21 april 2012: onder dit artikel is een referentielijst toegevoegd van studies gedaan met Q-10

J Am Acad Dermatol. 2006 Feb;54(2):234-41. Epub 2005 Dec 27.

Het natuurlijke niveau van Q-10 in het bloed van melanoompatiënten lijkt een onafhankelijke en betrouwbare voorspeller voor de kans op het krijgen van wel of geen recidief blijkt uit een gerandomiseerde studie met totaal 220 deelnemers. Hoe lager het niveau van Q-10 in het bloed hoe groter de kans op een recidief of progressie van de ziekte. Wie onderstaand abstract leest begrijpt nu denk ik ook beter waarom orthomoleculaire artsen altijd Q-10 voorschrijven aan kankerpatiënten. Waarom de reguliere oncologie daar nog niet aan wil is ons een raadsel gezien de vele studies met Q-10 en de positieve effecten daarvan. En dit geldt algemeen voor alle kankerpatiënten en niet alleen voor in dit geval melanoompatiënten.

RESULTATEN: CoQ10 waarden waren significant lager bij de patientengroep dan in de controlegroep (t test: P < .0001) en ook significant lager bij patiënten die uitzaaiïngen hadden ontwikkeld dan in de uitzaaiïngenvrije subgroep (t test: P < .0001). Logistische regressie analyse duidt erop dat plasma CoQ10 waarden significante voorspellers van uitzaaiïngen zijn (P = .0013). De odds ratio voor gevorderde ziekte (met utizaaiïngen dus) in patiënten met CoQ10 waarden welke lager waren dan 0.6 mg/L (het laagste-eindpunt van de schaal gemeten in een normale populatie) was 7.9, en de uitzaaiïngenvrije intervalperiode was bijna het dubbele bij patiënten met CoQ10 waarden van 0.6 mg/L of hoger (Kaplan-Meier analyse: P < .001)

Am Acad Dermatol. 2006 Feb;54(2):234-41. Epub 2005 Dec 27.

Low plasma coenzyme Q10 levels as an independent prognostic factor for melanoma progression.

Rusciani L, Proietti I, Rusciani A, Paradisi A, Sbordoni G, Alfano C, Panunzi S, De Gaetano A, Lippa S. Department of Dermatology, Catholic University of the Sacred Heart, Rome, Italy.

BACKGROUND: Abnormally low plasma levels of coenzyme Q10 (CoQ10) have been found in patients with cancer of the breast, lung, or pancreas.

OBJECTIVE: A prospective study of patients with melanoma was conducted to assess the usefulness of CoQ10 plasma levels in predicting the risk of metastasis and the duration of the metastasis-free interval.

METHODS: Between January 1997 and August 2004, plasma CoQ10 levels were measured with high-performance liquid chromatography in 117 consecutive melanoma patients without clinical or instrumental evidence of metastasis according to American Joint Committee on Cancer criteria and in 125 matched volunteers without clinically suspect pigmented lesions. Patients taking CoQ10 or cholesterol-lowering medications and those with a diagnosis of diabetes mellitus were excluded from the study. Multiple statistical methods were used to evaluate differences between patients and control subjects and between patients who did (32.5%) and did not (67.5%) develop metastases during follow-up.

RESULTS: CoQ10 levels were significantly lower in patients than in control subjects (t test: P < .0001) and in patients who developed metastases than in the metastasis-free subgroup (t test: P < .0001). Logistic regression analysis indicated that plasma CoQ10 levels were a significant predictor of metastasis (P = .0013). The odds ratio for metastatic disease in patients with CoQ10 levels that were less than 0.6 mg/L (the low-end value of the range measured in a normal population) was 7.9, and the metastasis-free interval was almost double in patients with CoQ10 levels 0.6 mg/L or higher (Kaplan-Meier analysis: P < .001).

LIMITATIONS: A study with a larger sample, which is currently being recruited, and a longer follow-up will doubtlessly increase the statistical power and enable survival statistics to be obtained.

CONCLUSIONS: Analysis of our findings suggests that baseline plasma CoQ10 levels are a powerful and independent prognostic factor that can be used to estimate the risk for melanoma progression.

PMID: 16443053 [PubMed - indexed for MEDLINE]

References
  • Kessenbrock K, Plaks V, Werb Z. Bicknell R: Matrix Metalloproteinases: regulators of the tumor microenvironment. Cell. 2010;141:52–67. doi: 10.1016/j.cell.2010.03.015. [PMC free article] [PubMed] [Cross Ref]
  • Roy R, Yang J, Moses MA. Matrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer. J Clin Oncol. 2009;27:5287–97. doi: 10.1200/JCO.2009.23.5556. [PMC free article] [PubMed] [Cross Ref]
  • Qian Q, Wang Q, Zhan P, Peng L, Wei SZ, Shi Y. The role of matrix metalloproteinase 2 on the survival of patients with non-small cell lung cancer: a systematic review with meta-analysis. Cancer Invest. 2010;28:661–9. doi: 10.3109/07357901003735634. [PubMed] [Cross Ref]
  • Ala-aho R, Kähäri VM. Collagenases in cancer. Biochimie. 2005;87:273–86. doi: 10.1016/j.biochi.2004.12.009. [PubMed] [Cross Ref]
  • Brown NS, Bicknell R. Hypoxia and oxidative stress in breast cancer Oxidative stress: its effects on the growth, metastatic potential and response to therapy of breast cancer. Breast Cancer Res. 2001;3:323–7. doi: 10.1186/bcr315. [PMC free article] [PubMed] [Cross Ref]
  • Wu WS. The signaling mechanism of ROS in tumor progression. Cancer Metastasis Rev. 2006;25:695–705. doi: 10.1007/s10555-006-9037-8. [PubMed] [Cross Ref]
  • Shekelle P, Hardy ML, Coulter I, Udani J, Spar M, Oda K. Effect of the supplemental use of antioxidants vitamin C, vitamin E, and coenzyme Q10 for the prevention and treatment of cancer. Evid Rep Technol Assess (Summ) 2003;75:1–3. [PubMed]
  • Yuvaraj S, Premkumar VG, Vijayasarathy K, Gangadaran SG, Sachdanandam P. Ameliorating effect of coenzyme Q10, riboflavin and niacin in tamoxifen-treated postmenopausal breast cancer patients with special reference to lipids and lipoproteins. Clin Biochem. 2007;40:623–8. doi: 10.1016/j.clinbiochem.2007.02.003. [PubMed] [Cross Ref]
  • Adhikary A, Mohanty S, Lahiry L, Hossain DM, Chakraborty S, Das T. Theaflavins retard human breast cancer cell migration by inhibiting NF-kappaB via p53-ROS cross-talk. FEBS Lett. 2010;584:7–14. doi: 10.1016/j.febslet.2009.10.081. [PubMed] [Cross Ref]
  • Chao HP, Kuo CD, Chiu JH, Fu SL. Andrographolide Exhibits Anti-Invasive Activity against Colon Cancer Cells via Inhibition of MMP2 Activity. Planta Med. 2010. in press . [PubMed]
  • Bentinger M, Brismar K, Dallner G. The antioxidant role of coenzyme Q. Mitochondrion. 2007. pp. S41–50. Epub 2007 Mar 16. [PubMed] [Cross Ref]
  • Littarru GP, Tiano L. Clinical aspects of coenzyme Q10: an update. Nutrition. 2010;26:250–4. doi: 10.1016/j.nut.2009.08.008. [PubMed] [Cross Ref]
  • Portakal O, Ozkaya O, Erden Inal M, Bozan B, Kosan M, Sayek I. coenzyme Q10 concentrations and antioxidant status in tissues of breast cancer patients. Clin Biochem. 2000;33:279–284. doi: 10.1016/S0009-9120(00)00067-9. [PubMed] [Cross Ref]
  • Hertz N, Lister RE. Improved survival in patients with end-stage cancer treated with coenzyme Q(10) and other antioxidants: a pilot study. J Int Med Res. 2010;38:293.
  • Sachdanandam P. Antiangiogenic and hypolipidemic activity of coenzyme Q10 supplementation to breast cancer patients undergoing Tamoxifen therapy. Biofactors. 2008;32:151–9. doi: 10.1002/biof.5520320118. [PubMed] [Cross Ref]
  • Premkumar VG, Yuvaraj S, Vijayasarathy K, Gangadaran SG, Sachdanandam P. Effect of coenzyme Q10, riboflavin and niacin on serum CEA and CA 15-3 levels in breast cancer patients undergoing tamoxifen therapy. Biol Pharm Bull. 2007;30:367–70. doi: 10.1248/bpb.30.367. [PubMed] [Cross Ref]
  • Premkumar VG, Yuvaraj S, Sathish S, Shanthi P, Sachdanandam P. Anti-angiogenic potential of CoenzymeQ10, riboflavin and niacin in breast cancer patients undergoing tamoxifen therapy. Vascul Pharmacol. 2008;48:191–201. doi: 10.1016/j.vph.2008.02.003. [PubMed] [Cross Ref]
  • Rusciani L, Proietti I, Rusciani A, Paradisi A, Sbordoni G, Alfano C. Low plasma coenzyme Q10 levels as an independent prognostic factor for melanoma progression. J Am Acad Dermatol. 2006;54:234–41. doi: 10.1016/j.jaad.2005.08.031. [PubMed] [Cross Ref]
  • Ito T, Ito M, Shiozawa J, Naito S, Kanematsu T, Sekine I. Expression of the MMP-1 in human pancreatic carcinoma: relationship with prognostic factor. Mod Pathol. 1999;12:669–74. [PubMed]
  • Cheng CJ, Lin YC, Tsai MT, Chen CS, Hsieh MC, Chen CL. SCUBE2 suppresses breast tumor cell proliferation and confers a favorable prognosis in invasive breast cancer. Cancer Res. 2009;69:3634–41. doi: 10.1158/0008-5472.CAN-08-3615. [PubMed] [Cross Ref]
  • Bogani P, Canavesi M, Hagen TM, Visioli F, Bellosta S. Thiol supplementation inhibits metalloproteinase activity independent of glutathione status. Biochem Biophys Res Commun. 2007;363:651–5. doi: 10.1016/j.bbrc.2007.09.018. [PubMed] [Cross Ref]
  • Griffith OW. Biologic and pharmacologic regulation of mammalian glutathione synthesis. Free Radic Biol Med. 1999;27:922–35. doi: 10.1016/S0891-5849(99)00176-8. [PubMed] [Cross Ref]
  • Pei P, Horan MP, Hille R, Hemann CF, Schwendeman SP, Mallery SR. Reduced nonprotein thiols inhibit activation and function of MMP-9: implications for chemoprevention. Free Radic Biol Med. 2006;41:1315–24. doi: 10.1016/j.freeradbiomed.2006.07.014. [PMC free article] [PubMed] [Cross Ref]
  • Das S, Banerji A, Frei E, Chatterjee A. Rapid expression and activation of MMP-2 and MMP-9 upon exposure of human breast cancer cells (MCF-7) to fibronectin in serum free medium. Life Sci. 2008;82:467–76. doi: 10.1016/j.lfs.2007.12.013. Epub 2007 Dec 27. [PubMed] [Cross Ref]
  • Rosenkranz AR, Schmaldienst S, Stuhlmeier KM, Chen W, Knapp W, Zlabinger GJ. A microplate assay for the detection of oxidative products using 2',7'-dichlorofluorescin-diacetate. J Immunol Methods. 1992;156:39–45. doi: 10.1016/0022-1759(92)90008-H. [PubMed] [Cross Ref]
  • Factor VM, Kiss A, Woitach JT, Wirth PJ, Thorgeirsson SS. Disruption of redox homeostasis in the transforming growth factor-alpha/c-myc transgenic mouse model of accelerated hepatocarcinogenesis. J Biol Chem. 1998;273:15846–53. doi: 10.1074/jbc.273.25.15846. [PubMed] [Cross Ref]
  • Kupai K, Szucs G, Hajdu I, Csonka C, Csont T. Matrix metalloproteinase activity assays: Importance of zymography. J Pharmacol Toxicol Methods. 2010;61:205–9. doi: 10.1016/j.vascn.2010.02.011. [PubMed] [Cross Ref]
  • Khorramizadeh MR, Pezeshki M, Ghahary A, Zeraati H, Berahmeh A. Determination of gelatinase A using a modified indirect hemagglutination assay in human prostate cancer screening and assessment of its correlation with prostate-specific antigen parameters. Int J Urol. 2005;12:637–43. doi: 10.1111/j.1442-2042.2005.01094.x. [PubMed] [Cross Ref]
  • Das S, Banerji A, Frei E, Chatterjee A. Rapid expression and activation of MMP-2 and MMP-9 upon exposure of human breast cancer cells (MCF-7) to fibronectin in serum free medium. Life Sci. 2008;82:467–76. doi: 10.1016/j.lfs.2007.12.013. [PubMed] [Cross Ref]
  • Ortega A, Ferrer P, Carretero J, Obrador E, Asensi M, Pellicer JA. Down-regulation of glutathione and Bcl-2 synthesis in mouse B16 melanoma cells avoids their survival during interaction with the vascular endothelium. J Biol Chem. 2003;278:39591–9. doi: 10.1074/jbc.M303753200. [PubMed] [Cross Ref]
  • Nelson KK, Melendez JA. Mitochondrial redox control of matrix metalloproteinases. Free Radic Biol Med. 2004;37:768–84. doi: 10.1016/j.freeradbiomed.2004.06.008. [PubMed] [Cross Ref]
  • Sandhya T, Mishra KP. Cytotoxic response of breast cancer cell lines, MCF 7 and T 47 D to triphala and its modification by antioxidants. Cancer Lett. 2006;238:304–13. doi: 10.1016/j.canlet.2005.07.013. [PubMed] [Cross Ref]
  • Voronkina IV, Kirpichnikova KM, Smagina LV, Gamaliĭ IA. Changes in matrix metalloproteinases activities in normal and transformed mouse fibroblasts under effect of antioxidants. Tsitologiia. 2008;50:877–81. [PubMed]
  • Bogani P, Canavesi M, Hagen TM, Visioli F, Bellosta S. Thiol supplementation inhibits metalloproteinase activity independent of glutathione status. Biochem Biophys Res Commun. 2007;363:651–5. doi: 10.1016/j.bbrc.2007.09.018. [PubMed] [Cross Ref]
  • Tyagi SC, Kumar S, Borders S. Reduction-oxidation (redox) state regulation of extracellular matrix metalloproteinases and tissue inhibitors in cardiac normal and transformed fibroblast cells. J Cell Biochem. 1996;61:139–51. doi: 10.1002/(SICI)1097-4644(19960401)61:1<139::AID-JCB15>3.0.CO;2-J. [PubMed] [Cross Ref]
  • Lazo JS, Kuo SM, Woo ES, Pitt BR. The protein thiol metallothionein as an antioxidant and protectant against antineoplastic drugs. Chem Biol Interact. 1998;111-112:255–262. doi: 10.1016/S0009-2797(97)00165-8. [PubMed] [Cross Ref]
  • Brenneisen P, Briviba K, Wlaschek M, Wenk J, Scharffetter-Kochanek K. Hydrogen peroxide (H2O2) increases the steady-state mRNA levels of collagenase/MMP-1 in human dermal fibroblasts. Free Radic Biol Med. 1997;22:515–24. doi: 10.1016/S0891-5849(96)00404-2. [PubMed] [Cross Ref]
  • Wenk J, Brenneisen P, Wlaschek M, Poswig A, Briviba K, Oberley TD. Stable overexpression of manganese superoxide dismutase in mitochondria identifies hydrogen peroxide as a major oxidant in the AP-1-mediated induction of matrix-degrading metalloprotease-1. J Biol Chem. 1999;274:25869–76. doi: 10.1074/jbc.274.36.25869. [PubMed] [Cross Ref]
  • Schmelzer C, Lindner I, Rimbach G, Niklowitz P, Menke T, Döring F. Functions of coenzyme Q10 in inflammation and gene expression. Biofactors. 2008;32:179–83. doi: 10.1002/biof.5520320121. [PubMed] [Cross Ref]
  • Factor VM, Kiss A, Woitach JT, Wirth PJ, Thorgeirsson SS. Disruption of redox homeostasis in the transforming growth factor-alpha/c-myc transgenic mouse model of accelerated hepatocarcinogenesis. J Biol Chem. 1998;273:15846–53. doi: 10.1074/jbc.273.25.15846. [PubMed] [Cross Ref]
  • Linnane AW, Kios M, Vitetta L. Coenzyme Q10 - its role as a prooxidant in the formation of superoxide anion/hydrogen peroxide and the regulation of the metabolome. Mitochondrion. 2007. pp. S51–61. Epub 2007 Mar 30. [PubMed] [Cross Ref]
  • Abbasi N, Khaghani S, Sharif-Tabrizi A, Farzami B, Vardasbi S, Bahar M. et al. Comparison of Lipoamide dehydrogenase activity in HL-60 Leukemia cells and normal lymphocyte. Acta Medica Iranica. 2007;45:282–284.

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