|Date:||Saturday, December 3, 2016|
|Time:||5:30 - 7:30 p.m. PST|
|Location:||Hall GH of the San Diego Convention Center|
|Poster Session:||101. Red Cells and Erythropoiesis, Structure and Function, Metabolism, andSurvival, Excluding Iron: Poster I|
Regulatory News: ERYTECH Pharma (Paris:ERYP) (ADR:EYRYY) (Euronext Paris: ERYP), the French biopharmaceutical company developing 'tumor starvation' treatments for acute leukemia and other oncology indications with unmet medical needs, today announced the presentation of promising preliminary data for the Company's lead product candidate, eryaspase, also known as ERY-ASP or under the trade name GRASPA®, at the 58th American Society of Hematology (ASH) Annual Meeting and Exposition , being held December 3-6, 2016 in San Diego, California. The research was conducted at The University of Texas MD Anderson Cancer Center. Dr. Philip Lorenzi, Co-Director of the Proteomics and Metabolomics Core Facility and lead author of the poster, will present a summary of the findings from a preclinical study which demonstrates that eryaspase, L-asparaginase encapsulated in red blood cells (RBC), has differential dual activity on its main targets, asparagine and glutamine, when compared to non-encapsulated native asparaginase (L-ASP), during a poster session. Abstract #1266 : Red Blood Cell-Encapsulation of L-Asparaginase Favorably Modulates Target Selectivity and Pharmacodynamics
The anticancer effect of asparaginase products is attributed to the systemic degradation of asparagine, a critical amino acid for the growth and survival of cancer cells. Asparaginase is also known to have a glutaminase effect. The degradation of glutamine has been demonstrated to be associated with clinical toxicity. The study aimed to characterize the transport and degradation of the different amino acids between the plasma and the RBC cytoplasm in the presence of L-ASP or eryaspase. Using a new bioanalytical method, MD Anderson researchers analyzed several metabolites to study differential conversion of asparagine and glutamine. In the presence of eryaspase, asparagine was rapidly and extensively converted to aspartic acid inside the RBC, whereas eryaspase displayed significantly decreased glutaminase activity as compared to L-ASP. The approximately 3.5-fold increase in selectivity for asparagine over glutamine may explain the observed decrease in frequency of adverse events in clinical trials with eryaspase compared to L-ASP. Altered target selectivity is believed to be an additional beneficial property of the encapsulation in the RBC, on top of improved half-life and decreased immunogenicity. The results also provided further evidence of the 'bioreactor' mode of action of eryaspase, demonstrating that the enzymatic activity is essentially happening inside the RBC.