sunnuntai 26. helmikuuta 2017

GcMAF Goleic Therapy - 4 Verita Life Clinical Programmes

Macrophages are large immune cells found in
our bodies that are able 
to recognise, engulf and
digest cancer cells. 

Also responsible for stimulating other immune cells, 
macrophages can be activated by ‘MAF’
(macrophage activating factor), a naturally 
protein. The precursor of MAF inside the body is called
Gc protein.

How Tumours prevent Macrophages

Tumour cells produce nagalase, a special enzyme inhibiting the
Gc protein’s function leading to high nagalase levels resulting in lower
MAF levels. The body’s macrophages subsequently cannot be activated,
leading to the suppression of the immune system.
Complementary oncology utilises breakthrough GcMAF therapy to
counteract this effect and enhance the immune system.

GcMAF Goleic Therapy

GcMAF therapy regulates the human protein required to reactivate immune
cells and boost patients’ immune systems. Many published peer reviewed
studies have proven that GcMAF Goleic therapy is not only an immune
activator, but can be used as a natural cancer treatment. In addition
to rebuilding a diminished immune system, GcMAF Goleic inhibits
angiogenesis (stops blood supply to tumours), activates macrophages
and apoptosis (suicide of cancer cells); reverts cancer cells’ phenotype
(characteristics) to normal healthy cells; reduces the metastatic
potential of human cancer cells and increases energy production at
the mitochondrial level.

The treatments available at Verita Life >

GcMAF Goleic is one of 15 separate core cancer treatments that can be
combined into your personal protocol.

The exact combination and frequency of treatments is planned
according to your specific needs.

Chosen for proven effectiveness, every treatment has been shown, through
numerous medical studies and extensive experience, to attack and defeat
cancer cells.
Following your enquiry and review of your case by our medical team, you
will receive a Doctor consultation.
A full personalised protocol will follow and this will recommend the
treatments needed. 

Treatments are delivered in 4 Verita Life Clinical Programmes

Whatever phase of treatment, or Stage you are at, Verita Life can help treat your
Cancer and your cancer-related symptoms.
GcMAF Goleic and the other treatments are combined and delivered in 4 separate
Clinical Programmes, one of which is best for you, or your loved one.
1. If you are currently having Chemo or Radio therapy – maximise results
and minimise side effects. Verita Life Oncoboost™ protects your organs and
boosts your immune system.
2. If you are looking for Alternative treatments to defeat cancer
– Verita Life 360 ™
– Complete treatment protocols combining cancer-specific treatments if you don’t
 want to, or can’t, undergo conventional treatments.
3. If you have not started treatment yet – Prepare your Immune system and
organs to withstand chemo and radio therapy with uniquely combined treatment protocols.
 Verita BodyBoost™.
4. If you are in remission. Recover from cancer side effects with All Clear Aftercare™
– rebuild a weakened immune system and damaged organs.
Regain your health and prevent cancer returning.


1. We treat the cancer and support the immune system at the same time.
2. We ensure a diet and lifestyle change so that patients remove the conditions
that promoted or supported tumour growth.
3. We give patients a chance to heal or maintain the status quo, even when
conventional medicine has given up.
4. In almost all cases, we achieve a stronger immune system and improved
quality of life.

 (or Gc protein-derived macrophage activating factor)[1] is a protein
produced by modification of 
vitamin D-binding protein. Proponents of GcMAF claim
that it is an 
immunomodulatory protein that has antitumor properties and strengthens
immune system bymacrophage activation.[2][3] /Wikipedia

Gene Review

Gc  -  group specific component

Mus musculus

Synonyms: DBP, Gc-globulin, Group-specific component, VDB, Vitamin D-binding protein, ...

 Hoffmann, R. A w iki for the life sciences w here authorship matters. Nature Genetics (2008)

Disease relevance of Gc

When maintained on vitamin D-deficient diets for a brief period, the DBP-/-, but not DBP+/+, mice developed secondary hyperparathyroidism and the accompanying bone changes associated with vitamin D deficiency [1].
Osteopathy and resistance to vitamin D toxicity in mice null for vitamin D binding protein [1].
After an overload of vitamin D, DBP-/- mice were unexpectedly less
susceptible to hypercalcemia and its toxic effects [1].
Specific forms of renal Fanconi syndrome are associated with endocytic
pathway dysfunction with disruption of megalin-mediated uptake DBP/25- (OH)D3 complex, producing metabolic bone disease in affected individuals as a prominent clinical finding [2].
Prognostic utility of serum alpha-N-acetylgalactosaminidase and
immunosuppression resulted from deglycosylation of serum Gc protein in oral cancer patients [3].

Psychiatry related information on Gc
Mice homozygous for a DBP-null allele display less locomotor activity and free-run with a shorter period than otherwise isogenic wild-type animals [4].

High impact information on Gc
We show that 25-(OH) vitamin D3 in complex with its plasma carrier, the vitamin D-binding protein, is filtered through the glomerulus and reabsorbed in the proximal tubules by the endocytic receptor megalin [5].
BACKGROUND: The vitamin D(3)-binding protein (Gc protein)-derived
macrophage activating factor (GcMAF) activates tumoricidal macrophages against a variety of cancers indiscriminately [6].
Peak steady-state mRNA levels of the vitamin D-dependent calbindin-D9K gene were induced by 1,25(OH)2D more rapidly in the DBP-/- mice [1].
A line of mice deficient in vitamin D binding protein (DBP) was generated by targeted mutagenesis to establish a model for analysis of DBP's biological functions in vitamin D metabolism and action [1].
Thus, the role of DBP is to maintain stable serum stores of vitamin D
metabolites and modulate the rates of its bioavailability, activation, and endorgan responsiveness [1].

Chemical compound and disease context of Gc
Phthalate esters with short alkyl chains, such as di-ethyl (DEP), di-n-propyl (DPP), and di-butyl phthalate (DBP), have adjuvant effects on an FITCinduced contact hypersensitivity mouse model [7].

Biological context of Gc
The fourth gene, Gc, encoding vitamin D-binding protein or group-specific component, maps to the same chromosome as the other family members, but linkage has not been established [8].
This report describes the genetic and physical mapping of Gc in mouse and establishes that, although Gc is genetically linked to the other genes, its physical distance from them extends beyond the resolution range of yeast artificial chromosome cloning and pulsed-field gel electrophoresis [8].
Population gene frequencies for these proteins binding vitamin D were in the range of those reported for Gc, and individuals of known Gc phenotype were found to have the corresponding vitamin-D-binding phenotype [9].
Vitamin D-binding protein (DBP) has been reported to contribute to innate immunity [10].
Anti-megalin antibodies produced a similar reduction in DBP/25-(OH)D3
endocytosis [2].
Anatomical context of Gc
Initial studies revealed a marked defect in the ability of these DBP(-/-) mice to recruit cells to the peritoneum after localized thioglycolate injection [10].
To verify prior in vitro and cell-based observations supporting this role, we assessed the ability of a recently developed DBP-null mouse line to recruit neutrophils and macrophages to a site of chemical inflammation [10].
The interrupted DBP allele had been generated by homologous recombination in 129X1/SvJ embryonic stem cells and these cells were subsequently used to generate a line of DBP(-/-) (null) mice [10].
Analysis of intercellular signal transmission among nonadherent (B and T) cells revealed that lyso-PC-treated B cells modify Gc protein to yield a proactivating factor, which can be converted by T cells to the macrophage activating factor [11].
Identification of the serum factor required for in vitro activation of
macrophages. Role of vitamin D3-binding protein (group specific component, Gc) in lysophospholipid activation of mouse peritoneal macrophages [12].

Associations of Gc with chemical compounds
Three lines of evidence are reported:
(1) Polyacrylamide gel electrophoresis 
and autoradiography of serum labeled with (14-C)vitamin D3 revealed patterns of radioactive bands identical to those expected of the two Gc alleles [9].
Group-specific component (Gc) proteins bind vitamin D and 25-
hydroxyvitamin D [9].
This review describes these new pathways for uptake of 25-hydroxyvitamin- D3 and the gonadal sex-steroids (17beta-estradiol and testosterone) bound to vitamin D-binding protein and sex hormone-binding globulin respectively [13].
This rapid process of macrophage activation was found to require a serum factor, the vitamin D3 binding protein (the human protein is known as group-specific component; Gc) [11].
Vitamin D3-binding protein (Gc protein), a serum glycoprotein, is the
precursor for the macrophage activating factor [3].
Physical interactions of Gc
Recent studies have shown that vitamin D-binding protein (DBP)/25-(OH)D3 complex is one of the megalin/cubilin ligands [2].
The influence of age, sex and strain on the serum concentration of
transcortin (corticosteroid-binding globulin) and vitamin D-binding protein (DBP) in mice was investigated [14].

Other interactions of Gc
Linkage between vitamin D-binding protein and alpha-fetoprotein in the
mouse [8].
In a previous study, the s locus was included in the same linkage group as serum albumin (Alb) and vitamin-D binding protein (GC) which are mapped on chicken (Gallus gallus) chromosome 4 (GGA4) [15].
Incubation of Gc protein with a mixture of beta-galactosidase and sialidase efficiently generated the macrophage-activating factor [11].
The antibody was subtyped IgG2b kappa and had a kd of 3.0 x 10(-8) M for antigen Gc [16].
Transcortin and vitamin D-binding protein levels in mouse serum [14].
Analytical, diagnostic and therapeutic context of Gc
(2) Immunoelectrophoresis and autoradiography of labeled serum reacted against antiserum to human Gc revealed labeling by (14-C)vitamin D3 of Gcantibody precipitation ares [9].
Deglycosylated Gc protein cannot be converted to macrophage activating factor, leading to immunosuppression [3].
Competition assays with vitamin D3 and Gc in enzyme-linked immunosorbent assay indicate that the epitope of hDBP-1 on the Gc molecule may be related to the vitamin-D3-binding site [17].
CONCLUSION: The difference of isoelectric focusing mobility in Gc protein and GcMAF would be useful to develop a GcMAF detection method [18]. Gc protein from human serum was purified by affinity chromatography with 25-hydroxyvitamin D3-sepharose [19].

1. Osteopathy and resistance to vitamin D toxicity in mice null for vitamin D
binding protein. Safadi, F.F., Thornton, P., Magiera, H., Hollis, B.W., Gentile, M.,
Haddad, J.G., Liebhaber, S.A., Cooke, N.E. J. Clin. Invest. (1999)
2. Proximal tubule endocytic apparatus as the specific renal uptake
mechanism for vitamin D-binding protein/25-(OH)D3 complex (Review
Article). Negri, A.L. Nephrology (Carlton, Vic.) (2006)
3. Prognostic utility of serum alpha-N-acetylgalactosaminidase and
immunosuppression resulted from deglycosylation of serum Gc protein in
oral cancer patients. Yamamoto, N., Naraparaju, V.R., Urade, M. Cancer
Res. (1997)
4. The DBP gene is expressed according to a circadian rhythm in the
suprachiasmatic nucleus and influences circadian behavior. Lopez-Molina,
L., Conquet, F., Dubois-Dauphin, M., Schibler, U. EMBO J. (1997)
5. An endocytic pathway essential for renal uptake and activation of the
steroid 25-(OH) vitamin D3. Nykjaer, A., Dragun, D., Walther, D., Vorum, H.,
Jacobsen, C., Herz, J., Melsen, F., Christensen, E.I., Willnow, T.E. Cell (1999)
6. Effects of vitamin D(3)-binding protein-derived macrophage activating
factor (GcMAF) on angiogenesis. Kanda, S., Mochizuki, Y., Miyata, Y.,
Kanetake, H., Yamamoto, N. J. Natl. Cancer Inst. (2002)
7. Effects of phthalate esters on dendritic cell subsets and interleukin-4
production in fluorescein isothiocyanate-induced contact
hypersensitivity. Maruyama, T., Shiba, T., Iizuka, H., Matsuda, T., Kurohane,
K., Imai, Y. Microbiol. Immunol. (2007)
8. Linkage between vitamin D-binding protein and alpha-fetoprotein in the
mouse. Guan, X.J., Arhin, G., Leung, J., Tilghman, S.M. Mamm. Genome (1996)
9. Group-specific component (Gc) proteins bind vitamin D and 25-
hydroxyvitamin D. Daiger, S.P., Schanfield, M.S., Cavalli-Sforza, L.L. Proc. Natl.
Acad. Sci. U.S.A. (1975)
10. 129X1/SvJ mouse strain has a novel defect in inflammatory cell
recruitment. White, P., Liebhaber, S.A., Cooke, N.E. J. Immunol. (2002)
11. Vitamin D3 binding protein (group-specific component) is a precursor for
the macrophage-activating signal factor from lysophosphatidylcholinetreated
lymphocytes. Yamamoto, N., Homma, S. Proc. Natl. Acad. Sci.
U.S.A. (1991)
12. Identification of the serum factor required for in vitro activation of
macrophages. Role of vitamin D3-binding protein (group specific
macrophages. Role of vitamin D3-binding protein (group specific
component, Gc) in lysophospholipid activation of mouse peritoneal
macrophages. Yamamoto, N., Homma, S., Millman, I. J. Immunol. (1991)
13. The role of plasma-binding proteins in the cellular uptake of lipophilic
vitamins and steroids. Andreassen, T.K. Horm. Metab. Res. (2006)
14. Transcortin and vitamin D-binding protein levels in mouse serum. Faict, D.,
De Moor, P., Bouillon, R., Heyns, W., Heiniger, H.J., Corrow, D., Lesaffre, E. J.
Endocrinol. (1986)
15. Mapping of panda plumage color locus on the microsatellite linkage map of
the Japanese quail. Miwa, M., Inoue-Murayama, M., Kobayashi, N., Kayang,
B.B., Mizutani, M., Takahashi, H., Ito, S. BMC Genet. (2006)
16. Binding of a monoclonal antibody E12 to Gc globulin (vitamin D-binding
protein) is inhibited by actin. Osawa, M., Sabbatini, A.R., Erukhimov, J.,
Werner, P.A., Galbraith, R.M. Biochim. Biophys. Acta (1992)
17. A monoclonal antibody against human vitamin-D-binding protein for the
analysis of genetic variation in the group-specific component system
(Gc). Hoffmann, R., Braun, A., Cleve, H. Hum. Genet. (1990)
18. Gc protein-derived macrophage activating factor (GcMAF): isoelectric
focusing pattern and tumoricidal activity. Mohamad, S.B., Nagasawa, H.,
Sasaki, H., Uto, Y., Nakagawa, Y., Kawashima, K., Hori, H. Anticancer Res. (2003)
19. Association of the macrophage activating factor (MAF) precursor activity
with polymorphism in vitamin D-binding protein. Nagasawa, H., Sasaki, H.,
Uto, Y., Kubo, S., Hori, H. Anticancer Res. (2004)

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