow positions were measured immediately following surgery and 6 months later. Results For all cases, cortical tunneling was done at the central incision and both paramedian incisions; therefore, three tunnels were used in the control group and six tunnels in the experimental group. In the single-tunnel group, relapse distances were 2.39±0.83 mm for the medial brow and 3.26±0.91 mm for the lateral brow (6 months postoperatively; n=100). The dual-tunnel group showed significantly smaller (P<0.001) relapse distances, with values of 1.69±0.46 mm and 2.17±0.59 mm for the medial and lateral brow, respectively (6 months postoperatively; n=100). The experimental group did not show an increase in complications. Conclusions The dual-tunneling method, designed to minimize the cheese-wiring effect, uses a triangular plane to avoid a focal fixation. The fixation also includes the periosteum to hold the forehead tissue in place, inducing stronger adhesion.ope

Robotic Microsurgery Training for Robot Assisted Reconstructive Surgery

Purpose: Recent advances in robotic surgery have affected not only surgery for visceral organs but also head and neck cancer surgery and microsurgery. The authors intended to analyze and share experience gained from performing microanastomosis training in a new robotic surgery system. Methods: Robotic microanastomosis training was performed using Da Vinci Xi. The robot arm used two black diamond forceps, one Potts scissor, and one vision camera. First, basic robotic surgery skills were trained with Da Vinci Skill Simulator training. Actual microanastomosis practice was performed using artificial blood vessel, chicken wing and porcine leg. Results: Three simulation training sessions were performed and five vessel anastomosis were performed. A total of 8 vascular anastomosis were performed, and anastomosis for one vessel took 31-57 minutes. The number of sutures used was more than one initially due to suture material damage, but one suture was used after four anastomosis. In the anastomosis time analysis with porcine legs, the actual anastomosis process took 2 minutes 15 seconds±41 seconds per stitch. The vascular anastomosis interval took more time than vascular anastomosis itself due to robot arm change and camera movement. Conclusion: Robotic microsurgery training was not difficult process for surgeons who had undergone conventional microsurgery. However, more training was needed to replace the robot arm and move the camera. In the long term, mechanical improvements in diamond forceps and camera resolution were necessary. In order to master robotic microsurgery, surgeons must get used to robotic surgery system through simulation training.ope

Effective botulinum toxin injection point for treatment of headache

치과대학/박사The underlying causes of migraine are often nerve and muscle disorders, which has led to botulinum toxin type A (BoNT-A) injection gaining traction as a viable treatment option. However, previous injection sites on the temporalis muscle for treating migraine were determined by observing the trigger point of migraines, and it is unsure whether these are the most anatomically effective sites for injection (Whitcup et al., 2014). This study performed an extensive analysis of published research on the morphology of the temporalis muscle in order to provide an anatomical guideline on how to distinguish the temporalis muscle and temporalis tendon by observing the surface of the patient’s face. Furthermore, it was found that Sihler’s staining could be applied to the temporalis muscle in order to identify accurate and effective BoNT-A injection sites for treating migraines. Twenty-one hemifaces of cadavers (16 males, 5 females; mean age, 81.0 years; age range, 63？93 years) were used in this study. The experiment was divided into two steps: (1) morphologically analyzing the temporalis region of the cadavers and (2) applying Sihler’s staining to the temporalis muscle and tendon. The posterior border of the temporalis tendon was classified into three types according to its location relative to five reference lines: in Type I the posterior border of the temporalis tendon is located in front of reference line L2 (4.8%, 1/21), in Type Ⅱ it is located between reference lines L2 and L3 (85.7%, 18/21), and in Type Ⅲ it is located between reference lines L3 and L4 (9.5%, 2/21). The vertical distances between the horizontal line passing through the jugale (LH) and the temporalis tendon along each of reference lines L0, L1, L2, L3, and L4 were 29.74±6.87 mm (mean±SD), 45.06±8.84 mm, 37.76±11.18 mm, 42.50±7.59 mm, and 32.14±0.47 mm, respectively; the corresponding vertical distances between LH and the temporalis muscle were 55.02±8.25 mm, 74.99±9.90 mm, 73.97±10.12 mm, 55.24±13.25 mm, and 47.56±11.41 mm. Sihler’s staining shows that the anterior and posterior branches of the deep temporal nerve run through the anterior and posterior fibers of the temporalis muscle, respectively. BoNT-A should be injected into the temporalis muscle at least 45 mm vertically above the zygomatic arch. This will ensure that the muscle region is targeted and so produce the greatest clinical effect with the minimum concentration of BoNT-A. In order to easily identify the temporalis muscle in a clinical setting, the second finger should be placed on the bottom corner of the zygomatic arch; the tip of the thumb will then be located 45 mm from the zygomatic arch.ope

새로운 프로테아좀 조절 단백질에 관한 연구

학위논문 (박사)-- 서울대학교 대학원 : 생명과학부, 2015. 8. 정용근.The proteasome is a large protein complex that degrades diverse proteins in ubiquitine-proteasome system (UPS). Numerous substrates which play roles in many signaling to maintain homeostasis are known to be degraded by the complicated degradation processes. In addition, aberrant regulation in UPS and of this complex is associated with various diseases such as cancer, disorder of immune response and neurodegenerative disease. However, it is not known whether and how this elaborate machinery is regulated by diverse cellular signaling. Thus, discovery of novel proteasome regulators is important to understand UPS-associated cellular function and the pathogenesis of various diseases related to proteasome malfunction. To identify new proteasome modulators regulating the proteasome activity, a cell-based functional screening was established using Degron-GFP and a collection of cDNA library. In this study, I have isolated iRhom1 as a stimulator of proteasome activity from genome-wide functional screening using cDNA expression and an unstable GFP-degron. Expression level of iRhom1 regulated enzymatic activity and assembly of proteasome complexes. iRhom1 expression was induced by endoplasmic reticulum (ER) stressors, leading to the enhancement of proteasome activity, especially in ER-containing microsomes. iRhom1 interacted with PAC1 and PAC2, the 20S proteasome assembly chaperones, affecting their protein stability by dimerization of them. In addition, iRhom1 deficiency in D. melanogaster accelerated the rough-eye phenotype of mutant Huntingtin, while transgenic flies expressing either human iRhom1 or Drosophila iRhom showed rescue of the rough-eye phenotype. S5b was previously identified as a proteasome-assembly chaperone in yeast and a negative regulator of 26S proteasome in mammalian. Although regulation of GRK2 is considered as one of cell death mediators in neuronal cells, the regulation of GRK2 expression is not known. Here, I show that GRK2 is regulated by S5b in neuronal cells and mouse model. GRK2 is down-regulated in the cortex and hippocampus of S5b transgenic mice, a chronic inflammation model and also reduced by S5b expression in HT22 mouse hippocampal cells. Conversely, knockdown of S5b expression increases GRK2 level through increasing the stability of GRK2 protein, independent of its ability to impair proteasome activity. GRK2 and GRK2 K220R, a kinase dead mutant, similarly interacts with S5b in the mouse cortex and HT22 cells through its C-terminal domain, and this domain also decreases GRK2 level. Membrane targeting of GRK2 is affected by S5b expression, as assessed with immunocytochemistry, fractionation, and surface biotinylation assays. In addition, neurotoxic effect of S5b is suppressed by overexpression of GRK2 but not by GRK2 K220R. Thus, S5b may exert its toxic effect through down-regulation of GRK2, a neurotoxic mediator, in neuronal cells, showing an aberrant role of S5b as a negative regulator of GRK2 in neuronal cell death. In addition, Psmd5/S5b knockout mouse was successfully generated by the Cas9/CRISPR-mediated Psmd5/S5b knockout cassette and show enhanced proteasome activity compared to aged matched littermates. Together, S5b plays a diverse role in the regulation of proteasome activity under pathologic condition and in neuronal cell death through GRK2. In conclusion, I suggest a novel stress signaling pathway responsible for proteasome regulation and critical role of S5b in neuronal cell death independent of its inhibitory function of proteasome.ABSTRACT. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .i CONTENTS. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .v LIST OF FIGURES AND TABLES. . . . . . . . . . . . . .ix ABBREVIATIONS. . . . . . . . . . . . . . . . . . . . . . . . . . . .xiii CHAPTER I. iRhom1 regulates proteasome activity via PAC 1/2 under ER stress I-1. Abstract. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .2 I-2. Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . .3 I-3. Materials and Methods . . . . . . . . . . . . . . .6 Cell culture and transfection. . . . . . . . . . . . . . . . . . . . . .6 Generation of stable cell line. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .6 Genome-wide functional screening. . . . . . . . . . . . . . . . . . . . . .6 Plasmid construction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .7 Antibodies and western blotting. . . . . . . . . . . . . . . . . . . . . . . . .7 Assays for proteasome activities. . . . . .. . . . . . . . . . . . . . . . . . . . . .8 Reverse transcriptase-PCR . . . . . . . . . . . . . . . . . . .8 Subcellular fractionation. . . . . . . . . . . . . . . . . . . . . . . . . .9 Glycerol gradient analysis. . . . . . . . . . . . . . . . . . . . . . . . . . . . . .10 Immunoprecipitation assay. . . . . . . . . . . . . . . . . . . . . . . . . . . .10 Immunocytochemistry . . . . . . . . . . . . . . . . . . . . . . . . . . . . .11 Native gel analysis. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .11 Filter trap assay. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .12 Drosophila genetics. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .12 I-4. RESULTS. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .13 iRhom1 isolated by functional screening enhances proteasome activity . . . . . . . . . . . . . . . . . . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. . . .13 iRhom1 affects the assembly of proteasome complexes. . . . . .. . . .15 iRhom1 regulates microsomal proteasome activity in response to ER stress. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .16 iRhom1 increases protein stability and dimerization of PAC1 and PAC2 . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .19 iRhom1 relieves mutant Huntingtin aggregation in cells and Drosophila . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .20 I-5. DISCUSSION. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .77 I-6. REFERENCES. . . . . . . . . . . . . . . . . . . . . . . . . . . . . .82 CHAPTER II. S5b induces neuronal cell death via downregulation of GRK2 II-1. Abstract . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .94 II-2. Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . .96 II-3. Materials and Methods . . . . . . . . . . . . . . .98 Antibodies and sh- or si- RNA construction . . . . . . . . . . . . . . . . .98 Cell Culture and DNA Transfection . . . . . . . . . . . . . . . . . . . . . . . .98 SDS-PAGE and Immunoblot Analysis. . . . . . . . . . . . . . . . . . . . . .98 Immunoprecipitation and Immunohistochemisty . . . . . . . . . . . .99 Subcellular Fractionation . . . . . . . . . . . . . . . . . . . . . . . . . . . 99 Biotinylation assay . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 100 II-4. RESULTS. . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 101 GRK2 level is regulated by S5b in HT22 cells and the brain of S5b transgenic mice. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .101 S5b interacts with GRK2 through its C-terminus. . . . . . . . . . . . . . 102 S5b impairs the targeting of GRK2 to the plasma membrane. . . . . .103 S5b affects neuronal cell death probably via down-regulation of GRK2 . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .105 Generation of Psmd5/S5b knockout mice with enhanced proteasome Activity . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .105 II-5. DISCUSSION . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .130 II-6. REFERENCES . . . . . . . . . . . . . . . . . . . . . . . . . . . . .135 ABSTRACT IN KOREAN/국문 초록. . . . . . . . . . .143 LIST OF FIGURES Figure I-1. Stimulatory effect of iRhom1 overexpression on proteasome activity . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .23 Figure I-2. Ectopic expression of iRhom1 reduces degron (GFPU) and elevates proteasome catalytic activity . . . . . . . . . . . . . . . . . . . . . .25 Figure I-3. Effects of cDNAs encoding polytopic membrane proteins on proteasome activity . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .27 Figure I-4. Downregulation of iRhom1 reduces proteasome activity and increases the accumulation of ubiquitin-conjugates. . . . . . . . . .29 Figure I-5. Ectopic expression of iRhom1 increases catalytic activity of proteasome and reduces ub-conjugation . . . . . . . . . . . . . . . . . . ...31 Figure I-6. Ectopic expression of iRhom1 increases proteasome assembly in native gel and reduces MG132 induced ub-conjugation. . . . . . .33 Figure I-7. Overexpression effects of the Rhomboid protein family and their activity-dead mutants on proteasome activity. . . . . . . . . . . . . . . .35 Figure I-8. iRhom1 does not affect RNA or protein levels of proteasome subunit . . . . . . . . . . . . . . . . . . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .37 Figure I-9. Downregulation of iRhom1 impairs the assembly of proteasome complexes by native gel analysis. . . . . . . . . . . . . . . . . . . . . .39 Figure I-10. Knockdown of iRhom1 expression impairs the assembly of proteasome complexes in a fractionation assay . . . . . . . . . . . . .41 Figure I-11. Ectopic expression of iRhom1 does not increase protein levels of proteasome subunit but only elevates proteasome activity in fractionation assays . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .43 Figure I-12. iRhom1 localizes in the ER of HeLa and HEK293T cells. . . . ...45 Figure I-13. iRhom1 regulates proteasome activity in the microsomal fractions. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .47 Figure I-14. iRhom1 regulates proteasome assembly in the microsomal Fractions. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .49 Figure I-15. iRhom1 is increased by ER stress . . . . . . . . . . . . . . . . . . . . . . . . . .51 Figure I-16. Increase in iRhom1 expression by stress signals . . . . . . .53 Figure I-17. Knockdown of iRhom1 expression impairs ER stress-induced activation and assembly of proteasomes in the microsomal fraction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . ..55 Figure I-18. The amounts of PAC1 and PAC2 proteins are decreased by iRhom1-knockdown . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .57 Figure I-19. iRhom1 enhances the stability of PAC1 protein. . . . . . . . . . . . . .59 Figure I-20. iRhom1 regulates the stability of PAC1 and PAC2 proteins. . . .61 Figure I-21. iRhom1 affects the interaction between PAC1 and PAC2. . . . . .63 Figure I-22. ER stress increases PAC1/PAC2 dimerization in an iRhom1- dependent manner. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .65 Figure I-23. Expression level of iRhom1 modulates the aggregation of mutant Huntingtin in cells. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .67 Figure I-24. Ectopic expression of PAC1 and PAC2 elevates proteasome Activity. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .69 Figure I-25. Expression level of iRhom1 modulates the aggregation of the rough-eye phenotype in a fly model expressing Htt120Q. . . . .71 Figure I-26. Overexpression of drosophila iRhom or human iRhom1 in drosophila eye shows mild disturbance in eye development and increases proteasome activity. . . . . . . . . . . . . . . . . . . . . . . . . . . .73 Figure I-27. Schematic diagram showing the proposed role of iRhom1 in proteasome activation under ER stress. . . . . . . . . . . . . . . . . . . . .75 Figure II-1. S5b overexpression downregulates GRK2 in the cortex and hippocampus. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .107 Figure II-2. Ectopic expression level of S5b reduces GRK2. . . . . . . . . . . . . .109 Figure II-3. Knockdown of S5b expression increases GRK2 at post- translational level. . . . . . . . . . . . . . . . . . . . . . . . . . . . .111 Figure II-4. S5b interacts with GRK2 via S5b C-terminal domain. . . . . . . 113 Figure II-5. Regulation in the translocation of GRK2 from cytosol to plasma membrane by S5b expression. . . . . . . . . . . . . . . . . . . . . . . . . .115 Figure II-6. S5b recruits membrane GRK2 into cytosol. . . . . . . . . . . . . . . . . .117 Figure II-7. Ectopic expression of S5b induces apoptosis in HT22 cell line . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. . . . . . . 119 Figure II-8. GRK2 activation suppresses S5b overexpression induced cell death . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 121 Figure II-9 Generation of PSMD5/S5b knockout mice . . . . . . . . . . . . . . . . .123 Figure II-10. S5b expression levels were determined in th tissue of WT and PSMD5/S5b deficient mouse . . . . . . . . . . . . . . . . . . . . . . . . . . .125 Figure II-11. Elevated proteasome activity in S5b knockout mouse . . . . . 127 Figure II-12. Proposed model for the role of GRK2 in S5b-mediated neuronal cell death . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 129Docto

Selection of Varoius Free Flap Donor Sites in Palatomaxillary Reconstruction

PURPOSE : A palatal defect following maxillectomy can cause multiple problems like the rhinolalia, leakage of foods into the nasal cavity, and hypernasality. Use of a prosthetic is the preferred method for obturating a palate defect, but for rehabilitating palatal function, prosthetics have many shortcomings. In a small defect, local flap is a useful method, however, the size of flap which can be elevated is limited. In 12 cases of palatomaxillary defect, we used various microvascular free flaps in reconstructing the palate and obtained good functional results. METHOD : Between 1990 and 2004, 12 patients underwent free flap operation after head and neck cancer ablation, and were reviewed retrospectively. Among the 12 free flaps, 6 were latissimus dorsi myocutaneous flaps, 3 rectus abdominis myocutaneous flaps, and 3 radial forearm flaps. RESULT : All microvascular flap surgery was successful. Mean follow up time was 8 months and after the follow up time all patients reported satisfactory speech and swallowing. Wound dehiscence was observed in 4 cases, ptosis was in 1 case and fistula was in 1 case, however, rhinolalia, leakage of food, or swallowing difficultly was not reported in the 12 cases. CONCLUSION : We used various microvascular flaps for palatomaxillary reconstruction. For 3-dimensional flap needs, we used the latissimus dorsi myocutaneous flap to obtain enough volume for filling the defect. Two-dimensional flaps were designed with latissimus dorsi myocutaneous flap, rectus abdominis flap and radial forearm flap. For cases with palatal defect only, we used the radial forearm flap. In palatomaxillary reconstruction, we can choose various free flap techniques according to the number of skin paddles and flap volume needed.ope

Research, Plastic Surgery, and Archives of Plastic Surgery

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청년세대 격차문제와 새로운 정책패러다임의 필요성

20대 청년세대를 바라보는 한국사회의 시선은 동정과 희망의 두 단어로 요약된다. 우선 동정은 세대 전체를 불쌍한 시대를 맞아 억압받고 고통받는 사람들로 규정하는 시선이다. 취업, 결혼, 출산을 포기했다는 삼포 세대론은 이런 시선을 대표한다. 그리고 희망은 막연하게 청년이 일어서야 나라가 일어선다는 류의 시선이다. 정책적으로 말하자면 새로운 노동력으로 보며 이 노동력으로부터 새로운 생산이 더 많이 일어나야 한국경제가 동력을 받을 수 있다는 시선이기도 하다. 과장된 청년창업진흥정책이 이런 맥락에서 나온다. 이 두 시선 모두 청년과 청년 아닌 사람들로 사회를 나누고 청년 아닌 사람들의 시선으로 청년을 바라보는 관점이다. 하지만 실제로 이 세대가 미래 한국사회의 특성을 보여줄 세대라고 생각한다면, 이 세대 자체의 특성을 잘 파악하고 그에 맞는 사회시스템을 디자인할 필요가 있다. 즉 문제를 세대 간 갈등 또는 연대의 문제로 이해하는 것이 아니라, 미래에 사회의 지배적 다수가 될 세대로 규정하고 바라보는 시각도 필요하다는 것이다. 그러려면 우선 지금 한국사회가 어디에 서 있는지 살펴봐야 하고, 청년세대가 어떤 특성을 갖고 있는지도 따져봐야 하며, 한국사회 특성과 청년세대가 잘 맞을지를 살펴보고, 맞지 않다면 현재 청년 세대의 특성에 맞는 사회패러다임은 어떤 것인지를 설계하고 구현해 가야 한다. 이 글에서는 토마 피케티가 『21세기 자본론(Le Capital au XXIe siècle)』에서 제시한 세습자본주의 개념을 중심으로 한국사회의 특성과 청년세대 특서ᅟᅧᆼ에 맞는 새로운 사회패러다임을 개념적 수준에서 제시하고자 한다

Reconstruction of Ankle and Heel Defects with Peroneal Artery Perforator-Based Pedicled Flaps

BACKGROUND: The reconstruction of ankle and heel defects remains a significant problem for plastic surgeons. The following options exist for reconstructing such defects: local random flaps, reverse flow island flaps, and free flaps. However, each of these methods has certain drawbacks. Peroneal artery perforators have many advantages; in particular, they are predictable and reliable for ankle and heel reconstructions. In this study, we report our clinical experience with peroneal artery perforator-based pedicled flaps in ankle and heel reconstructions. METHODS: From July 2005 to October 2012, 12 patients underwent the reconstruction of soft tissue defects in the ankle and heel using a peroneal artery perforator-based pedicled flap. These 12 cases were classified according to the anatomical area involved. The cause of the wound, comorbidities, flap size, operative results, and complications were analyzed through retrospective chart review. RESULTS: The mean age of the patients was 52.4 years. The size of the flaps ranged from 5×4 to 20×8 cm(2). The defects were classified into two groups based on whether they occurred in the Achilles tendon (n=9) or heel pad (n=3). In all 12 patients, complete flap survival was achieved without significant complications; however, two patients experienced minor wound dehiscence. Nevertheless, these wounds healed in response to subsequent debridement and conservative management. No patient had any functional deficits of the lower extremities. CONCLUSIONS: Peroneal artery perforator-based pedicled flaps were found to be a useful option for the reconstruction of soft tissue defects of the ankle and heel.ope