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    Eccipienti, coloranti e conservanti
    Autore Messaggio
    Eva Offline


    Messaggio: #1
    Eccipienti, coloranti e conservanti
    ho acquistato seppioline penscate nell'oceano indiano surgelate.
    Hanno acido citrico e citrato di sodio. Che roba sono? Sono dannosi per la salute?

    Ovvio che non li ricomprerò!
    (Questo messaggio è stato modificato l'ultima volta il: 12-11-2015 02:21 PM da Eva.)
    12-11-2015 02:21 PM
    Cerca Quota
    Bloomberg5593 Offline


    Messaggio: #2
    RE: Eccipienti, coloranti e conservanti
    Sì, sarebbe meglio evitare i citrati, perché interferiscono con dei meccanismi regolatori nelle cellule. Tra l'altro l'acido citrico industriale e quello "naturale" sono diversi nel senso che tramite analisi possono notarsi le differenze. In alcuni casi, a detta di Ray Peat, possono indirizzare le cellule verso pattern caratteristici del cancro.

    Tra l'altro avevo aperto un thread proprio su questo ultimamente:

    "Per favore registrati qui per vedere il link :-) "


    "If extra citrate enters the cytoplasm of cells from the blood, there could be chronic disturbance of pyruvate dehydrogenase and fatty acid metabolism (in the direction characteristic of cancer)."

    Vopr Med Khim. 1981 Jan-Feb;27(1):68-72.
    [Features of pyruvate and lactate metabolism in tumor-bearing rats following
    citrate administration].
    [Article in Russian]
    Velichko MG, Trebukhina RV, Ostrovskiĭ IuM.
    Everyday administration of citrate (250 mg/kg of body mass) into healthy rats
    within 4 days inhibited activities of pyruvate kinase, pyruvate dehydrogenase,
    alanine transaminase and of reverse lactate dehydrogenase in liver tissue but not
    in sceletal muscles. Within the longer period of citrate administration (8 or 12
    days) activities of pyruvate dehydrogenase and alanine transaminase continued to
    decrease in liver tissue, at the same time, content of pyruvate proceeded to
    increase in sceletal muscles. More distinct inhibitory effect of citrate on the
    pyruvate dehydrogenase activity was observed not only in liver tissue but and in
    sceletal muscles of tumor-bearing animals. Alanine transaminase, which was
    inactivated in liver tissue of healthy animals after citrate treatment, was
    markedly activated in tumor-bearing rats in the same conditions. The data
    obtained suggest that some regulatory functions of citrate were qualitatively
    transformed in tumor-bearing animals, mainly, in relation to turnover of
    glucogenic amino acids.

    Mol Cancer Ther. 2012 Sep;11(9):1925-35.
    ATP citrate lyase knockdown induces growth arrest and apoptosis through different
    cell- and environment-dependent mechanisms.
    Zaidi N (1), Royaux I, Swinnen JV, Smans K.
    (1)Department of Oncology, Janssen Research and Development, Division of Janssen
    Pharmaceutica NV, Beerse, Belgium.
    ATP citrate lyase (ACLY) is a cytosolic enzyme that catalyzes generation of
    acetyl-CoA, which is a vital building block for fatty acid, cholesterol, and
    isoprenoid biosynthesis. ACLY is upregulated in several types of cancer, and its
    inhibition induces proliferation arrest in certain cancer cells. As ACLY is
    involved in several pathways, its downregulation may affect multiple processes.
    Here, we have shown that short hairpin RNA-mediated ACLY silencing in cell lines
    derived from different types of cancers induces proliferation, cell-cycle arrest,
    and apoptosis. However, this antiproliferative effect of ACLY knockdown was
    observed only when cells were cultivated under lipid-reduced growth conditions.
    Proliferation arrest induced by ACLY silencing was partially rescued by
    supplementing the media with fatty acids and/or cholesterol. This indicates that
    the ACLY knockdown-mediated growth arrest might be the result of either fatty
    acid or cholesterol starvation or both. In the absence of ACLY, the cancer cells
    displayed elevated expression of sterol regulatory element binding
    protein-regulated downstream genes involved in de novo fatty acid and cholesterol
    biosynthesis. Furthermore, ACLY suppression resulted in elevated expression of
    acyl-CoA synthetase short-chain family member 2 (ACSS2), an enzyme that also
    produces acetyl-CoA using acetate as a substrate. Acetate supplementation
    partially rescued the cancer cells from ACLY suppression-induced proliferation
    arrest. We also observed that the absence of ACLY enhanced ACSS2-dependent lipid
    synthesis. These findings provide new insights into the role of ACLY in cancer
    cell growth and give critical information about the effects of ACLY silencing on
    different pathways. This information is crucial in understanding the possible
    application of ACLY inhibition in cancer therapeutics.

    Biochem J. 2011 Sep 15;438(3):e5-6.
    A critical role for citrate metabolism in LPS signalling.
    O'Neill LA.
    School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland.
    email laoneill@tcd.ie
    Comment on
    Biochem J. 2011 Sep 15;438(3):433-6.
    Macrophage activation is a key event in the inflammatory process, since these
    cells produce a range of pro-inflammatory molecules, including ROS (reactive
    oxygen species), prostaglandins, cytokines and nitric oxide. These factors
    promote inflammation by causing vasodilation and recruitment of neutrophils,
    monocytes and lymphocytes, which ultimately clear infection and repair damaged
    tissue. One of the most potent macrophage activators is the Gram-negative-derived
    bacterial cell wall component LPS (lipopolysaccharide). LPS is sensed by TLR4
    (Toll-like receptor 4) and triggers highly complex signalling pathways that
    culminate in activation of transcription factors such as NF-κB (nuclear factor
    κB), which in turn increases transcription of genes encoding proteins such as
    COX2 (cyclo-oxygenase 2, a key enzyme in prostaglandin biosynthesis), nitric
    oxide synthase and cytokines such as TNF (tumour necrosis factor). Recently, a
    role for metabolic pathways in the regulation of LPS signalling has become a
    focus of research in inflammation. A notable example is LPS promoting the
    so-called Warburg effect - aerobic glycolysis. This allows for an up-regulation
    in ATP production, and also for the production of biosynthetic intermediates to
    meet the demands of the activated macrophages. In this issue of the Biochemical
    Journal, Infantino et al. add a new finding to the role of metabolism in LPS
    action. They demonstrate a requirement for the mitochondrial citrate carrier in
    the induction of ROS, nitric oxide and prostaglandins by LPS. The knockdown of
    the carrier with siRNA (small interfering RNA), or the use of an inhibitor BTA
    (benzene-1,2,3-tricarboxylate), abolishes these responses. Although no mechanism
    is provided, the authors speculate that acetyl-CoA is synthesized from citrate in
    the cytosol. The acetyl-CoA generated could be required for phospholipid
    biosynthesis, the phospholipids being the source of arachidonic acid for
    prostaglandin production. Another product of citrate metabolism, oxaloacetate,
    will indirectly generate nitric oxide and ROS. This finding places citrate,
    transported from the mitochondria, as a key player in LPS signalling, at least
    for ROS, nitric oxide and prostaglandin production. This somewhat unexpected role
    for citrate in LPS action adds to a growing literature on the role for metabolism
    in the regulation of signalling in inflammation.

    Recent Pat Anticancer Drug Discov. 2012 May 1;7(2):154-67.
    ATP citrate lyase inhibitors as novel cancer therapeutic agents.
    Zu XY, Zhang QH, Liu JH, Cao RX, Zhong J, Yi GH, Quan ZH, Pizzorno G.
    Clinical Research Institution, the First Affiliated Hospital, and School of
    Medicine, University of South China, Hengyang, Hunan, PR China.
    ATP citrate lyase (ACL or ACLY) is an extra-mitochondrial enzyme widely
    distributed in various human and animal tissues. ACL links glucose and lipid
    metabolism by catalyzing the formation of acetyl-CoA and oxaloacetate from
    citrate produced by glycolysis in the presence of ATP and CoA. ACL is aberrantly
    expressed in many immortalized cells and tumors, such as breast, liver, colon,
    lung and prostate cancers, and is correlated reversely with tumor stage and
    differentiation, serving as a negative prognostic marker. ACL is an upstream
    enzyme of the long chain fatty acid synthesis, providing acetyl-CoA as an
    essential component of the fatty acid synthesis. Therefore, ACL is a key enzyme
    of cellular lipogenesis and potent target for cancer therapy. As a hypolipidemic
    strategy of metabolic syndrome and cancer treatment, many small chemicals
    targeting ACL have been designed and developed. This review article provides an
    update for the research and development of ACL inhibitors with a focus on their
    patent status, offering a new insight into their potential application.

    Nature. 2011 Nov 20;481(7381):380-4.
    Reductive glutamine metabolism by IDH1 mediates lipogenesis under hypoxia.
    Metallo CM, Gameiro PA, Bell EL, Mattaini KR, Yang J, Hiller K, Jewell CM,
    Johnson ZR, Irvine DJ, Guarente L, Kelleher JK, Vander Heiden MG, Iliopoulos O,
    Stephanopoulos G.
    Department of Chemical Engineering, Massachusetts Institute of Technology,
    Cambridge, Massachusetts 02139, USA.
    Acetyl coenzyme A (AcCoA) is the central biosynthetic precursor for fatty-acid
    synthesis and protein acetylation. In the conventional view of mammalian cell
    metabolism, AcCoA is primarily generated from glucose-derived pyruvate through
    the citrate shuttle and ATP citrate lyase in the cytosol. However, proliferating
    cells that exhibit aerobic glycolysis and those exposed to hypoxia convert
    glucose to lactate at near-stoichiometric levels, directing glucose carbon away
    from the tricarboxylic acid cycle and fatty-acid synthesis. Although glutamine is
    consumed at levels exceeding that required for nitrogen biosynthesis, the
    regulation and use of glutamine metabolism in hypoxic cells is not well
    understood. Here we show that human cells use reductive metabolism of
    α-ketoglutarate to synthesize AcCoA for lipid synthesis. This isocitrate
    dehydrogenase-1 (IDH1)-dependent pathway is active in most cell lines under
    normal culture conditions, but cells grown under hypoxia rely almost exclusively
    on the reductive carboxylation of glutamine-derived α-ketoglutarate for de novo
    lipogenesis. Furthermore, renal cell lines deficient in the von Hippel-Lindau
    tumour suppressor protein preferentially use reductive glutamine metabolism for
    lipid biosynthesis even at normal oxygen levels. These results identify a
    critical role for oxygen in regulating carbon use to produce AcCoA and support
    lipid synthesis in mammalian cells.

    Vol. 248, No. 12, Issue of June 25, PP. 4318-4326, 1973
    Printed in U.S.A.
    Regulation of Fatty Acid Synthesis in Isolated Hepatocytes
    From the Bantina and Best Department of Medical Research, University of Toronto, Toronto, On,tario, Canada
    M5GlL6 ”
    In isolated hepatocytes prepared from unfed neonatal
    chicks, stimulation of fatty acid synthesis by fructose or di-
    hydroxyacetone required acetate or octanoate in the medium,
    suggesting that the stimulatory effect of these compounds
    required the enhanced production of intramitochondrial
    acetyl coenzyme A. Stimulation of fatty acid synthesis by
    lactate or pyruvate did not require a supplementary substrate.
    Distribution of acetyl-CoA synthetase was 80% intramito-
    chondrial and 20% cytosolic. However, sufficient acetate
    could be activated in the cytosol to accommodate the most
    rapid rates of fatty acid synthesis observed in isolated cells.
    This was shown experimentally by an undiminished rate of
    incorporation of [lJ4C]acetate plus [W]lactate or [Y]fruc-
    tose into fatty acids when ATP-citrate lyase was inhibited by
    ( -)-hydroxycitrate.
    The citrate content of the isolated cells was positively cor-
    related with fatty acid synthesis under all incubation condi-
    tions. The ATP content of the cells did not correlate with
    fatty acid synthesis. Fatty acyl-CoA and cu-glycerophos-
    phate levels only partially correlated with fatty acid synthesis.
    Hence, citrate appears to be an important determinant in the
    regulation of fatty acid synthesis in intact liver cells, probably
    via its ability to activate acetyl-CoA carboxylase.
    Inhibition of fatty acid synthesis by free fatty acids was
    reversible, did not increase with time of incubation, and was
    not relieved by simultaneous incubation with the inhibitor
    of fatty acid oxidation, (+)-decanoylcarnitine. Thus, the
    active inhibitor was not a stable product of the esterification
    of fatty acids nor a product of the oxidation of fatty acids.
    Inhibition of fatty acid synthesis by medium free fatty acids
    was accompanied by an increase in the fatty acyl-CoA level.
    Fatty acyl-CoA may inhibit fatty acid synthesis by directly
    inhibiting acetyl-CoA carboxylase or by inhibiting the mito-
    chondrial citrate carrier and, thereby, reducing the activation
    of acetyl-CoA carboxylase caused by citrate.

    Mechanisms by which tumor necrosis factor stimulates hepatic fatty acid synthesis in vivo
    Carl Grunfeld: Jennifer A. Verdier: Richard Neese,t Arthur H. Moser: and
    Kenneth R. Feingold*
    Metabolism Section' and Cardiology Section,t Department of Medicine, University of California,
    San Francisco, and the Veterans Administration Medical Center, San Francisco, CA 94121
    Abstract We have previously shown that bolus intravenous ad-
    ministration of tumor necrosis factor (TNF) to normal rats
    results in a rapid (within 90 min) stimulation of hepatic fatty
    acid synthesis, which is sustained for 17 hr. We now demonstrate
    that TNF stimulates fatty acid synthesis by several mechanisms.
    Fatty acid synthetase and acetyl-coA carboxylase (measured
    after maximal stimulation by citrate) were not higher in livers
    from animals that had been treated with TNF 90 min before
    study compared to controls. In contrast, 16 hr after treatment
    with TNF, fatty acid synthetase was slightly elevated (35%)
    while acetyl-CoA carboxylase was increased by 58%. To explain
    the early rise in the hepatic synthesis of fatty acids, we examined
    the regulation of acetyl-coA carboxylase. The acute increase in
    fatty acid synthesis was not due to activation of acetyl-coA car-
    boxylase by change in its phosphorylation state (as calculated by
    the ratio of activity in the absence and presence of 2 mM
    citrate). However, hepatic levels of citrate, an allosteric activator
    of acetyl-coA carboxylase, were significantly elevated (51 %)
    within 90 min of TNF treatment. TNF also induces an acute in-
    crease (within 90 min) in the plasma levels of free fatty acids.
    However, hepatic levels of fatty acyl-CoA, which can inhibit
    acetyl-coA carboxylase, did not rise 90 min following TNF
    treatment and were 35% lower than in control livers by 16 hr
    after TNF. IIp These data suggest that TNF acutely regulates
    hepatic fatty acid synthesis in vivo by raising hepatic levels of
    citrate. This is later followed by an increase in acetyl-coA car-
    boxylase and fatty acid synthetase and a decrease in hepatic
    fatty acyl CoA levels. - Grunfeld, C., J. A. Verdier, R. Neese,
    A. H. Moser, and K. R. Feingold. Mechanisms by which
    tumor necrosis factor stimulates hepatic fatty acid synthesis in
    vivo. J. Lipid Res. 1988. 29: 1327-1335

    Diabetes. 2002 Jul;51(7):2018-24.
    Critical role for cataplerosis via citrate in glucose-regulated insulin release.
    Flamez D(1), Berger V, Kruhøffer M, Orntoft T, Pipeleers D, Schuit FC.
    (1)Molecular Pharmacology Unit, Diabetes Research Center, Faculty of Medicine, Vrije
    Universiteit Brussel, Laarbeeklaan 103, B-1090 Brussels, Belgium.
    The molecular mechanisms mediating acute regulation of insulin release by glucose
    are partially known. The process involves at least two pathways that can be
    discriminated on basis of their (in)dependence of closure of ATP-sensitive
    potassium (K+(ATP)) channels. The mechanism of the K+(ATP) channel-independent
    pathway was proposed to involve cataplerosis, the export of mitochondrial
    intermediates into the cytosol and in the induction of fatty acid-derived
    signaling molecules. In the present article, we have explored in
    fluorescence-activated cell sorter (FACS)-purified rat beta-cells the molecular
    steps involved in chronic glucose regulation of the insulin secretory response.
    When compared with culture in 10 mmol/l glucose, 24 h culture in 3 mmol/l glucose
    shifts the phenotype of the cells into a state with low further secretory
    responsiveness to glucose, lower rates of glucose oxidation, and lower rates of
    cataplerosis. Microarray mRNA analysis indicates that this shift can be
    attributed to differences in expression of genes involved in the K+(ATP)
    channel-dependent pathway, in cataplerosis and in fatty acid/cholesterol
    biosynthesis. This response was paralleled by glucose upregulation of the
    transcription factor sterol regulatory element binding protein 1c (SREBP1c)
    (ADD1) and downregulation of peroxisome proliferator-activated receptor
    (PPAR)-alpha and PPAR-beta (PPARdelta). The functional importance of cataplerosis
    via citrate for glucose-induced insulin release was further supported by the
    observation that two ATP-citrate lyase inhibitors, radicicol and
    (-)-hydroxycitrate, block part of glucose-stimulated release in beta-cells. In
    conclusion, chronic glucose regulation of the glucose-responsive secretory
    phenotype is associated with coordinated changes in gene expression involved in
    the K+(ATP) channel-dependent pathway, in cataplerosis via citrate and in acyl
    CoA/cholesterol biosynthesis.
    (Questo messaggio è stato modificato l'ultima volta il: 12-11-2015 03:47 PM da Bloomberg5593.)
    12-11-2015 03:46 PM
    Cerca Quota
    Eva Offline


    Messaggio: #3
    RE: Eccipienti, coloranti e conservanti
    In passato le compravo perché non c'erano quelle schifezze.
    Ora non le comprerò più.
    12-11-2015 07:12 PM
    Cerca Quota
    Bloomberg5593 Offline


    Messaggio: #4
    RE: Eccipienti, coloranti e conservanti
    Lo so, purtroppo è un problema, ma che vuoi farci :(
    13-11-2015 01:42 AM
    Cerca Quota
    Eva Offline


    Messaggio: #5
    RE: Eccipienti, coloranti e conservanti
    Erano un buon prodotto in sè. Peccato. Non le ricomprerò più!
    13-11-2015 12:02 PM
    Cerca Quota

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