21 research outputs found
Estudio Geocientífico Aplicado al Ordenamiento Territorial las Termas de Río Hondo, Provincia de Santiago del Estero, República Argentina
Fil: Balbi, A.B. Servicio Geológico Minero Argentino. Instituto de Geología y Recursos Minerales; Argentina.Fil: Cavallaro, S.L. Servicio Geológico Minero Argentino. Instituto de Geología y Recursos Minerales; Argentina.Fil: Coppolecchia, M. Servicio Geológico Minero Argentino. Instituto de Geología y Recursos Minerales; Argentina.Fil: Fernández, D.S. Servicio Geológico Minero Argentino. Instituto de Geología y Recursos Minerales; Argentina.Fil: Grecco, G. Servicio Geológico Minero Argentino. Instituto de Geología y Recursos Minerales; Argentina.Fil: Lamarca, L. Servicio Geológico Minero Argentino. Instituto de Geología y Recursos Minerales; Argentina.Fil: Oliva, J.A. Servicio Geológico Minero Argentino. Instituto de Geología y Recursos Minerales; Argentina.Fil: Rivas, I.S. Servicio Geológico Minero Argentino. Instituto de Geología y Recursos Minerales; Argentina.Fil: Serrano, M. Servicio Geológico Minero Argentino. Instituto de Geología y Recursos Minerales; Argentina.Fil: Sosa, I.G. Servicio Geológico Minero Argentino. Instituto de Geología y Recursos Minerales; Argentina.Fil: Tobio, I. Servicio Geológico Minero Argentino. Instituto de Geología y Recursos Minerales; Argentina.El presente estudio fue efectuado en el marco de un convenio celebrado entre la Municipalidad de Las Termas de Río Hondo y el Servicio Geológico Minero Argentino (SEGEMAR), con el propósito de brindar pautas al Municipio que permitan la toma de decisión en los diferentes aspectos que hacen al crecimiento de la ciudad, conciliando intereses y necesidades diversas.
La planificación es una herramienta adecuada para orientar y organizar el desarrollo equitativo y sustentable de un territorio y la población que lo ocupa. Nos permite determinar los usos del territorio según la mayor o menor aptitud de los diferentes elementos constitutivos del territorio respecto a ellos, garantizando el aprovechamiento sostenible de los recursos naturales y que el conjunto de intervenciones que se desarrollan a lo largo del territorio se realicen en condiciones de sostenibilidad con miras al bienestar común.
La ciudad de Las Termas de Río Hondo se localiza en el centro-oeste de la provincia de Santiago del Estero, siendo esta la cabecera del departamento Río Hondo, a orillas del río Dulce. La zona de estudio, que incluye las localidades de: Colonia Tinco, Villa Río Hondo y Termas de Río Hondo, se desarrolla entre las coordenadas 27º 24' y los 27º 37' de Latitud Sur y los 64º 46' y 64º 58' de Longitud Oeste, posee una cota variable entre 245 y 340 m s.n.m. (Figura 1.1.).
La mencionada localidad es el principal centro termal del país, con un gran desarrollo turístico, pero con problemas en su planificación. Esta actividad de reconocida importancia local, regional y nacional, evidencia una conflictividad creciente no solo entre los usos del suelo, sino también entre dichos usos y la aptitud del territorio.
Este estudio proporciona un inventario de la información biofísica y social del ambiente, integrando el clima, la geología, la geomorfología, la geotecnia, los suelos, la vegetación, amenazas naturales, aguas y el aspecto social. La interacción de estos datos constituye una herramienta adecuada para orientar la transformación, ocupación y utilización de los espacios geográficos, buscando su desarrollo socioeconómico y teniendo en cuenta las necesidades e intereses de la población, las potencialidades del territorio considerado y la armonía con el medio ambiente
Cathepsin K induces platelet dysfunction and affects cell signaling in breast cancer - molecularly distinct behavior of cathepsin K in breast cancer
Background: Breast cancer comprises clinically and molecularly distinct tumor subgroups that differ in cell histology and biology and show divergent clinical phenotypes that impede phase III trials, such as those utilizing cathepsin K inhibitors. Here we correlate the epithelial-mesenchymal-like transition breast cancer cells and cathepsin K secretion with activation and aggregation of platelets. Cathepsin K is up-regulated in cancer cells that proteolyze extracellular matrix and contributes to invasiveness. Although proteolytically activated receptors (PARs) are activated by proteases, the direct interaction of cysteine cathepsins with PARs is poorly understood. In human platelets, PAR-1 and -4 are highly expressed, but PAR-3 shows low expression and unclear functions. Methods: Platelet aggregation was monitored by measuring changes in turbidity. Platelets were immunoblotted with anti-phospho and total p38, Src-Tyr-416, FAK-Tyr-397, and TGF beta monoclonal antibody. Activation was measured in a flow cytometer and calcium mobilization in a confocal microscope. Mammary epithelial cells were prepared from the primary breast cancer samples of 15 women with Luminal-B subtype to produce primary cells. Results: We demonstrate that platelets are aggregated by cathepsin K in a dose-dependent manner, but not by other cysteine cathepsins. PARs-3 and -4 were confirmed as the cathepsin K target by immunodetection and specific antagonists using a fibroblast cell line derived from PARs deficient mice. Moreover, through co-culture experiments, we show that platelets activated by cathepsin K mediated the up-regulation of SHH, PTHrP, OPN, and TGF beta in epithelial-mesenchymal-like cells from patients with Luminal B breast cancer. Conclusions: Cathepsin K induces platelet dysfunction and affects signaling in breast cancer cells.Associacao Beneficente de Coleta de Sangue (Colsan)Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)Univ Fed Sao Paulo, Dept Gynecol, BR-04024002 Sao Paulo, SP, BrazilCOLSAN, Charitable Assoc Blood Collect, BR-04080006 Sao Paulo, SP, BrazilUniv Fed Sao Paulo, Dept Biophys, BR-04024002 Sao Paulo, SP, BrazilUniv Fed Sao Paulo, Dept Biochem, BR-04024002 Sao Paulo, SP, BrazilAntonio Prudente Fdn, AC Camargo Canc Ctr, AC Camargo Hosp Biobank, Dept Pathol, BR-01509010 Sao Paulo, SP, BrazilUniv Fed Sao Paulo, Cellular Gynecol Lab, Dept Gynecol, Rua Napoleao Barros 608, BR-04024002 Sao Paulo, BrazilUniv Fed Sao Paulo, Dept Gynecol, BR-04024002 Sao Paulo, SP, BrazilUniv Fed Sao Paulo, Dept Biophys, BR-04024002 Sao Paulo, SP, BrazilUniv Fed Sao Paulo, Dept Biochem, BR-04024002 Sao Paulo, SP, BrazilUniv Fed Sao Paulo, Cellular Gynecol Lab, Dept Gynecol, Rua Napoleao Barros 608, BR-04024002 Sao Paulo, BrazilFAPESP: 2012/19780-3FAPESP: 2012/19851-8FAPESP: 2009/53766-5Web of Scienc
Nanotopography reveals metabolites that maintain the immunomodulatory phenotype of mesenchymal stromal cells
Mesenchymal stromal cells (MSCs) are multipotent progenitor cells that are of considerable clinical potential in transplantation and anti-inflammatory therapies due to their capacity for tissue repair and immunomodulation. However, MSCs rapidly differentiate once in culture, making their large-scale expansion for use in immunomodulatory therapies challenging. Although the differentiation mechanisms of MSCs have been extensively investigated using materials, little is known about how materials can influence paracrine activities of MSCs. Here, we show that nanotopography can control the immunomodulatory capacity of MSCs through decreased intracellular tension and increasing oxidative glycolysis. We use nanotopography to identify bioactive metabolites that modulate intracellular tension, growth and immunomodulatory phenotype of MSCs in standard culture and during larger scale cell manufacture. Our findings demonstrate an effective route to support large-scale expansion of functional MSCs for therapeutic purposes
Mortality and pulmonary complications in patients undergoing surgery with perioperative SARS-CoV-2 infection: an international cohort study
Background: The impact of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) on postoperative recovery needs to be understood to inform clinical decision making during and after the COVID-19 pandemic. This study reports 30-day mortality and pulmonary complication rates in patients with perioperative SARS-CoV-2 infection. Methods: This international, multicentre, cohort study at 235 hospitals in 24 countries included all patients undergoing surgery who had SARS-CoV-2 infection confirmed within 7 days before or 30 days after surgery. The primary outcome measure was 30-day postoperative mortality and was assessed in all enrolled patients. The main secondary outcome measure was pulmonary complications, defined as pneumonia, acute respiratory distress syndrome, or unexpected postoperative ventilation. Findings: This analysis includes 1128 patients who had surgery between Jan 1 and March 31, 2020, of whom 835 (74·0%) had emergency surgery and 280 (24·8%) had elective surgery. SARS-CoV-2 infection was confirmed preoperatively in 294 (26·1%) patients. 30-day mortality was 23·8% (268 of 1128). Pulmonary complications occurred in 577 (51·2%) of 1128 patients; 30-day mortality in these patients was 38·0% (219 of 577), accounting for 81·7% (219 of 268) of all deaths. In adjusted analyses, 30-day mortality was associated with male sex (odds ratio 1·75 [95% CI 1·28–2·40], p\textless0·0001), age 70 years or older versus younger than 70 years (2·30 [1·65–3·22], p\textless0·0001), American Society of Anesthesiologists grades 3–5 versus grades 1–2 (2·35 [1·57–3·53], p\textless0·0001), malignant versus benign or obstetric diagnosis (1·55 [1·01–2·39], p=0·046), emergency versus elective surgery (1·67 [1·06–2·63], p=0·026), and major versus minor surgery (1·52 [1·01–2·31], p=0·047). Interpretation: Postoperative pulmonary complications occur in half of patients with perioperative SARS-CoV-2 infection and are associated with high mortality. Thresholds for surgery during the COVID-19 pandemic should be higher than during normal practice, particularly in men aged 70 years and older. Consideration should be given for postponing non-urgent procedures and promoting non-operative treatment to delay or avoid the need for surgery. Funding: National Institute for Health Research (NIHR), Association of Coloproctology of Great Britain and Ireland, Bowel and Cancer Research, Bowel Disease Research Foundation, Association of Upper Gastrointestinal Surgeons, British Association of Surgical Oncology, British Gynaecological Cancer Society, European Society of Coloproctology, NIHR Academy, Sarcoma UK, Vascular Society for Great Britain and Ireland, and Yorkshire Cancer Research
Bauhinia forficata lectin (BfL) induces cell death and inhibits integrin-mediated adhesion on MCF7 human breast cancer cells
Background: Plant lectins have attracted great interest in cancer studies due to their antitumor activities. These proteins or glycoproteins specifically and reversibly bind to different types of carbohydrates or glycoproteins. Breast cancer, which presents altered glycosylation of cell surface glycoproteins, is one of the most frequent malignant diseases in women. in this work, we describe the effect of the lectin Bauhinia forficata lectin (BfL), which was purified from B. forficata Link subsp.forficata seeds, on the MCF7 human breast cancer cellular line, investigating the mechanisms involved in its antiproliferative activity.Methods: MCF7 cells were treated with BfL Viability and adhesion alterations were evaluated using flow cytometry and western blotting.Results: BfL. inhibited the viability of the MCF7 cell line but was ineffective on MDA-MB-231 and MCF 10A cells. It inhibits MCF7 adhesion on laminin, collagen I and fibronectin, decreases alpha(1), alpha(6) and beta(1) integrin subunit expression, and increases alpha(5) subunit expression. BfL triggers necrosis and secondary necrosis, with caspase-9 inhibition. It also causes deoxyribonucleic add (DNA) fragmentation, which leads to cell cycle arrest in the G2/M phase and a decrease in the expression of the regulatory proteins pRb and p21.Conclusion: BfL shows selective cytotoxic effect and adhesion inhibition on MCF7 breast cancer cells. General significance: Cell death induction and inhibition of cell adhesion may contribute to understanding the action of lectins in breast cancer. (C) 2014 Elsevier B.V. All rights reserved.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Universidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, BrazilUniversidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, BrazilInst Pesquisas Jardim Bot Rio de Janeiro, BR-22460030 Rio de Janeiro, RJ, BrazilUniv Fed Pernambuco, Dept Bioquim, BR-50670910 Recife, PE, BrazilUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, BrazilUniversidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, BrazilFAPESP: 07/58929-4FAPESP: 09/53766-5FAPESP: 12/06366-4CAPES: 007239/2011-40CNPq: 47027/2012-0Web of Scienc
Immobilized Cratylia mollis lectin: An affinity matrix to purify a soybean (Glycine max) seed protein with in vitro platelet antiaggregation and anticoagulant activities
Lectins, proteins which recognize selectively carbohydrates, have been used as affinity chromatography to purify glycoproteins. Cratylia mollis seed lectin (Cramoll 1,4), of mannose/glucose binding class, immobilized on Sepharose CL-4B, was used as affinity matrix. This paper describes the purification by Cramoll 1,4-Sepharose matrix, and characterization of an anti-platelet and anticoagulant soybean (Glycine max) protein, ApcSP, and its in vitro platelet antiaggregation and anticoagulant activities. SDS-PAGE of ApcSP purified under reducing condition revealed a single glycosilated band of 51 kDa. the N-terminal 10-residue sequence of ApcSP is EGQFGPMIQS, distinct to other soybean seed proteins, such as peroxidase, lectin, 2S albumin and trypsin inhibitor. Deconvolution of CD spectrum indicated 35% alpha-helix, 17% beta-strand, 22% turn and 26% unordered structure; ApcSP fluorescence spectrum showed a maximum emission around 339 nm. the hemostatic parameters revealed inhibition of collagen (p<0.001), thrombin (p<0.05) and ADP (p<0.001)-induced platelet aggregation in the presence of ApcSP (2 mu M), in relation to positive control. the soy protein prolonged the blood coagulation time (activated partial thromboplastin time, more affected, and prothrombin time). the results indicated that immobilized Cramoll 1,4 lectin has the potential to isolate soybean glycoproteins and ApcSP may be important for anti-thrombotic and anticoagulant therapy. (C) 2010 Elsevier B.V. All rights reserved.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Fundacao de Amparo a Ciencia e Tecnologia do Estado de Pernambuco (FACEPE)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Univ Fed Pernambuco, Dept Bioquim, BR-50670420 Recife, PE, BrazilUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, BrazilUniv Estadual Oeste Parana, Ctr Engn & Ciencias Exatas, BR-85903000 Toledo, PR, BrazilUniv Fed Rio de Janeiro, Inst Bioquim Med, BR-21941590 Rio de Janeiro, BrazilUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, BrazilWeb of Scienc