Nagalese Blood Test *
The Nagalase test is a simple blood test that measures the presence of the enzyme Nagalase. Nagalase is produced by cancer cells (and some viruses) and not by healthy cells. Any amount of Nagalase in the blood means that there are cancer cells that are multiplying and dividing. It has been shown that nagalase basically undermines the Immune System so that the macrophages that gobble up and dismantle cancer cells can no longer do their job. (1)
The strong point of this Nagalase test is that it is ultra sensitive. It can detect cancer when it is at the cellular stage instead of the tumor stage. It can take 5-10 years for a tumor to develop and be seen on an x-ray or in blood work. This Nagalase test significantly accelerates detection time.
This test can also be used for monitoring the effect of therapy of cancer and certain viral infections, including but not limited to HIV & Autism.
The Scientific Data Supporting these Claims
Nagalase has been detected in many cancer patients, but not in healthy individuals (2). Studies have shown that the production of nagalase has a mutual relationship with Gc-MAF level and immunosuppression (2,3). It has been demonstrated that serum levels of nagalase are good prognosticators of some types of cancer (5). The nagalase level in serum correlates with tumor burden and it has been shown that Gc-MAF therapy progresses, nagalase activity decreases (4).
There are many other tools in conventional and integrative medicine. The French Oligoscan comes to mind. It has been touted as a great diagnostic tool, based on neurofeedback. But the Institute can’t form an opinioin not having experienced this scan.
Where to Get it ?
So far, it’s only available in Europe.
Reference and Precision Notes
1. This test measures the activity of alpha-N-acetylgalactosaminidase (nagalase) in blood. Nagalase is an extracellular matrix-degrading enzyme that is (increased) secreted by cancerous cells in the process of tumor invasion. It also is an intrinsic component of envelope protein of various virions, such as HIV and the influenza virus. It is secreted from virus-infected cells. (…) Increased activity of nagalase has been detected in the blood of patients with a wide variety of cancers, like cancer of the prostate, breast, colon, lung, oesophagus, stomach, liver, pancreas, kidney, bladder, testis, uterus and ovary, mesothelioma, melanoma, fibrosarcoma, glioblastoma, neuroblastoma and various leukeamias. For various types of tumors various levels of nagalase activity were found.7 It seems likely that secretory capacity of individual tumor tissue varies among tumor types depending upon tumor size, staging, and the degree of malignancy or invasiveness.7 Increased nagalase activity has not been detected in the blood of healthy humans. (….) It has been established that the nagalase activity is directly proportional to viable tumor burden. Studies correlating nagalase levels with tumor burden suggest that the measurement of this enzyme can diagnose the presence of cancerous lesions below levels detectable by other diagnostic means. In research a day after surgical removal of primary tumors from cancer patients nagalase activity suddenly decreased to near the tumor-free control level, suggesting that the half-life value of nagalase is less than 24 hours.1,6 The short half-life of nagalase is valuable for prognosis of the disease during various therapies. (Source)
(2). Reddi AL, Sankaranarayanan K, Arulraj HS, Devaraj N, Devaraj H. Serum alpha-N-acetylgalactosaminidase is associated with diagnosis/prognosis of patients with squamous cell carcinoma of the uterine cervix. Cancer Lett. 2000;158:61–4. [PubMed]
(3) Matsuura T, Uematsu T, Yamaoka M, Furusawa K. Effect of salivary gland adenocarcinoma cell-derived alpha-N-acetylgalactosaminidase on the bioactivity of macrophage activating factor. Int J Oncol. 2004;24:521–8. [PubMed]
(4). Yamamoto N, Suyama H. Immunotherapy for prostate cancer with Gc protein-derived macrophage-activating factor, GcMAF. Transl Oncol. 2008;1:65–72. [PMC free article] [PubMed]
(5) Rehder DS, Nelson RW, Borges CR. Glycosylation status of vitamin D binding protein in cancer patients. Protein Sci. 2009;18:2036–42. [PMC free article] [PubMed]
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