Wednesday, 14 October 2015

The 2nd edition of The holistic Prevention, Management and Treatment of Dementia under The Microscope of Conventional Medicine - The Metals binding proteins

Kyle J. Norton (Scholar)

Health article writer and researcher; Over 10.000 articles and research papers have been written and published on line, including world wide health, ezine articles, article base, healthblogs, selfgrowth, best before it's news, the karate GB daily, etc.,.
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Some articles have been used as references in medical research, such as international journal Pharma and Bio science, ISSN 0975-6299.


Dementia is defined as neuro degeneration syndrome among elder, affecting memory, thinking, orientation, comprehension, calculation, learning capacity, language, and judgement over 47 millions
of worldwide population, mostly in the West. The evaluation of the syndrome by holistic medicine has been lacking, especially through conventional medicine research and studies. The aim of this essay is to provide accurate information of how effective of holistic medicine in prevention, management and treatment of dementia through searching data base of PubMed.
This is the third time, a research paper has been written this way to general public that you will not find any where in the net.

Dementia is a neuropsychiatric disorder induced of cognitive impairment and behavioral disturbances. The behavioral and psychological symptoms of dementia (BPSD) are common, with a progressive loss of memory and other mental abilities, affecting a person's ability to perform usual tasks in everyday life.

Prevention and Management

B. Antioxidants and Dementia
B.2. Metals binding proteins
1. Ceruloplasmin
Ceruloplasmin, the major copper-carrying protein in the blood, plays a role iniron metabolism(227). Decreased level of ceruloplasmin impaired ferroportin stability(229)(230)may induce progressive action tremor, and cognitive decline(227), causing the forming of superoxide anion radicals(231) and iron overload in the brain, liver, pancreas, and other organs(232).

2. Ferritin
Ferritin, the protein produced by almost all living organisms, acts as a component to fight against iron deficiency and iron overload(233)(234). In a soluble and non-toxic form, the protein is transported to the body needs, including organs(236) for enhancement of the immune system in the presence of an infection(237), against proliferation of lymphoid and myeloid cells(235), cancer(238) and prevention of the infectious agent in attempt of binding iron to form free radicals(239) in most cellular oxidation reactions(239).

3. Lactoferrin
Lactoferrin, a multifunctional protein of the transferrin family, is one of the components of the immune system(240) of the body used for fighting against foreign invasion of bacteria and virus(241)(242) and lipid oxidation(243) by inhibiting oxidation in a concentration-dependent manner even at concentrations beyond its capacity(244).

4. Metallothionein
Metallothionein, a family of cysteine-rich(24), low molecular weight proteins binds both physiological heavy metals(245) through detoxified fraction of accumulation(245) by capturing harmful superoxide and hydroxyl radicals(246) through binding the metal ions(247)(248) bounded to cysteine(249).

5. Transferrin
Transferrin, a glycoprotein binded iron very tightly but reversibly, enhances the immune system in fighting against infection, inflammation(250) by creating an environment low in free iron(251) impeded to cell oxidation(253)(254), through rapidly evolving sites reverse to bacterial binding in counteract bacterial iron piracy(250). Transferrin deformation and aggregation are found to associate to neurological disorders such as Parkinson's and Alzheimer's disease(252).

6. Hemoglobin
Hemoglobin, the protein molecule in red blood cells enhances the carrying of oxygen from the lungs to the body's tissues and return CO2 from the tissues to the lungs(255)(256). During oxidate stress, the cell membrane is protected by intraerythrocytic hemoglobin from the forming of free radicals(259), probably through regulating NO(258) and auxin homeostasis(257).

7. Myoglobin
Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates. The binding of oxygen by myoglobin(260) through interaction with pathogens establishment of successful infection and survival is probably through peroxidase activity(261) in reducing the free radicals damage caused by oxidate stress(261)(262).

8. Etc.

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(233) Sulforaphane reduces the alterations induced by quinolinic acid: modulation of glutathione levels. by Santana-Martínez RA1, Galván-Arzáte S2, Hernández-Pando R3, Chánez-Cárdenas ME1, Avila-Chávez E4, López-Acosta G1, Pedraza-Chaverrí J5,Santamaría A6, Maldonado PD7.(PubMed)
(234) Ferritin in the red cells of normal subjects and patients with iron deficiency and iron overload. by Cazzola M, Arosio P, Barosi G, Bergamaschi G, Dezza L, Ascari E.(PubMed)
(235) New functions for an iron storage protein: the role of ferritin in immunity and autoimmunity. by Recalcati S1, Invernizzi P, Arosio P, Cairo G.(PubMed)
(236) CoCl2-induced biochemical hypoxia down regulates activities and expression of super oxide dismutase and catalase in cerebral cortex of mice. by Rani A1, Prasad S.(PubMed)
(237) Transferrin and ferritin response to bacterial infection: the role of the liver and brain in fish. by Neves JV1, Wilson JM, Rodrigues PN.(PubMed)
(238) The significance of ferritin in cancer: anti-oxidation, inflammation and tumorigenesis. by Alkhateeb AA1, Connor JR.(PubMed)
(239) The iron-binding protein Dps2 confers peroxide stress resistance on Bacillus anthracis. by Tu WY1, Pohl S, Gizynski K, Harwood CR.(PubMed)
(240) Antiviral properties of lactoferrin--a natural immunity molecule. by Berlutti F1, Pantanella F, Natalizi T, Frioni A, Paesano R, Polimeni A, Valenti P.(PubMed)
(241) Potential lactoferrin activity against pathogenic viruses. by Redwan EM1, Uversky VN2, El-Fakharany EM3, Al-Mehdar H4.(PubMed)
(242) The antimicrobial activity of lactoferrin: current status and perspectives. by Orsi N1.(PubMed)
(243) Role of lipid oxidation, chelating agents, and antioxidants in metallic flavor development in the oral cavity by Omür-Özbek P1, Dietrich AM, Duncan SE, Lee Y.(PubMed)
(244)Lactoferrin in infant formulas: effect on oxidation by Satué-Gracia MT1, Frankel EN, Rangavajhyala N, German JB.(PubMed)
(245) Contrasting metal detoxification in polychaetes, bivalves and fish from a contaminated Fan W1, Xu Z2, Wang WX3.(PubMed)
(246) Channa punctata brain metallothionein is a potent scavenger of superoxide radicals and prevents hydroxyl radical-induced in vitro DNA damage by Atif F1, Kaur M, Ansari RA, Raisuddin S.(PubMed)
(247) In vitro free radical scavenging activity of hepatic metallothionein induced in an Indian freshwater fish, Channa punctata Bloch by Atif F1, Kaur M, Yousuf S, Raisuddin S.(PubMed)
(248) Possible role of cutaneous metallothionein in protection against photo-oxidative stress--epidermal localization and scavenging activity for superoxide and hydroxyl radicals by Hanada K1, Baba T, Hashimoto I, Fukui R, Watanabe S.(PubMed)
(249) Quantitation of human metallothionein isoforms: a family of small, highly conserved, cysteine-rich proteins by Mehus AA1, Muhonen WW, Garrett SH, Somji S, Sens DA, Shabb JB.(PubMed)
(250) Nutritional immunity. Escape from bacterial iron piracy through rapid evolution of transferrin by Barber MF1, Elde NC2.(PubMed)
(251) Total iron binding capacity and transferrin concentration in the assessment of iron status by Kasvosve I1, Delanghe J.(PubMed)
(252) Fibrillation of transferrin by Booyjzsen C1, Scarff CA, Moreton B, Portman I, Scrivens JH, Costantini G, Sadler PJ.(PubMed)
(253) The formation of Fe3+-transferrin-CO3(2-) via the binding and oxidation of Fe2+ by Kojima N, Bates GW.(PubMed)
(254) Iron released from transferrin at acidic pH can catalyse the oxidation of low density lipoprotein. by Lamb DJ1, Leake DS.(PubMed)
(255) Blood substitutes: evolution from noncarrying to oxygen- and gas-carrying fluids by Cabrales P1, Intaglietta M.(PubMed)
(256) Hemoglobin solutions and tissue oxygenation by Muir WW1, Wellman ML.(PubMed)
(257) Plant hemoglobin participation in cell fate determination by Huang S1, Hill RD1, Stasolla C1.(PubMed)
(258) The dual effects of nitrite on hemoglobin-dependent redox reactions. by Lu N1, Chen C2, He Y3, Tian R4, Xiao Q5, Peng YY6.(PubMed)
(259) Redox reactivity in propolis: direct detection of free radicals in basic medium and interaction with hemoglobin by Mot AC1, Damian G, Sarbu C, Silaghi-Dumitrescu R.(PubMed)
(260) Spiking in cytosolic calcium concentration in single fibrinogen-bound fura-2-loaded human platelets by Heemskerk JW1, Hoyland J, Mason WT, Sage SO.(PubMed)
(261) Molecular characterization of Clonorchis sinensis secretory myoglobin: delineating its role in anti-oxidative survival. by Ren M, He L, Huang Y, Mao Q, Li S, Qu H, Bian M, Liang P, Chen X, Ling J, Chen T, Liang C, Wang X, Li X1, Yu X.(PubMed)
(262) Molecular characterization of Clonorchis sinensis secretory myoglobin: delineating its role in anti-oxidative survival by Ren M, He L, Huang Y, Mao Q, Li S, Qu H, Bian M, Liang P, Chen X, Ling J, Chen T, Liang C, Wang X, Li X1, Yu X.(PubMed)

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