You are not currently logged in.
Access your personal account or get JSTOR access through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Recombinant Human Nerve Growth Factor with a Marked Activity in vitro and in vivo
Anna M. Colangelo, Nicoletta Finotti, Michela Ceriani, Lilia Alberghina, Enzo Martegani, Luigi Aloe, Laura Lenzi and Rita Levi-Montalcini
Proceedings of the National Academy of Sciences of the United States of America
Vol. 102, No. 51, Enzymatic Rescue of Myelination (Dec. 20, 2005), pp. 18658-18663
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/4152673
Page Count: 6
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Recombinant human nerve growth factor (rhNGF) is regarded as the most promising therapy for neurodegeneration of the central and peripheral nervous systems as well as for several other pathological conditions involving the immune system. However, rhNGF is not commercially available as a drug. In this work, we provide data about the production on a laboratory scale of large amounts of a rhNGF that was shown to possess in vivo biochemical, morphological, and pharmacological effects that are comparable with the murine NGF (mNGF), with no apparent side effects, such as allodynia. Our rhNGF was produced by using conventional recombinant DNA technologies combined with a biotechnological approach for high-density culture of mammalian cells, which yielded a production of ≈21.5 ± 2.9 mg/liter recombinant protein. The rhNGF-producing cells were thoroughly characterized, and the purified rhNGF was shown to possess a specific activity comparable with that of the 2.5S mNGF by means of biochemical, immunological, and morphological in vitro studies. This work describes the production on a laboratory scale of high levels of a rhNGF with in vitro and, more important, in vivo biological activity equivalent to the native murine protein.
Proceedings of the National Academy of Sciences of the United States of America © 2005 National Academy of Sciences