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Mechanical Thrombectomy for Large Vessel Occlusion via the Transbrachial Approach: Case Series
Tsuji Yuichiro,Miki Takanori,Kakita Hiroto,Sato Kimitoshi,Yoshida Takashi,Shimizu Fuminori 대한신경중재치료의학회 2020 Neurointervention Vol.15 No.2
Mechanical thrombectomy has become a standard treatment for acute ischemic stroke with large vessel occlusion. In aged patients, it is difficult to guide the catheter via the transfemoral approach due to vessel tortuosity and aortic elongation. We report our preliminary clinical experience using the transbrachial approach. Among the 119 patients who underwent thrombectomy from April 2018 to December 2019, a total of 5 patients were treated via the transbrachial approach. Clinical outcomes were retrospectively analyzed. Successful reperfusion was achieved in 4 out of 5 cases. There was 1 death due to symptomatic intracranial hemorrhage. One patient had a good outcome at discharge. There were no access-site complications associated with any of these cases. Transbrachial access for mechanical thrombectomy is feasible and can provide an alternative to the transfemoral approach.
Murine doc-1 cDNA Cloning, Sequencing and Expression in Normal Adult Tissues
Kim, Young,Tsuji, Takanori,Elovic, Aram,Shintani, Satoru,Mihara, Mariko,Salih, Erdjan,Kohno, Yohko,Chin, Byung-Rho,Patel, Vipul,Wong, David,Todd, Randy Korean Academy of Oral Biology and the UCLA Dental 2001 International Journal of Oral Biology Vol.26 No.3
Human Deleted in Oral Cancer-1 (DOC-1) is a 115-amino acid polypeptide (p12^DOC-1) that is widely expressed in normal adult tissues but markedly reduced or absent in oral squamous cell carcinomas. We isolated the murine doc-1 cDNA homologue from NIH3T3 cells using PCR and 3'RACE. Sequence analysis confirms an open reading frame of 114 amino acids, with a 100% and 98% homology with hamster p12^doc-1 and human p12^doc-1 respectively. Gene expression and cellular localization of doc-1 were demonstrated using northern analysis and in situ hybridization using several adult mouse tissues. The murine p12^doc-1 peptide sequence was confirmed using protein from mouse liver extract purified by a cation exchange column and fractionated by reverse-phase HPLC. Western analysis was performed to verify the presence of p12^doc-1 in adult murine tissues. The production and cellular localization of p12^doc-1 were confirmed by western analysis and immunohistochemistry in corresponding tissues. This is the first study to examine the cellular localization of doc-1 mPNA and p12^doc-1.