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Last Updated May 3rd 2022, 12:41:16 am

Pectasol-c (Modified Citrus Pectin)[1]

Healing Properties

  • Antifibrotic: inhibits or reduces fibrosis (scar tissue).
  • Antitumor (Antitumor, anticancer, Anticancer, Antiproliferative, antiproliferative)
    • Inhibits bladder tumor growth
    • P-MCP is a competitive inhibitor of galectin-3, a carbohydrate-binding protein, which is known to be involved in cancer pathogenesis.[1:1]
    • Modified Citrus Pectin is a natural dietary fiber used prevention and therapy of Urinary Bladder Cancers.[2]
  • Antiinflammatory
    • Heart Health: promotes reduction of cardiac inflammation.[3]
  • Blood Health
    • Inhibits galectin-3-mediated hemagglutination (clumping together of red blood cells).[3:1]
  • Endothelial Health
    • Prevents atherosclerosis (the deposition of plaques of fatty material on their inner walls of the arteries).[3:2]

Disease / Symptom Treatment

  • Cancer
    • Bladder Cancer
      • Modified Citrus Pectin has remarkable inhibitory effects on Urinary Bladder Cancer cell proliferation and survival.[2:1]
      • Modified Citrus Pectin is a competitive inhibitor of galectin-3, which is upregulated in Urinary Bladder Cancers.
    • Prostate Cancer
      • Pectasol-C helps treat biochemically relapsed prostate cancer progression.[1:2]
  • Fibrosis (the accumulation of scar tissue)
    • attenuation of organ fibrosis.[3:3]

  1. Title: 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
    Author(s): Daniel Keizman, Moshe A. Frenkel, Avivit Peer, Eli Rosenbaum, David Margel, David Leonid Sarid, Victoria Neiman, Maya Gottfried, Natalie Maimon, Ilan Leibovitch, Hadas Dresler, Isaac Eliaz
    Institution(s): Meir Medical Center, Kfar-Saba, Israel; Rambam Health Care Campus, Haifa, Israel; Davidoff Cancer Center, Petah Tikva, Israel; Ichilov Medical Center, Tel Aviv, Israel; Lung Cancer Unit, Meir Medical Center, Kfar-Saba, Israel; Amitabha Medical Clinic and Healing Center, Santa Rosa, CA;
    Publication: Journal of Clinical Oncology
    Date: February 20 2018
    Abstract: Background: 30% of pts with localized PC will have a biochemical relapse post local tx. The optimal tx of these pts remains elusive. While androgen deprivation therapy is effective in reducing PSA level, its long-term benefit on survival remain undefined, and it is associated with significant cumulative toxicities.Thus, evaluation of new non-toxic compounds in this pt population is warranted. P-MCP is a competitive inhibitor of galectin-3, a carbohydrate-binding protein, which is known to be involved in cancer pathogenesis. Pre-clinical and clinical data suggest that P-MCP is active in PC. We aimed to evaluate the safety and PSA dynamics of tx with P-MCP in pts with BRPC. Methods: Pts with non-castrate non-metastatic BRPC were enrolled in a prospective phase 2 study of tx with oral P-MCP, at 4.8 grams X 3/day for 6 months (mos). Pts that did not progress clinically, biochemically (PSA), and radiologically, at 6 mos, were treated for subsequent 12 mos. Sample size provided 85% power to assess a decrease in PSA progression rate from 80% (natural history) to 40% (P-MCP tx) at 6 mos. Results: The study was initiated in June 2013. 35 pts were enrolled. Median age was 74 years. Treatment of the primary tumor consisted of surgery in 11% (n = 4), radiation in 69% (n = 24), and both in 20% (n = 7). No pt had tx related grade 3/4 toxicity. One patient withdrew his consent after 1 mos. Of the 34 pts analyzed, 18% (n = 6) had grade 1 toxicity. 62% (n = 21) had a stabilization/decrease of PSA, and negative scans, at 6 mos, and entered the second 12 mos tx phase. A stabilization or improvement (increase) of PSA doubling time was noted in 79% (n = 27) of pts. Disease progression at 6 mos was noted in 38% (n = 13: PSA only 29%, n = 10; PSA and scans 9%, n = 3). Conclusions: The present study suggests a potential benefit of P-MCP tx on progression of BRPC. P-MCP tx is safe.
    Citations: ↩︎ ↩︎ ↩︎

  2. Title: Modified citrus pectin inhibited bladder tumor growth through downregulation of galectin-3
    Author(s): Tian Fang, Dan-dan Liu, He-ming Ning, Dan Liu, Jing-ya Sun, Xiao-jing Huang, Yu Dong, Mei-yu Geng, Shi-feng Yun, Jun Yan & Rui-min Huang
    Institution(s): Department of Comparative Medicine, Jinling Hospital, Clinical School of Medical College of Nanjing University, Nanjing, 210002, China; Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China; State Key Laboratory of Pharmaceutical Biotechnology and MOE Key Laboratory of Model Animals for Disease Study, Model Animal Research Center of Nanjing University, Nanjing, 210061, China;
    Publication: Acta Pharmacologica Sinica
    Date: May 16 2018
    Abstract: Modified citrus pectin (MCP) is a carbohydrate enriched complex, which has been implicated in cancer treatment and prevention. However, the effects of MCP on urinary bladder cancer (UBC) are unknown. In this study, MCP was first tested in T24 and J82 human UBC cells and showed the inhibition of cell viability by the sulforhodamine B (SRB) assay. The MCP-treated UBC cells exhibited G2/M phase arrest with the decrease of Cyclin B1 and phosphorylated Cdc2. Caspase-3 was also activated, leading to the cleavage of Caspase-3 and PARP. We further explored the possible molecular mechanisms upon MCP treatment in UBC cells. Reduction of galectin-3 was observed and followed with the inactivation of Akt signaling pathway. Of note, galectin-3 knockdown by RNA interference recapitulated the MCP-mediated anti-proliferation, cell cycle arrest and apoptosis. Moreover, oral administration of MCP to the T24 xenograft-bearing nude mice inhibited the tumor growth significantly (P < 0.05). Quantification analysis of immunohistochemistry staining for Ki67 and cleaved Caspase-3 confirmed the decrease of proliferation index (P < 0.05) and the increase of apoptosis index (P < 0.01) in 700 mg/kg MCP-fed UBC xenografts. Using the information from TCGA database, we revealed that the overexpression of galectin-3 was associated with high tumor grade with lymph node metastasis, poor overall survival in UBC patients. Considering the remarkable inhibitory effects of MCP on UBC cell proliferation and survival in vitro and in vivo mainly through galectin-3, which is upregulated in UBCs, MCP may become an attractive agent, as a natural dietary fiber, for prevention and therapy of UBCs.
    Citations: ↩︎ ↩︎

  3. Title: Galectin-3 Activation and Inhibition in Heart Failure and Cardiovascular Disease: An Update
    Author(s): Navin Suthahar,1 Wouter C. Meijers,1 Herman H.W. Silljé,1 Jennifer E. Ho,2 Fu-Tong Liu,3 and Rudolf A. de Boer
    Institution(s): University Medical Center Groningen, University of Groningen, Department of Cardiology, PO Box 30.001, 9700 RB Groningen, the Netherlands, Massachusetts General Hospital, Cardiovascular Research Center, Boston, MA, USA, Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan
    Publication: Theranostics
    Date: 2018 Jan 1
    Abstract: Galectin-3 is a versatile protein orchestrating several physiological and pathophysiological processes in the human body. In the last decade, considerable interest in galectin-3 has emerged because of its potential role as a biotarget. Galectin-3 is differentially expressed depending on the tissue type, however its expression can be induced under conditions of tissue injury or stress. Galectin-3 overexpression and secretion is associated with several diseases and is extensively studied in the context of fibrosis, heart failure, atherosclerosis and diabetes mellitus. Monomeric (extracellular) galectin-3 usually undergoes further “activation” which significantly broadens the spectrum of biological activity mainly by modifying its carbohydrate-binding properties. Self-interactions of this protein appear to play a crucial role in regulating the extracellular activities of this protein, however there is limited and controversial data on the mechanisms involved. We therefore summarize (recent) literature in this area and describe galectin-3 from a binding perspective providing novel insights into mechanisms by which galectin-3 is known to be “activated” and how such activation may be regulated in pathophysiological scenarios.
    Citations: ↩︎ ↩︎ ↩︎ ↩︎