We often refer to cancer as one disease—but it’s not. Cancer manifests very differently depending on where it originates in the body, the person’s overall health condition, and numerous other individual factors. Despite these variations however, research continues to show that many, if not all cancers, are fueled by one “master alarm” protein in the body: Galectin-3.
And from this growing body of research, a natural anti-galectin-3 solution has also emerged, proving to be an effective tool in the integrative treatment and prevention of cancer and metastasis: The researched form of Modified Citrus Pectin.
Galectin-3: Bodyguard of the Tumor Environment
Cancer starts with regular healthy cells that turn rogue and overwhelm the immune system’s ability to fight them off. Unlike viral or bacterial infections, cancer invades the body from within.
But how does a healthy cell turn cancerous? When a cell gets damaged or ends its normal life cycle, it is supposed to self-destruct to make way for healthy cells—a normal process called “apoptosis”. But cancer forms when these damaged cells refuse to die. Instead of normal apoptosis, they continue to replicate and reproduce more damaged cells. These damaged cells multiply, stick together and form tumors. From there, they can create new blood vessels to feed the tumor (a process called “angiogenesis) and if they’re not stopped, can spread to other organs, aka, “metastasis.”
Out-of-control galectin-3 promotes all of these pro-cancer processes, earning it the title of “Guardian of the tumor microenvironment”. Extensive research shows how galectin-3 fuels the development and spread of numerous types of kinds of cancer.
Importantly, inhibiting the actions of galectin-3 offers a proven strategy for helping to prevent and treat cancer successfully.1
12 Cancers Fueled by Galectin-3
If the diagnosis is cancer, regardless of what kind, galectin-3 is likely to be involved.2 Data links numerous types of cancer directly to galectin-3:
- Breast cancer4
- Gynecological, such as cervical and ovarian cancer5
- Prostate cancer6
- Colon cancer7
- Lung cancer9
- Kidney cancer10
- Liver cancer11
- Bladder cancer12
- Bone cancer13
- Brain cancer14
As research into galectin-3 continues, additional cancer types will surely be added to this list. That’s because galectin-3 triggers a cascade of pro-cancerous actions that can overwhelm your body’s ability to fight the disease—without targeted help that is.
Galectin-3 Triggers Cancer 4 Ways
Cancer starts with damaged, mutated cells that evade apoptosis. Galectin-3 contributes to this original cell damage, by fueling degenerative processes like inflammation. But galectin-3 also helps cancer cells stay alive, grow and spread.
Galectin-3 contributes to initial cellular damage through four distinct mechanisms: 15,16
Fuels chronic inflammation—Chronic inflammation wreaks havoc on cells and contributes to increased wear and tear, and DNA damage. Galectin-3 triggers inflammation and keeps it on, allowing damaged cells to grow and multiply.
Oxidative stress—Oxidative stress in cells can cause mutations found in cancer. Galectin-3 hinders your body’s antioxidant responses to oxidative stress, fueling cellular damage.
Fibrosis—Fibrosis is driven by chronic inflammation, and is characterized by unhealthy scar tissue build-up in organs and systems. This leads to hardening of tissues and organ failure, in addition to cancer growth and progression. Galectin-3 triggers fibrosis and keeps it going, which can lead to the development of different cancers.
Immune suppression—Galectin-3 protects cancer
cells from immune system detection, thus blocking immune cells from effectively eliminating unhealthy and cancerous cells.
In addition to these initial cellular damages, Galectin-3 helps cancers grow and spread to other areas of the body. It does this by actively contributing to distinct pro-cancer mechanisms, including:
- Proliferation—Rapid replication of cancerous cells
- Angiogenesis—Formation of new blood vessels to feed tumors and allow metastasis
- Anti-apoptosis—Evasion of pre-programmed cell death in mutated cells
- Tumor formation—Clumping together of cancer cells into a tumor
- Metastasis—Spread of cancerous cells and subsequent tumor formation in other areas of the body
- Immune evasion—Shielding cancer cells from immune detection
These and other pathogenic processes fueled by galectin-3 make this out-of- control protein an important target for preventing and treating cancer. Research—including double blind clinical studies—continues to show that blocking galectin-3 offers a safe and effective tool for helping to address numerous types of cancer.
This is achievable with the researched form of Modified Citrus Pectin (MCP)
MCP Blocks Galectin-3 in the Fight Against Cancer
When it comes to blocking galectin-3 against cancer, you want the most researched and only available option: clinically proven Modified Citrus Pectin (MCP). This trusted anti-cancer ingredient has been shown repeatedly to halt and even reverse the actions of galectin-3 in the treatment of cancer, as well as numerous other chronic inflammatory conditions.
Modified Citrus Pectin starts as citrus pith, the white part between the peel and the fruit. From there, an advanced enzyme-based modification processes amplifies its healing powers significantly.
In its unmodified state, citrus pectin molecules are too big to enter your circulation, so they simply pass through the GI tract as fiber. However, MCP’s modification process transforms regular citrus pectin into much smaller molecules that can be easily absorbed, and have a unique structure that allows for powerful bioactivity throughout the body.17
When MCP gets to work, it blocks galectin-3 to halt and even reverses its degenerative effects—allowing your natural healing abilities to perform optimally.
By inhibiting galectin-3, MCP effectively treats the inflammation, fibrosis, and oxidative stress that promote cancer as well as other chronic life-threatening conditions like heart disease. At the same time, MCP activates specific immune cells against cancer, including NK and T cells. 18
But that’s not all. The researched form of MCP is also a synergistic complement to other cancer treatments like chemotherapy, immunotherapy, and radiation, as well as botanical anti-cancer formulas. By blocking galectin-3, MCP works to synergize with these and other therapies and increase their effectiveness, supporting greater clinical outcomes.
Research on Modified Citrus Pectin’s Cancer-Fighting Abilities
Researchers and clinicians have been documenting the anti-cancer actions of MCP for decades, with significant results. From cell studies, to animal research to double-blind human clinical trials, published research continues to demonstrate the numerous ways in which MCP acts as one of the most powerful anti-cancer tools we have today.
Here’s a brief summary of some of the research showing how MCP actively supports cancer treatment and improves clinical outcomes:
- Increases NK cell activation by 1,000% and enhances their fighting strength by 54%19
- Inhibits cancer growth by blocking galectin-320
- Supports apoptosis and blocks metastasis21
- Boosts cancer sensitivity to treatments22
- Enhances chemotherapy effects23
- Works synergistically with other botanical compounds to stop the invasive behavior of cancer cells24
The extensive and growing body of research, in addition to 25+ years of clinical success, demonstrate that Modified Citrus Pectin significantly improves your chances of defeating cancer and preventing it from recurring… while supporting long-term from the cellular level on up.
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3. Michalová Z, Čoma M, Kičová M, et al. Overexpression of Galectin-3 in Chronic Lymphocytic Leukemia Is Associated With 17p Deletion: A Short Report. Anticancer Res. 2019;39(6):2805-2810. doi:10.21873/anticanres.13408.
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8. Clark MC, Pang M, Hsu DK, et al. Galectin-3 binds to CD45 on diffuse large B-cell lymphoma cells to regulate susceptibility to cell death. Blood. 2012;120(23):4635-4644. doi:10.1182/blood-2012-06-438234.
9. Buttery R, Monaghan H, Salter DM, Sethi T. Galectin-3: differential expression between small-cell and non-small-cell lung cancer. Histopathology. 2004;44(4):339-344. doi:10.1111/j.1365-2559.2004.01815.
10. Xu Y, Li C, Sun J, Li J, Gu X, Xu W. Antitumor effects of galectin-3 inhibition in human renal carcinoma cells. Exp Biol Med (Maywood). 2016;241(13):1365-1373.
11. Jiang SS, Weng DS, Wang QJ, et al. Galectin-3 is associated with a poor prognosis in primary hepatocellular carcinoma. J Transl Med. 2014;12:273. Published 2014 Sep 27.
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17. Eliaz I. Letter to the Editor: Not all modified citrus pectins are the same: size does matter. Am J Physiol Heart Circ Physiol. 2019;316(5):H1232-H1233. doi:10.1152/ajpheart.00118.2019.
18. Eliaz I, Raz A. Pleiotropic Effects of Modified Citrus Pectin. Nutrients. 2019;11(11):2619.
19. Ramachandran C, Wilk BJ, Hotchkiss A, Chau H, Eliaz I, Melnick SJ. Activation of human T-helper/inducer cell, T-cytotoxic cell, B-cell, and natural killer (NK)-cells and induction of natural killer cell activity against K562 chronic myeloid leukemia cells with modified citrus pectin. BMC Complement Altern Med. 2011;11:59.
20. Fang T, Liu DD, Ning HM, et al. Modified citrus pectin inhibited bladder tumor growth through downregulation of galectin-3. Acta Pharmacol Sin. 2018;39(12):1885-1893.
21.Glinsky VV, Raz A. Modified citrus pectin anti-metastatic properties: one bullet, multiple targets. Carbohydr Res. 2009;344(14):1788-1791.
22. Conti S, Vexler A, Hagoel L, et al. Modified Citrus Pectin as a Potential Sensitizer for Radiotherapy in Prostate Cancer. Integr Cancer Ther. 2018;17(4):1225-1234.
23. Hossein G, Halvaei S, Heidarian Y, et al. Pectasol-C Modified Citrus Pectin targets Galectin-3-induced STAT3 activation and synergize paclitaxel cytotoxic effect on ovarian cancer spheroids. Cancer Med. 2019;8(9):4315-4329. doi:10.1002/cam4.2334.
24. Jiang J, Eliaz I, Sliva D. Synergistic and additive effects of modified citrus pectin with two polybotanical compounds, in the suppression of invasive behavior of human breast and prostate cancer cells. Integr Cancer Ther. 2013;12(2):145-152. doi:10.1177/1534735412442369.