“All viruses are alike in that they have protein coats containing nucleic acid...Enzymes fight viruses by breaking up this protein” (Anthony J Cichoke, D.C.)
Protease is a classification of a group of enzymes which act on protein molecules and assist in catalyzing reactions. These reactions, in effect help to change the molecular structure, or break down the protein molecules. Based on clinical studies, it is known that proteases are able to dissolve almost all proteins as long as they are not components of living cells. Normal living cells are protected against lysis by the inhibitor mechanism. Viruses, parasites, fungal forms, and bacteria are either protein or protected by protein. The introduction of oral proteases presents the ability of those enzymes to act upon the protein coating of viruses or any protein that is harmful to the body or does not belong. Enzymes can also break down undigested food protein, cellular debris, and toxins in the blood, sparing the immune system this task. The immune system can then concentrate its full action on the bacterial or parasitic invasion. It should be noted that protease when taken on an empty stomach are readily taken up into the mucosa cells of the intestine and passed into the blood circulation. Clinical observations have noted that upon high intake of oral protease, heavy metal concentrations have been significantly decreased in the blood. While in the blood, proteases are taken up byalpha II-macroglobulin which ensures its survival in the body. This same alpha II macroglobulin escorts the protease throughout the body and appears to have the same ability that white blood cells have for determining what does not belong. Once identified the Alpha II macroglobulin exposes the protease to the protein invader and digestion of that protein begins.
Tuesday, June 3, 2008
A Host Lipase Detoxifies Bacterial Lipopolysaccharides in the Liver and Spleen*
Baomei Shao, Mingfang Lu, Steven C. Katz, Alan W. Varley, John Hardwick, Thomas E. Rogers, Noredia Ojogun, Donald C. Rockey, Ronald P. DeMatteo, and Robert S. Munford
From the Departments of Internal Medicine, Microbiology and Pathology, University of Texas Southwestern Medical School, Dallas, Texas 75390-9113 and the Hepatobiliary Service, Memorial Sloan-Kettering Cancer Center, New York, New York 10021
Much of the inflammatory response of the body to blood borne Gram-negative bacteria occurs in the liver and spleen, the major organs that remove these bacteria and their lipopolysaccharide (endotoxin) from the bloodstream. We show here that Lipopolysaccharide undergoes deacylation in the liver and spleen by acyloxyacyl hydrolase (AOAH), an endogenous lipase that selectively removes the secondary fatty acyl chains that are required for Lipopolysaccharide recognition by its mammalian signaling receptor, MD-2-TLR4. We further show that Kupffer cells produce AOAH and are required for hepatic Lipopolysaccharide deacylation in vivo. AOAH-deficient mice did not deacylate Lipopolysaccharide and, whereas their inflammatory responses to low doses of Lipopolysaccharide were similar to those of wild type mice for 3 days after Lipopolysaccharide challenge, they subsequently developed pronounced hepatosplenomegaly. Providing recombinant AOAH restored Lipopolysaccharide deacylating ability to Aoah-/- mice and prevented Lipopolysaccharide-induced hepatomegaly. AOAH-mediated deacylation is a previously unappreciated mechanism that prevents prolonged inflammatory reactions to Gram-negative bacteria and Lipopolysaccharide in the liver and spleen.
From the Departments of Internal Medicine, Microbiology and Pathology, University of Texas Southwestern Medical School, Dallas, Texas 75390-9113 and the Hepatobiliary Service, Memorial Sloan-Kettering Cancer Center, New York, New York 10021
Much of the inflammatory response of the body to blood borne Gram-negative bacteria occurs in the liver and spleen, the major organs that remove these bacteria and their lipopolysaccharide (endotoxin) from the bloodstream. We show here that Lipopolysaccharide undergoes deacylation in the liver and spleen by acyloxyacyl hydrolase (AOAH), an endogenous lipase that selectively removes the secondary fatty acyl chains that are required for Lipopolysaccharide recognition by its mammalian signaling receptor, MD-2-TLR4. We further show that Kupffer cells produce AOAH and are required for hepatic Lipopolysaccharide deacylation in vivo. AOAH-deficient mice did not deacylate Lipopolysaccharide and, whereas their inflammatory responses to low doses of Lipopolysaccharide were similar to those of wild type mice for 3 days after Lipopolysaccharide challenge, they subsequently developed pronounced hepatosplenomegaly. Providing recombinant AOAH restored Lipopolysaccharide deacylating ability to Aoah-/- mice and prevented Lipopolysaccharide-induced hepatomegaly. AOAH-mediated deacylation is a previously unappreciated mechanism that prevents prolonged inflammatory reactions to Gram-negative bacteria and Lipopolysaccharide in the liver and spleen.
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