J. Agric. Food Chem. 2009, 57, 503–508 [
missclasses.com]
Amyloid-Degrading Ability of Nattokinase from Bacillus subtilis Natto
RUEI-LIN HSU, KUNG-TA LEE, JUNG-HAO WANG, LILY Y.-L. LEE, AND RITA P.-Y. CHEN,
Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan, R. O. C.,
Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan, R. O. C.,
Department of Biochemical Science and Technology, National Taiwan University, Taipei 106, Taiwan, R. O. C.
[overview:]
More than 20 unrelated proteins can form amyloid fibrils in vivo which are related to various diseases, such as Alzheimer’s disease, prion disease, and systematic amyloidosis. Amyloid fibrils are an ordered protein aggregate with a lamellar cross-structure. Enhancing amyloid clearance is one of the targets of the therapy of these amyloid-related diseases. Although there is debate on whether the toxicity is due to amyloids or their precursors, research on the degradation of amyloids may help prevent or alleviate these diseases. In this study, we explored the amyloid-degrading ability of nattokinase, a fibrinolytic subtilisin-like serine protease, and determined the optimal conditions for amyloid hydrolysis. This ability is shared by proteinase K and subtilisin Carlsberg, but not by trypsin or plasmin.
KEYWORDS: Nattokinase; amyloid; natto; subtilisin NAT; amyloid degradation; fibril; amyloidosis
[quote:]
The discovery of an enzyme which can be safely taken orally and can degrade amyloid fibrils could be very useful in the therapy of amyloid-related diseases. Nattokinase not only dissolved blood clots (9) but also degraded amyloid fibrils. Our amyloid-degrading studies demonstrated that it is active at neutral pH and body temperature. Previous results in rats, dogs, and humans have suggested that nattokinase can enter the circulation when taken orally (11, 12), so it has the potential to clear amyloid deposits in various parts of the body.
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amyloid protein [
en.wikipedia.org]
Amyloids are insoluble fibrous protein aggregates sharing specific structural traits. They arise from at least 18 inappropriately folded versions of proteins and polypeptides present naturally in the body.[1] These misfolded structures alter their proper configuration such that they erroneously interact with one another or other cell components forming insoluble fibrils.
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amyloidosis [
en.wikipedia.org]
In medicine, amyloidosis refers to a variety of conditions wherein amyloid proteins are abnormally deposited in organs or tissues and cause harm.
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Isolated atrial amyloidosis [
en.wikipedia.org]
Isolated atrial amyloidosis is a form of amyloidosis affecting the atria of the heart. It is associated with accumulation of atrial natriuretic factor.[1] It may cause arrythmias.
Edited 2 time(s). Last edit at 08/15/2012 09:12PM by Erling.
