Esophageal mucosal resection versus esophagectomy: a comparative study of surgical results in patients with advanced megaesophagus / Mucosectomia esofágica versus esofagectomia: estudo comparativo dos resultados cirúrgicos imediatos e tardios em pacientes operados por megaesôfago avançado

BACKGROUND: The surgical treatment of advanced megaesophagus has no consensus, being esophagectomy the more commonly used method. Since it has high morbimortality - inconvenient for benign disease -, in recent years an alternative has been introduced: the esophageal mucosal resection. AIM: To compare early and late results of the two techniques evaluating the operative time, length of ICU stay; postoperative hospitalization; total hospitalization; intra- and postoperative complication rates; mortality; and long-term results. METHODS: Were evaluated retrospectively 40 charts, 23 esophagectomies and 17 mucosectomies. In assessing postoperative results, interviews were conducted by using a specific questionnaire. RESULTS: Comparing the means of esophagectomy and mucosal resection, respectively, the data were: 1) surgical time - 310.2 min and 279.7 min (p> 0.05); 2) length of stay in ICU - 5 days and 2.53 days (p <0.05); 3) total time of hospitalization - 24.25 days and 20.76 days (p> 0.05); 4) length of hospital stay after surgery - 19.05 days and 14.94 days (p> 0.05); 5) presence of intraoperative complications - 65% and 18% (p <0.05); 6) the presence of postoperative complications - 65% and 35% (p> 0.05). In the assessment of late postoperative score (range 0-10) esophagectomy (n = 5) obtained 8.8 points and 8.8 points also got mucosal resection (n = 5). CONCLUSIONS: Esophageal mucosal resection proved to be good alternative for surgical treatment of megaesophagus. It was advantageous in the immediate postoperative period by presenting a lower average time in operation, the total hospitalization, ICU staying and complications rate. In the late postoperative period, the result was excellent and good in both operations. .

RACIONAL: O tratamento cirúrgico do megaesôfago avançado não é consensual sendo mais comumente usada a esofagectomia. Por tratar-se de técnica que apresenta maior morbimortalidade e empregada em doença benigna, foi introduzida nos últimos anos, como alternativa, a mucosectomia esofágica. OBJETIVO: Comparar os resultados imediatos e tardios das duas técnicas avaliando-se os tempos operatório, de internação em UTI, de internação do pós-operatório, de internação total; taxas de complicações intra-operatórias e pós-operatórias; taxa de mortalidade; e resultados a longo prazo. MÉTODOS: Foram avaliados 40 prontuários, retrospectivamente, sendo 23 esofagectomias e 17 mucosectomias. Na avaliação dos resultados pós-operatórios, foram realizadas entrevistas, mediante uso de questionário específico. RESULTADOS: Comparando-se as médias da esofagectomia e mucosectomia, respectivamente, os dados foram: 1) tempo cirúrgico - 310,2 min e 279,7 min (p>0,05); 2) tempo de internação em UTI - 5 dias e 2,53 dias (p<0,05); 3) tempo de internação total - 24,25 dias e 20,76 dias (p>0,05); 4) tempo de internação após a operação - 19,05 dias e 14,94 dias (p>0,05); 5) presença de complicações intra-operatórias - 65% e 18% (p<0,05); 6) presença de complicações pós-operatórias imediatas - 65% e 35% (p>0,05). Na avaliação do escore pós-operatório tardio (escala 0-10) a esofagectomia (n=5) obteve 8,8 pontos e também 8,8 pontos obteve a mucosectomia (n=5). CONCLUSÕES: A mucosectomia esofágica mostrou-se boa alternativa no tratamento cirúrgico do megaesôfago avançado. Foi vantajosa no pós-operatório imediato por apresentar menor média de tempo na operação, na internação total, na UTI e no índice de complicações. No pós-operatório tardio, o resultado foi excelente e bom nas duas operações. .

Cleavage of purified neuronal clathrin assembly protein (CALM) by caspase 3 and calpain

The most efficient means of protein internalization from the membrane are through clathrin-coated pits, which concentrate protein interactions with the clathrin-associated assembly protein complex AP-2 and internalization signals in the cytoplasmic domain of transmembrane proteins. Binding of clathrin assembly protein to clathrin triskelia induces their assembly into clathrin-coated vesicles (CCVs). Due to a difficulty of isolating clathrin molecules from their complex or assembly state in the cells, most of the studies were carried out with recombinant clathrin proteins, which may present different conformation and structural variation. In this study, we have developed an efficient method of isolating the native clathrin assembly protein lymphoid myeloid (CALM) from the bovine brain that is enriched with clathrin and clathrin associated proteins and characterized by their sensitivity to proteases and it's ability to form CCV. The purified CALM has molecular weight of approximately 100,000 dalton on SDS-PAGE, which is consistent with the result of in vitro translation. The purified CALM protein could promote the assembly of clathrin triskelia into clathrin cage, and cleaved CALM proteolysed by caspase 3 and calpain could not promote them. In this respect, our data support a model in which CALM functions like AP180 as a monomeric clathrin assembly protein and might take part in apoptotic process in neuronal cells.

Cleavage of purified neuronal clathrin assembly protein (CALM) by caspase 3 and calpain

The most efficient means of protein internalization from the membrane are through clathrin-coated pits, which concentrate protein interactions with the clathrin-associated assembly protein complex AP-2 and internalization signals in the cytoplasmic domain of transmembrane proteins. Binding of clathrin assembly protein to clathrin triskelia induces their assembly into clathrin-coated vesicles (CCVs). Due to a difficulty of isolating clathrin molecules from their complex or assembly state in the cells, most of the studies were carried out with recombinant clathrin proteins, which may present different conformation and structural variation. In this study, we have developed an efficient method of isolating the native clathrin assembly protein lymphoid myeloid (CALM) from the bovine brain that is enriched with clathrin and clathrin associated proteins and characterized by their sensitivity to proteases and it's ability to form CCV. The purified CALM has molecular weight of approximately 100,000 dalton on SDS-PAGE, which is consistent with the result of in vitro translation. The purified CALM protein could promote the assembly of clathrin triskelia into clathrin cage, and cleaved CALM proteolysed by caspase 3 and calpain could not promote them. In this respect, our data support a model in which CALM functions like AP180 as a monomeric clathrin assembly protein and might take part in apoptotic process in neuronal cells.

Purification of clathrin assembly protein from rat liver

Recently, the gene encoding clathrin assembly protein of lymphoid myeloid leukemia (CALM), which is homologous to the AP180, was cloned from rat brain, and its expression differential to AP180 was reported (Kim and Lee, 1999). This gene product promotes the polymerization of clathrin into clathrin cage and found to be a regulator in membrane trafficking between intracellular compartments in eukaryotic cells (Kim et al., 2000). In this study, we have purified the CALM protein from clathrin-coated vesicles of rat liver using the monoclonal antibody against the recombinant N-terminal region of the CALM. The coated proteins extracted from the coated vesicle fraction was further purified by multi-step procedures involving gel-filtration and ion-exchange chromatography and SDS-PAGE. The purified protein with an apparent molecular weight of 100 kD promoted the assembly of clathrin triskelia into clathrin cage. In this respect the CALM protein bears a functional resemblance to the AP180 that has been previously described.