نتایج جستجو برای: ricin

تعداد نتایج: 1594  

2016
Dakshina M. Jandhyala John Wong Nicholas J. Mantis Bruce E. Magun John M. Leong Cheleste M. Thorpe

Ricin activates the proinflammatory ribotoxic stress response through the mitogen activated protein 3 kinase (MAP3K) ZAK, resulting in activation of mitogen activated protein kinases (MAPKs) p38 and JNK1/2. We had a novel zak-/- mouse generated to study the role of ZAK signaling in vivo during ricin intoxication. To characterize this murine strain, we intoxicated zak-/- and zak+/+ bone marrow-d...

2011
Julie Prigent Laetitia Panigai Patricia Lamourette Didier Sauvaire Karine Devilliers Marc Plaisance Hervé Volland Christophe Créminon Stéphanie Simon

The Centers for Disease Control and Prevention have listed the potential bioweapon ricin as a Category B Agent. Ricin is a so-called A/B toxin produced by plants and is one of the deadliest molecules known. It is easy to prepare and no curative treatment is available. An immunotherapeutic approach could be of interest to attenuate or neutralise the effects of the toxin. We sought to characteris...

2017
Kendrick B. Turner Sabrina Hardy Jinny L. Liu Dan Zabetakis Audrey Brozozog Lee Ellen R. Goldman George P. Anderson Dimiter S. Dimitrov

Previously, our group isolated and evaluated anti-ricin single domain antibodies (sdAbs) derived from llamas, engineered them to further increase their thermal stability, and utilized them for the development of sensitive immunoassays. In work focused on the development of therapeutics, Vance et al. 2013 described anti-ricin sdAbs derived from alpacas. Herein, we evaluated the utility of select...

Journal: :The Journal of Cell Biology 1986
B van Deurs T I Tønnessen O W Petersen K Sandvig S Olsnes

Receptor-mediated endocytosis and intracellular routing of native ricin, and of ricin conjugated to colloidal gold (Ri-Au) and to horseradish peroxidase (Ri-HRP), have been studied in cultured MCF-7 and Vero cells by electron microscopical techniques including serial section analysis. Both native ricin, as demonstrated by immunoperoxidase cytochemistry, and the ricin conjugates were internalize...

2015
Sylvia Worbs Martin Skiba Martin Söderström Marja-Leena Rapinoja Reinhard Zeleny Heiko Russmann Heinz Schimmel Paula Vanninen Sten-Åke Fredriksson Brigitte G. Dorner Daniel Gillet

Ricinus communis intoxications have been known for centuries and were attributed to the toxic protein ricin. Due to its toxicity, availability, ease of preparation, and the lack of medical countermeasures, ricin attracted interest as a potential biological warfare agent. While different technologies for ricin analysis have been established, hardly any universally agreed-upon "gold standards" ar...

2004
Om Kumar A. B. Nashikkar R. Jayaraj R. Vijayaraghavan

Ricin is a highly toxic plant toxin of Ricinus comtnunis seeds, commonly known as castor seeds. The toxin was extracted and purified using affinity and size exclusion chromatography. The purity of ricin was evaluated by the sodium dodecylsulphate-polyacrylamide gel electrophoresis. Purified ricin gives a single band under non-reduced condition and two bands under reduced condition. The molecula...

2012
Ronald B. Reisler Leonard A. Smith

Ricin toxin, an extremely potent and heat-stable toxin produced from the bean of the ubiquitous Ricinus communis (castor bean plant), has been categorized by the US Centers for Disease Control and Prevention (CDC) as a category B biothreat agent that is moderately easy to disseminate. Ricin has the potential to be used as an agent of biological warfare and bioterrorism. Therefore, there is a cr...

2011
Tove Irene Klokk Anne Berit Dyve Lingelem Anne-Grethe Myrann Kirsten Sandvig

Ricin is a protein toxin classified as a bioterror agent, for which there are no known treatment options available after intoxication. It is composed of an enzymatically active A-chain connected by a disulfide bond to a cell binding B-chain. After internalization by endocytosis, ricin is transported retrogradely to the Golgi and ER, from where the ricin A-chain is translocated to the cytosol wh...

Journal: :Infection and immunity 2006
Nicholas J Mantis Carolyn R McGuinness Oluwakemi Sonuyi Gary Edwards Stephanie A Farrant

Epithelial cells of the respiratory and gastrointestinal tracts are extremely vulnerable to the cytotoxic effects of ricin, a Shiga-like toxin with ribosome-inactivating properties. While mucosal immunity to ricin correlates with secretory immunoglobulin A (IgA) antibody levels in vivo, the potential of IgA to protect epithelial cells from ricin in vitro has not been examined due to the unavail...

Journal: :The Biochemical journal 1991
S Magnusson T Berg E Turpin J P Frénoy

We have investigated the interactions of the plant toxin ricin with sinusoidal endothelial rat liver cells (EC). In these cells, ricin can be bound and internalized via either cell surface galactosyl residues or mannose receptors. Binding and uptake via galactosyl residues and mannose receptors was studied in the presence of mannan (1 mg/ml) and lactose (50 mM) respectively. Whereas most of the...

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