Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
1.
J Endourol ; 28(2): 208-13, 2014 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-24044423

RESUMO

OBJECTIVE: Robot-assisted radical prostatectomy (RARP) is a minimally invasive alternative to open retropubic radical prostatectomy (RP), and is reported to offer equivalent oncologic outcomes while reducing perioperative morbidity. However, the technique of extirpation can differ based on the usage of thermal energy and coagulation during RARP, which may alter the risk of finding a positive surgical margin (PSM) as cautery may destroy residual cancer cells. We sought to evaluate whether the method of surgery (RP vs RARP) affects the rate of biochemical recurrence (BCR) in patients with PSMs. MATERIALS & METHODS: The Columbia University Urologic Oncology Database was reviewed to identify patients who underwent RP and RARP from 2000 to 2010 and had a PSM on final pathology. BCR was defined as a postoperative prostate-specific antigen (PSA) ≥0.2 ng/mL. The Kaplan-Meier analysis was utilized to calculate BCR rates based on the method of surgery. Cox regression analysis was performed to determine if the method of surgery was associated with BCR. RESULTS: We identified 3267 patients who underwent prostatectomy, of which 910 (28%) had a PSM. Of those with a PSM, 337 patients had available follow-up data, including 229 who underwent RP (68%) and 108 who underwent RARP (32%). At a mean follow-up time of 37 months for the RP group, 103 (46%) patients demonstrated BCR; at a mean follow-up time of 44 months for the RARP group, 62 (57%) patients had a BCR (p=0.140). Two-year BCR-free rates for RP vs RARP were 65% and 49%, respectively (log-rank p<0.001). However, after controlling for age, PSA, grade, and year of surgery, the surgical method was not significantly associated with increased risk of BCR (HR 1.25; p=0.29). CONCLUSION: Our results confirm the noninferiority of RARP to RP with regard to patients with PSMs. As such, all patients with a PSM at RP are at high risk for BCR and should be followed in the same manner regardless of the surgical approach.


Assuntos
Adenocarcinoma/cirurgia , Neoplasia Residual/diagnóstico , Prostatectomia/mortalidade , Neoplasias da Próstata/cirurgia , Robótica , Adenocarcinoma/mortalidade , Adenocarcinoma/patologia , Idoso , Progressão da Doença , Seguimentos , Humanos , Estimativa de Kaplan-Meier , Masculino , Pessoa de Meia-Idade , Gradação de Tumores , Estadiamento de Neoplasias , Neoplasia Residual/cirurgia , Antígeno Prostático Específico/sangue , Neoplasias da Próstata/mortalidade , Neoplasias da Próstata/patologia , Estudos Retrospectivos , Medição de Risco , Taxa de Sobrevida
2.
J Chromatogr B Analyt Technol Biomed Life Sci ; 879(24): 2437-42, 2011 Aug 15.
Artigo em Inglês | MEDLINE | ID: mdl-21783437

RESUMO

Heparin binding (HB) proteins mediate a wide range of important cellular processes, which makes this class of proteins biopharmaceutically important. Engineering HB proteins may bring many advantages, but it necessitates cost effective and efficient purification methodologies compared to currently available methods. One of the most important classes of HB proteins are fibroblast growth factors (FGFs) and their receptors (FGFRs). In this study, we report an efficient off-column purification of FGF-1 from soluble fractions and purification of the D2 domain of FGFR from insoluble inclusion bodies, using a weak Amberlite cation (IRC) exchanger. FGF-1 and the D2 domain have been expressed in Escherichia coli and purified to homogeneity using IRC resin. This approach is an alternative to conventional affinity column chromatography, which exhibits several disadvantages, including time-consuming experimental procedures for purification and regeneration and results in the expensive production of recombinant proteins. Results of the heparin binding chromatography and steady state fluorescence experiments show that the FGF-1 and the D2 are in a native conformation. The findings of this study will not only aid an in-depth investigation of this class of proteins but will also provide avenues for inexpensive and efficient purification of other important biological macromolecules.


Assuntos
Cromatografia por Troca Iônica/métodos , Fator 1 de Crescimento de Fibroblastos/isolamento & purificação , Heparina/química , Receptores de Fatores de Crescimento de Fibroblastos/isolamento & purificação , Cromatografia por Troca Iônica/economia , Fator 1 de Crescimento de Fibroblastos/genética , Fator 1 de Crescimento de Fibroblastos/metabolismo , Humanos , Ligação Proteica , Estrutura Terciária de Proteína , Receptores de Fatores de Crescimento de Fibroblastos/química , Receptores de Fatores de Crescimento de Fibroblastos/genética , Receptores de Fatores de Crescimento de Fibroblastos/metabolismo , Proteínas Recombinantes/genética , Proteínas Recombinantes/isolamento & purificação , Proteínas Recombinantes/metabolismo
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA