Shire plc, the global specialty biopharmaceutical company, today reported that it has completed its submission of a New Drug Application (NDA) for velaglucerase alfa, its enzyme replacement therapy in development for the treatment of Type 1 Gaucher disease, with the US Food and Drug Administration (FDA).
The Company also announced positive results from the final two phase III studies of velaglucerase alfa, with both studies reaching all of their primary and secondary endpoints.
“The submission of the NDA for velaglucerase alfa, earlier than previously announced, is an important milestone for Shire, bringing us another step closer to providing a new treatment option for patients with Type 1 Gaucher disease,” said Sylvie Grégoire, President of Shire Human Genetic Therapies.
“We are also pleased to report that the data from our final two phase III trials met our expectations by reaching all of their primary and secondary endpoints, demonstrating consistency with the results recently reported from the first phase III trial. In addition, we are on-track to submit our European filing for velaglucerase alfa by the end of 2009.”
Shire’s velaglucerase alfa program included the largest and most comprehensive set of phase III clinical trials conducted to date for Gaucher disease. Over 100 patients at 24 sites in 10 countries around the world have participated in the clinical studies.
“I am impressed by the series of clinical trials that were designed to evaluate velaglucerase alfa at multiple doses and in different patient groups,” said Dr Christine Eng, Professor of Molecular and Human Genetics, Baylor College of Medicine.
“The inclusion of children, who are often the sickest patients, is especially useful. I believe velaglucerase alfa will be an important new treatment option for Type 1 Gaucher disease and I am pleased that there is a mechanism in place for physicians to access this therapy for their patients.”
Velaglucerase alfa is made using Shire’s proprietary technology, in a human cell line. The enzyme produced has the exact human amino acid sequence and has a human glycosylation pattern.