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Nerve Growth Factor: A Protease that can Activate Plasminogen
Neil S. Orenstein, Harold F. Dvorak, Muriel H. Blanchard and Michael Young
Proceedings of the National Academy of Sciences of the United States of America
Vol. 75, No. 11 (Nov., 1978), pp. 5497-5500
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/68659
Page Count: 4
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The single, highly stable form of mouse submandibular gland nerve growth factor (NGF), prepared as described by Young et al. [(1978) Biochemistry 17, 1490-1498] is a protease of restricted specificity that can convert plasminogen to plasmin. In the absence of plasminogen, NGF is not fibrinolytic, nor does it hydrolyze casein at a measurable rate. Treatment of NGF with diisopropyl fluorophosphate inhibits its ability to activate plasminogen as well as its capacity to hydrolyze certain synthetic arginine esters. These results indicate that NGF is a member of the class of serine proteases. Since NGF is known to be secreted at high concentrations in mouse saliva, it may serve to activate plasminogen (with subsequent fibrinolysis) somewhere in the alimentary tract. Plasminogen activation is the only known action of NGF upon a biologically important non-neural substrate.
Proceedings of the National Academy of Sciences of the United States of America © 1978 National Academy of Sciences