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I. Eliaz, E. Weil and B. Wilk, “Integrative Medicine and the Role of Modified Citrus Pectin/Alginates in Heavy Metal Chelation and Detoxification — Five Case Reports,” Forsch Komplementmed. 14(6), 358–364 (2007). PectaSol-C Modified Citrus Pectin, Potassium, Sodium, Dietary Fiber, Vegetable capsule (natural vegetable cellulose, water), stearic acid, magnesium stearate, microcrystalline cellulose, silicon dioxide. PectaSol® Metal Detox exerts a dual action in the body. Algimate® Modified Alginate Complex remains in the digestive tract where it works to bind and eliminate heavy metals and radioactive particles to be eliminated through the stools. PectaSol-C® MCP is absorbed into the circulation from the intestine and works systemically, binding heavy metals and environmental pollutants in the circulation for safe elimination through the urinary system.* R. Di, et al., “Pectic Oligosaccharide Structure-Function Relationships: Prebiotics, Inhibitors of Escherichia coli O157:H7 Adhesion and Reduction of Shiga Toxin Cytotoxicity in HT29 Cells,” Food Chem. 227, 245–254 (2017). Eliaz I, Hotchkiss AT, Fishman ML, Rode D. The effect of modified citrus pectin on urinary excretion of toxic elements. Phytother Res. 2006 Oct;20(10):859–64. DOI: 10.1002/ptr.1953. PMID: 16835878.
GAL3 expression is upregulated in fibrotic lesions in human subjects 63, and the severity of hepatic and lung fibrosis is reduced in GAL3-deficient mice 33, 142, 143, 144, 145. Thus, GAL3 has emerged as a promising therapeutic target for fibrotic diseases. Mechanistically, GAL3 induces a pro-fibrotic macrophage phenotype by interacting with the neutral amino acid transporter CD98 (ref. 123). Likewise, GAL3-secreting macrophages drive myofibroblast differentiation, which ultimately results in scar formation 146. Moreover, ECs and myofibroblasts upregulate GAL3 expression upon their activation 142, 147, 148; this facilitates EMT, apoptosis, myofibroblast proliferation and enhanced production of fibronectin and other proteins found in the extracellular matrix 149, 150, 151. F. Sanchis-Gomar, et al., “Galectin-3, Osteopontin and Successful Aging,” Clin. Chem. Lab. Med. 54(5), 873–877 (2016).Hopefully, this dietary supplement will ultimately be one that lives up to its promise. In the meantime, we will continue to keep an eye on all this has to offer. Z.Y. Zhao, et al., “The Role of Modified Citrus Pectin as an Effective Chelator of Lead in Children Hospitalized with Toxic Lead Levels,” Altern. Ther. Health Med. 14(4), 34–38 (2008).
Meanwhile, animal studies have shown that MCP can reduce galectin-3 levels in rats [ 15]. Could the same be true for humans? And could MCP therefore help to lower galectin-3 levels and improve thinking? Possibly. But of course, further study is needed here. Side Effects of Modified Citrus PectinAs the research on this form of MCP continues, it’s critical to note that, in the nutraceutical world, MCP is not a carefully defined term. Experts emphasise that other “modified” citrus pectins do not offer the same benefits as the only researched, clinically studied and substantiated MCP. D. Keizman, et al., Effect of Pectasol-C Modified Citrus Pectin (P-MCP) Treatment (tx) on PSA Dynamics in Non-Metastatic Biochemically Relapsed Prostate Cancer (BRPC) Patients (pts): Results of a Prospective Phase II Study,” J. Clin. Oncol. 36(6), 14 (2018). Artibani W., Porcaro A.B., De Marco V., Cerruto M.A., Siracusano S. Management of Biochemical Recurrence after Primary Curative Treatment for Prostate Cancer: A Review. Urol. Int. 2017;100:251–262. doi: 10.1159/000481438.
There were also no negative side effects observed in a clinical trial involving children with lead toxicity in China. For three months, the hospitalized children between the ages of 5 and 12 were given 15 g of MCP in three divided doses a day [ 4]. C. Ramachandran, et al., “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. 11, 59 (2011). Several published studies demonstrate the synergistic properties of the correct, original MCP and highlight its ability to enhance the benefits of other pharmaceutical and nutraceutical compounds and ingredients. Because of its interactions with Gal-3 and its ability to break Gal-3’s profibrotic lattice formation, it is hypothesised that this MCP can support other therapies in part by allowing treatments to better reach target tissues. Continued studies suggest that MCP offers significant synergistic enhancement potential when added to formulas for cellular health, cardiovascular health, immunity and other areas. Not unlike most substances, there can be potential downsides to taking modified citrus pectin. MCP’s main side effects include cramping and diarrhea. These generally resolve once MCP is discontinued [ 5, 7, 10]. Plant-derived polysaccharides have also been proposed as therapeutics for liver, kidney and lung fibrosis, mainly via mechanisms that involve inhibition of GAL3 (refs. 142, 146). Inhibition of GAL3 with belapectin ( 18, Fig. 4) and Davanat ( 19, Fig. 4) was first evaluated in a toxin-induced model of liver fibrosis 232. Intraperitoneal administration of these polysaccharides resulted in decreased collagen content, attenuated liver fibrosis, diminished cirrhosis and a reduced percentage of GAL3-expressing macrophages 232. These two inhibitors were also tested in a murine model of NASH 233. Intravenous administration of belapectin resulted in a substantial reduction in collagen deposition, hepatocellular damage, NASH activity and fibrosis — features that were associated with reduced markers of inflammation that included inducible nitric oxide synthase (iNOS) and CD36 + pro-inflammatory macrophages. By contrast, administration of Davanat had no effect 233. A phase I clinical trial of belapectin ( 18) in patients with NASH with advanced hepatic fibrosis revealed no toxicity and good tolerability 234 (NCT01899859, Table 1). Two phase II clinical trials evaluated the efficacy of this compound in liver fibrosis. In patients with NASH with advanced fibrosis (NCT02421094, Table 1), belapectin had no significant effects on levels of non-invasive biomarkers of liver inflammation or fibrosis over a 4-month period 234. In liver fibrosis and resultant portal hypertension in patients with NASH cirrhosis 235 (NCT02462967, Table 1), belapectin had no impact on fibrosis or nonalcoholic fatty liver disease activity score. However, in a patient subgroup it showed a significant effect on portal pressure and prevented the development of oesophageal varices, which is an early sign of serious complications in patients with cirrhosis. This led to the development of a phase IIb/III trial designed to evaluate its safety and efficacy specifically in patients with NASH-associated cirrhosis for the prevention of oesophageal varices (NCT04365868, Table 1).
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Given that the functions of galectins vary between the intracellular and extracellular compartments 16, 46, Stegmayr et al. 209 investigated the intracellular activity and membrane permeability of selected small-molecule GAL3 inhibitors including compounds GB1107 ( 2), GB0139 ( 11) and a 1 H-1,2,3-triazol-1-yl TDG derivative 210. Inhibitor uptake and intracellular potency correlated with the polar surface area of the compounds, which is a determinant for passive membrane permeability. Of the compounds investigated, GB1107 was the most potent, although GB0139 had increased intracellular activity following pre-incubation, suggesting that it can reach the cytosolic compartment given sufficient time to cross the plasma membrane 209. Thus, small-molecule galectin inhibitors that can cross the cell membrane, such as GB0139, are important tools to discern extracellular and intracellular functions of galectins, and could potentially be used to target intracellular galectins. Polysaccharides and derivatives
Mucin-type O-glycosylation is initiated by the actions of polypeptide N-acetylgalactosamine transferases (ppGalNAcTs). Synthesis of core 1 O-glycan structures (Galβ(1–3)GalNAc) is initiated by C1GALT1 (core 1 β(1–3)-galactosyltransferase 1), assisted by the chaperone protein, COSMC. Although both GAL1 and GAL3 can recognize core 1 structures, GAL3 binds with higher affinity. Core 1 can be sialylated by β-galactoside-α(2–3) sialyltransferase 1 (ST3GAL1), elongated or branched. Branching by N-acetylglucosaminyltransferases such as C2GNT1 results in a core 2 O-glycan structure, which can be further elongated by GALTs, generating LacNAc residues. Functional roles of GAL1 have been associated with binding to both core 1 and extended core 2 O-glycans. Unmodified citrus pectin does not have the same short, systemically available polysaccharide chains as MCP … and thus remains in the gastrointestinal (GI) tract. And other “modified” pectins may simply indicate that the pectin has been altered in some way, but doesn’t contain the shorter polysaccharide chains and molecular structure required for efficacy. R.A. de Boer, et al., “The Fibrosis Marker Galectin-3 and Outcome in the General Population,” J. Intern. Med. 272(1), 55–64 (2012). Converting glycan-encoded information into biological programmes relies, at least in part, on the contributions of endogenous glycan-binding proteins or lectins 6. The three major lectin families that have decisive roles in shaping both inflammatory and tumour microenvironments are sialic acid-binding immunoglobulin-like lectins (Siglecs), C-type lectin receptors (including selectins 14) and galectins. Galectins are a family of soluble lectins that share affinity for β-galactoside-containing saccharides 15. Examples of some natural ligands for mammalian galectins are summarized in Box 1. Galectins might be involved in the transition from healthy to neoplastic or inflamed tissues and contribute to the persistence of these pathological conditions via both intracellular and extracellular mechanisms 16, 17. Galectins also influence most hallmarks of tumour progression 17 and modulate resistance to numerous anticancer treatments, including immunotherapy, chemotherapy, radiotherapy, targeted therapies and anti-angiogenic therapy 18. Furthermore, galectins might contribute to regulatory circuits that amplify, sustain or alleviate tissue fibrosis and inflammation by selectively targeting different cell types and their microenvironments 16, 19, 20, 21. Accordingly, these glycan-binding proteins have been proposed as therapeutic targets in a broad range of pathological conditions and are currently under clinical evaluation.According to a fast-growing body of published data, a major target has been found. More than 8000 studies show that the carbohydrate binding protein, galectin-3 (Gal-3), serves as a primary therapeutic target for the prevention and treatment of our most critical conditions, effectively meeting this growing demand in chronic disease management.
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