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1.
Front Robot AI ; 8: 773830, 2021.
Artículo en Inglés | MEDLINE | ID: mdl-35174216

RESUMEN

Robotic Surgery is getting widely spread and applied to more and more clinical cases due to its advantages compared to open surgery, for both the patients and surgeons. However, Robotic Surgery requires a different set of skills and learning compared to open and also laparoscopic surgery. Tele-operation for a robotic system with hand controllers, the delay in the hand commands to be translated into robotic movements, slowness of the robotic movements, remote 2D or 3D vision of the actual operation, and lack of haptic feedback are some of the challenges that Robotic Surgery poses. Surgeons need to go through an intensive training for Robotic Surgery, and the learning and skill development continues throughout their early professional years. Despite the importance of training for Robotic Surgery, there are not yet dedicated, low-cost, and widespread training platforms; rather, surgeons mostly train with the same Robotic Surgery system they use in surgery; hence institutions need to invest on a separate surgical setup for training purposes. This is expensive for the institutions, it provides very limited access to the surgeons for training, and very limited, if any, access to researchers for experimentation. To address these, we have developed in our laboratory a low-cost, and experimental Robotic Surgery Trainer. This setup replicates the challenges that a Robotic Surgery system poses and further provides widespread access through internet connected control of the actual physical system. The overall system is composed of equipment that a standard engineering laboratory can afford. In this paper, we introduce the Robotic Surgery Training System and explain its development, parts, and functionality.

2.
Ann Thorac Surg ; 97(4): 1440-3, 2014 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-24694427

RESUMEN

We review the journey to myocardial and neurologic recovery of a 42-year-old mother with severe acute cardiogenic shock and multiorgan failure after extensive subarachnoid hemorrhage, who was salvaged successfully using a CentriMag short-term biventricular assist device.


Asunto(s)
Corazón Auxiliar , Choque Cardiogénico/etiología , Choque Cardiogénico/cirugía , Hemorragia Subaracnoidea/complicaciones , Adulto , Femenino , Humanos
4.
Plant J ; 51(2): 322-30, 2007 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-17610544

RESUMEN

Progress in analysing the cellular functions of many structural proteins has accelerated through the use of confocal microscopy together with transient gene expression. Several methods for transient expression have been developed in the past few years, but their application has seen limited success beyond a few tractable species and tissues. We have developed a simple and efficient method to visualize fluorescent proteins in Arabidopsis root epidermis using co-cultivation of seedlings with Agrobacterium rhizogenes. The method is equally suitable for transient gene expression in other species, including Thellungiella, and can be combined with supporting molecular and biochemical analyses. The method promises significant advantages for study of membrane dynamics, cellular development and polar growth in root hairs without interference in the development of the plant. Since the method targets specifically the root epidermis, it also offers a powerful tool to approach issues of root-rhizosphere interactions, such as ion transport and nutrient acquisition. As a proof of principle, we carried out transfections with fluorescent markers for the plasma membrane (NpPMA2-GFP, Nicotiana plumbaginifolia L. Plasma Membrane H(+)-ATPase 2), the endoplasmic reticulum (YFP-HDEL), and the Golgi apparatus (sialyl transferase-GFP) to trace their distribution in growing Arabidopsis root hairs and epidermis. The results demonstrate that, in Arabidopsis root hairs, movement of the Golgi is faster than previously reported for tobacco leaf epidermal cells, consistent with the high secretory dynamics of the tip growing cell; they show a pattern to the endoplasmic reticulum within the cytoplasm that is more diffuse than found in tobacco leaf epidermis, and they confirm previous findings of a polarized distribution of the endoplasmic reticulum at the tip of growing root hairs.


Asunto(s)
Arabidopsis/citología , Endosomas/metabolismo , Epidermis de la Planta/citología , Epidermis de la Planta/genética , Raíces de Plantas/citología , Raíces de Plantas/genética , Transfección/métodos , Arabidopsis/genética , Biomarcadores
5.
J Biol Chem ; 280(48): 39677-80, 2005 Dec 02.
Artículo en Inglés | MEDLINE | ID: mdl-16204243

RESUMEN

C5L2 is an enigmatic serpentine receptor that is co-expressed with the C5a receptor on many cells including polymorphonuclear neutrophils. The apparent absence of coupling of C5L2 with G proteins suggests that this receptor may modulate the biological activity of C5a, perhaps by acting as a decoy receptor. Alternatively, C5L2 may affect C5a function through formation of a heteromeric complex with the C5aR, or it may utilize a G protein-independent signaling pathway. Here we show that in mice bearing a targeted deletion of C5L2, the biological activity of C5a/C5a(desArg) is enhanced both in vivo and in vitro. The biological role of C5L2 thus appears to be limiting to the pro-inflammatory response to the anaphylatoxin. Accordingly, up-regulation of C5L2 may be of benefit in inflammatory states driven by C5a, including sepsis, asthma, cystic fibrosis, and chronic obstructive lung disease.


Asunto(s)
Antiinflamatorios/farmacología , Complemento C5a/química , Receptores de Quimiocina/fisiología , Anafilatoxinas/química , Animales , Células de la Médula Ósea/metabolismo , Quimiotaxis , Clonación Molecular , ADN Complementario/metabolismo , Femenino , Proteínas de Unión al GTP/metabolismo , Regulación de la Expresión Génica , Inflamación , Interleucina-6/biosíntesis , Pulmón/patología , Lesión Pulmonar , Masculino , Ratones , Ratones Endogámicos C57BL , Ratones Transgénicos , Modelos Genéticos , Neutrófilos/metabolismo , Fenotipo , Unión Proteica , ARN Mensajero/metabolismo , Receptor de Anafilatoxina C5a , Receptores de Quimiocina/genética , Proteínas Recombinantes/química , Factor de Necrosis Tumoral alfa/biosíntesis , Regulación hacia Arriba
6.
J Virol ; 78(10): 5448-57, 2004 May.
Artículo en Inglés | MEDLINE | ID: mdl-15113923

RESUMEN

The synthetic peptide T-20, which corresponds to a sequence within the C-terminal heptad repeat region (HR2) of the human immunodeficiency virus type 1 (HIV-1) gp41 envelope glycoprotein, potently inhibits viral membrane fusion and entry. Although T-20 is thought to bind the N-terminal heptad repeat region (HR1) of gp41 and interfere with gp41 conformational changes required for membrane fusion, coreceptor specificity determined by the V3 loop of gp120 strongly influences the sensitivity of HIV-1 variants to T-20. Here, we show that T-20 binds to the gp120 glycoproteins of HIV-1 isolates that utilize CXCR4 as a coreceptor in a manner determined by the sequences of the gp120 V3 loop. T-20 binding to gp120 was enhanced in the presence of soluble CD4. Analysis of T-20 binding to gp120 mutants with variable loop deletions and the reciprocal competition of T-20 and particular anti-gp120 antibodies suggested that T-20 interacts with a gp120 region near the base of the V3 loop. Consistent with the involvement of this region in coreceptor binding, T-20 was able to block the interaction of gp120-CD4 complexes with the CXCR4 coreceptor. These results help to explain the increased sensitivity of CXCR4-specific HIV-1 isolates to the T-20 peptide. Interactions between the gp41 HR2 region and coreceptor-binding regions of gp120 may also play a role in the function of the HIV-1 envelope glycoproteins.


Asunto(s)
Antígenos CD4/fisiología , Proteína gp120 de Envoltorio del VIH/metabolismo , Proteína gp41 de Envoltorio del VIH/metabolismo , VIH-1/fisiología , Receptores CXCR4/metabolismo , Secuencia de Aminoácidos , Productos del Gen env/metabolismo , Humanos , Datos de Secuencia Molecular , Productos del Gen env del Virus de la Inmunodeficiencia Humana
7.
Cell ; 114(6): 689-99, 2003 Sep 19.
Artículo en Inglés | MEDLINE | ID: mdl-14505569

RESUMEN

HIV-1 and other retroviruses exit infected cells by budding from the plasma membrane, a process requiring membrane fission. The primary late assembly (L) domain in the p6 region of HIV-1 Gag mediates the detachment of the virion by recruiting host Tsg101, a component of the class E vacuolar protein sorting (Vps) machinery. We now show that HIV Gag p6 contains a second region involved in L domain function that binds AIP1, a homolog of the yeast class E Vps protein Bro1. Further, AIP1 interacts with Tsg101 and homologs of a subunit of the yeast class E Vps protein complex ESCRT-III. AIP1 also binds to the L domain in EIAV p9, and this binding correlates perfectly with L domain function. These observations identify AIP1 as a component of the viral budding machinery, which serves to link a distinct region in the L domain of HIV-1 p6 and EIAV p9 to ESCRT-III.


Asunto(s)
Productos del Gen gag/metabolismo , VIH-1/metabolismo , Virus de la Anemia Infecciosa Equina/metabolismo , Proteínas de Microfilamentos/metabolismo , Esparcimiento de Virus/fisiología , Adenosina Trifosfatasas/genética , Adenosina Trifosfatasas/metabolismo , Sitios de Unión/genética , Membrana Celular/metabolismo , Membrana Celular/virología , Proteínas de Unión al ADN/genética , Proteínas de Unión al ADN/metabolismo , Complejos de Clasificación Endosomal Requeridos para el Transporte , Productos del Gen gag/genética , VIH-1/genética , Células HeLa , Humanos , Virus de la Anemia Infecciosa Equina/genética , Proteínas de Microfilamentos/genética , Microscopía Electrónica , Proteínas Nucleares/genética , Proteínas Nucleares/metabolismo , Unión Proteica/genética , Estructura Terciaria de Proteína/genética , Proteínas Recombinantes de Fusión/genética , Proteínas Recombinantes de Fusión/metabolismo , Proteínas de Saccharomyces cerevisiae/genética , Proteínas de Saccharomyces cerevisiae/metabolismo , Virus de la Inmunodeficiencia de los Simios/genética , Virus de la Inmunodeficiencia de los Simios/metabolismo , Factores de Transcripción/genética , Factores de Transcripción/metabolismo , Proteínas de Transporte Vesicular , Productos del Gen gag del Virus de la Inmunodeficiencia Humana
8.
Ann Thorac Surg ; 74(3): 929-31, 2002 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-12238873

RESUMEN

Lung volume reduction operation is an important therapeutic option in patients with advanced emphysema. We report a case of spontaneous rupture of the right diaphragm after a video-assisted thoracoscopic surgical procedure for emphysema. The pathophysiology of this complication is also discussed, along with practical points for perioperative management of emphysematous patients.


Asunto(s)
Hernia Diafragmática/diagnóstico por imagen , Complicaciones Posoperatorias/diagnóstico por imagen , Enfisema Pulmonar/cirugía , Cirugía Torácica Asistida por Video , Diagnóstico Diferencial , Femenino , Hernia Diafragmática/cirugía , Humanos , Persona de Mediana Edad , Complicaciones Posoperatorias/cirugía , Radiografía , Reoperación , Rotura Espontánea
9.
Asian Cardiovasc Thorac Ann ; 10(4): 376-7, 2002 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-12538297

RESUMEN

A method of performing redo cardiac operations using port-access technology and total circulatory arrest is described. The technique was useful in 2 cases requiring re-intervention within 4 months of the primary procedure. The indications were repair of an infected ventricular aneurysm and recurrence of a postinfarction ventricular septal defect. Dense mediastinal adhesions were avoided by approaching the site of pathology directly via a left anterior thoracotomy.


Asunto(s)
Cateterismo Cardíaco/instrumentación , Cateterismo Cardíaco/métodos , Puente Cardiopulmonar/instrumentación , Puente Cardiopulmonar/métodos , Aneurisma Cardíaco/cirugía , Defectos del Tabique Interventricular/cirugía , Instrumentos Quirúrgicos , Humanos , Reoperación
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