- Reports have been circulating around the natural health community of a compound known as Gc-protein derived macrophage activating factor, or GcMAF, and its remarkable effects on cancer, Autism and other terminal conditions.
- One of these is a video clip (below) of an in vitro attack of macrophages, a type of immune cell, which have been treated with GcMAF against human breast cancer cells. This can be best described by the common internet meme caption of “nom nom nom,” as the clusters of cancer cells are mercilessly devoured. Fortunately for humans, research on real patients has shown that its effects are not confined to a laboratory.In human patients, however, GcMAF is not administered alone. In this study, GcMAF is described as being complexed with oleic acid (OA), which is found in olive oil. Additionally, the GcMAF is prescribed alongside a vegetarian diet; vitamin D3, omega-3 fatty acids, and fermented products containing naturally-occurring GcMAF.
Although these patients all suffered from advanced cancers, within a few weeks, their tumor volume had decreased by an average of 25%. While some clinical results were compared to chemo in tumor-shrinking power, OA- complexed GcMAF, along with some other types of OA- complexed proteins, destroys cancer cells without any ill effects on healthy cells.
One patient discussed in research is a 56-year-old man suffering from a recurrence of metastatic squamous cell carcinoma that was “successfully” treated with chemo and radiation. Because of his cancer’s location, GcMAF was administered by both a nebulizer and subcutaneous injections. Even after only 5 days of treatment, ultrasonography had shown that his tumors had shrunk by approximately one quarter. He also reported improvement in breathing, with ventilation in the apical right lobe improving.
Another patient was a 62-year-old woman with “extensive” breast cancer and no history of conventional treatment. Within one week, the diameter of the two main lymph metastases (the primary tumor was unable to be measured due to size) shrunk from 3.9 to 3.46cm.
While GcMAF has anti-proliferative, anti-metastatic abilities, oleic acid has its own anticancer properties and may assist in binding to cell membranes. Together, they are 200 times more potent than GcMAF alone in destroying cancer cells in vitro. They also increase levels of nitric oxide, which has anticancer as well as antihypertensive properties.
Other documented cases show similar results. For example, a 63-year-old woman with colon cancer that later spread to her lungs and liver experienced a reduction in her liver tumor from 13 to 6.6mL in only 2 weeks of treatment! This was once again achieved by alternating nebulization and injection of OA-GcMAF.
Another patient was a 43-year old-woman with metastatic breast cancer to the bone and liver. After 1 week of both inhaled OA-GcMAF and that injected into her breast, her primary tumor shrunk from 1.8 to 1.3 mL, which was considered representative of four other cases.
Some are less dramatic, such as that of a man in his 30\s who experienced a reduction in one of his melanoma metastases from 52.1 to 48.6mm.
Overall, the use of GcMAF as a safe treatment alternative looks promising despite frightening stories of opposition. However, more evidence, whether scientific or anecdotal, is needed for a definitive conclusion. This is partly because of the lack of instruction on how to produce anything resembling GcMAF at home (unlike the more well-known cannabis oil), which may either be unfeasible or undesired by those producing it. See links below to purchase or for further information.
Q: Does GcMaf work for HIV?
GcMaf has been very successful with HIV.
To sabotage the immune system and put macrophages to sleep, all viruses make Nagalase, the enzyme that blocks production of GcMAF. Without GcMAF (the protein that activates macrophages and jump-starts the entire immune response) HIV and other viruses can grow unimpeded. Nagalase puts the immune system to sleep. Dr. Nobuto Yamamoto demonstrated that GcMAF administration bypasses the Nagalase blockage and re-activates the macrophages, which then proceed to kill the HIV viruses and cure the infection.
Something to cheer about?
People infected with the Human Immunodeficiency Virus (HIV) have something to get excited about. They just don’t know it yet. In 2009 Dr. Nobuto Yamamoto published a landmark paper entitled: “Immunotherapy of HIV-Infected Patients With Gc Protein-Derived Macrophage Activating Factor (GcMAF)” in the Journal of Medical Virology in which he demonstrated that GcMAF cured 100% of nonanemic HIV infected patients. After seven years of followup, there were no recurrences. All patients maintained healthy CD+ counts. I am experiencing the very same with our patients at the clinic.
Of course, this is just one study. And it had the disadvantage of containing some complex molecular biological chemo-speak. If the reader weren’t familiar with Yamamoto’s decades of background research (all of which was published in journals that HIV researchers and patients wouldn’t be likely to read), this study would fall on deaf ears. But Professor Yamamoto’s HIV study was no quirk. Based on a quarter-century of solid research that predicted success long before the actual human trials, it presented all the science one would need to understand exactly why these HIV patients were cured.
Though this study was published in 2009, there has been no informed discussion on this topic, no further GcMAF research as a therapy for HIV, and no media chatter. It’s as if this study never happened. Why is this?
How GcMAF destroys HIV
HIV—like all viruses—makes Nagalase, the enzyme that blocks GcMAF production. Without GcMAF, macrophages become indolent and the anti-viral immune response shuts down. This allows the HIV infection to spread. To remedy this situation, Dr. Yamamoto simply gave these patients GcMAF. This reactivated the sleeping macrophages, which then proceeded to phagocytize all of the viruses.
The precise molecular biological pathways and mechanisms involved with HIV, Nagalase, and GcMAF are identical to those for cancer cells, and need not be repeated here.
In his HIV study Yamamoto first showed that HIV patients had high Nagalase levels which correlated with their high HIV RNA levels (a way to measure the amount of HIV infection). Then, as he administered GcMAF (100 ng. once a week for 18 weeks), all patients’ Nagalase levels gradually went down to control levels, and, in tandem with the Nagalase, viral load went down to zero. Yamamoto wrote that these data “suggest that these patients were free of both HIV virions and HIV-infected cells.”
Professor Yamamoto followed these patients for seven years, and their viral load (HIV-1 RNA), CD4 counts (helper cells, a type of lymphocyte used to evaluate immunocompetence), p24 antigen (HIV-specific antigen), viral culture, and Nagalase levels remained normal. All patients continued to be free of disease. (Note: anemic HIV patients were excluded from this study. Anemia is common in HIV patients. The effect of GcMAF on anemic HIV patients is thus unknown.)
I personally have followed our patients for 3 years after taking the GcMaf protocols, we confirm that all 6 patients remain HIV free, we continue to follow the results until 10 years have been reached. GcMaf continue’s to prove the most effective protocol for HIV.
How your body makes GcMaf:
An illustrated description of the biochemical transformations involved in the synthesis of GcMAF from Vitamin D Binding protein.
How your body makes the GcMAF that activates macrophages and protects you from cancer and viruses
GcMAF and Nagalase are both proteins, so let me start with a brief—and hopefully painless—primer on proteins. You know those birthday present bows made of clusters of curly ribbons? Under a very powerful microscope, proteins look like that. The ribbons are long chains of hundreds of amino acids that make up a protein molecule. Our DNA is programmed to make tens of thousands of different proteins, and what makes them different is the ordering of the amino acids. Each strand (usually there are three or four of them) of curled ribbon in our birthday bow is one of those chains. The curly ribbons are all attached together where the bow is fastened to the present. They may look like a big blob of randomly-placed bands—and in the ribbon, they are. But in a protein, there is a very specific three-dimensional structure, such that even though the curly ribbons look randomly placed, they are, in fact, very precisely positioned—and even slight positional changes will significantly alter the nature of the protein.
Vitamin D-binding protein (DBP) is the precursor protein out of which our immune cells make GcMAF. Up close DBP looks kind of like a small Brillo pad, but the convolutions are not sharp-edged; they’re actually quite soft and sticky. DBP contains 458 amino acids, one of which is very special and quite different from all the others. This is a threonine amino acid, the 420th amino acid in its chain. Attached to this threonine is a group of three sugars. The presence of these sugars defines the purpose of the entire DBP protein molecule. To keep things simple, I am going to name the three sugar molecules after candy bars.
Because Vitamin D Binding Protein comes with sugars attached, we can now refer to it as a glycoprotein. Most of the immune system’s “messenger molecules” are glycoproteins.
Now imagine DBP as this large protein with three sugars (or candy bars) attached. The first is a Hershey’s bar, the second is a Milky Way, and the third is a Snickers. All three are attached to one another, as shown in the diagram, in an upside-down “Y”-shaped configuration.
Vitamin D-Binding Protein (DBP) is the starting point in GcMAF production.
DBP is the protein from which we are going to make GcMAF.
The dashes (–) indicate chemical bonds (pairs of electrons that hold atoms together to form chemicals) that attach the sugars to each other and to the protein.
Making GcMAF from DBP
Now let’s transform our candy bar model of DBP into GcMAF. There are two steps in this process. The first step is to snip off the Milky Way bar. (This is performed by the enzyme beta-galactosidase which is embedded in the outer cell membrane of B-lymphocytes.) You can go ahead and eat it; we won’t need it anymore. If you don’t want it, your body will just recycle it.Intermediate in GcMAF production.
The second step is to snip off the Snickers bar. (This is performed by the enzyme sialidase, which is located in the outer membrane of T-lymphocyte cells.) (You can have that one too, if you want to get on the fast track to diabetes.)
Now we’re left with a huge protein that has just the remaining Hershey’s hanging off of it. Guess what: this is GcMAF.
By snipping off two of the three sugars (first the Milky Way and then the Snickers bar), we have transformed the Vitamin D-Binding Protein into GcMAF.
It’s fully formed and ready to float off, find a macrophage, lock onto its receptor, and then send a powerful message to the entire cell, telling it to stop watching reruns of Desperate Housewives and get to work beating up microbes and killing cancer cells. And, as you know, when GcMAF talks, macros listen.
Candy bar identities revealed
Just for the record (and for you biochemists in the house) my Hershey’s bar is alpha-N-acetylgalactosamine (GalNAc), the Milky Way is D-galactose, and the Snickers bar is sialic acid (also known as N-acetylneuraminic acid).
Now that we have synthesized some GcMAF, we’ll see—in Chapter 9 how Nagalase sabotages it…
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