Call us toll-free

Protein Synthesis -Translation and Regulation

Dailey HA (ed) (1990) Biosynthesis of Heme and Chlorophylls. New York: McGraw‐Hill.

Approximate price

Pages:

275 Words

$19,50

Role of heme in the biosynthesis of cytochrome c6

Kellie received her PhD from the University of California, San Francisco, Department of Pharmaceutical Chemistry. She is the Manager of the . Kellie’s projects range from utilizing NMR methods in the structural characterization of the bacterial HemO’s, protein-protein interactions, SAR and Fragment based screening by NMR in the design and synthesis of novel inhibitors.

The effects of inhibition of heme synthesis on the intracellular localization of iron in ..

(The old ideathat diphtheria toxin blocks fatty acid burning by inhibiting the carnitine shuttlehas been replaced by the finding that the protein is a nonspecificand very potent inhibitor of protein synthesis.)

Regulation of protein synthesis in rabbit ..

In the absence of added hemin, protein synthesis in a rabbitreticulocyte lysate declines abruptly (shuts off) after about 5 min at30 degrees.

Although production of ferrous (Fe2+) iron couldpotentially result in free radical production, heme oxygenase activity is tightly coupled to ferritinprotein synthesis, which results in binding of iron [].

Garrick is working jointly with on the the development of novel therapeutic strategies targeting the interaction of the P. aeruginosa hemophore HasA with the outer membrane HasR. In the Wilks lab he is combining NMR and HDX-MS exchange to characterize the protein-protein interaction in the development of peptidomimetic strategies. With Dr. Xue he is designing and synthesizing peptidomimetics targeting the heme-dependent ECF signaling system. We have previously shown the Has system is the most unregulated set of genes in an acute murine lung infection, and that deletion of HasR leads to a significant attenuation in virulence. We hypothesize disrupting the heme signal and the cells ability to sense the presence of heme in the extracellular environment will aid in the prevention of P. aeruginosa colonization and infection within the host.

Porphyrin and Heme Synthesis and Bilirubin Metabolism

Layer G, Reichelt J, Jahn D and Heinz DW (2010) Structure and function of enzymes in heme biosynthesis. Protein Science 19 (6): 1137–1161.

The number of diferric transferrin receptors on HeLa cells decreases when cells are grown in iron-supplemented media. The experiments reported here suggest that heme is the iron-containing compound which serves as the signal for receptor number regulation. When HeLa cells were grown in the presence of hemin, transferrin receptor number decreased to a greater degree than when cells were grown in equivalent amounts of iron supplied as ferric ammonium citrate. Incubation of cells in conditions which increased cellular heme content resulted in a decrease in cellular transferrin receptors. Incubating cells with 5-aminolevulinic acid (thus bypassing the rate-limiting step in heme biosynthesis, 5-aminolevulinic acid synthase) led to a decrease in transferrin receptor number. Incubation of cells with an inhibitor of heme oxygenase, Sn-protoporphyrin IX, also led to a decrease in transferrin receptor number. When cellular heme content was decreased by inhibiting heme synthesis with succinylacetone (an inhibitor of 5-aminolevulinic acid dehydratase), or by depriving cells of iron with deferoxamine, an increase in HeLa cell transferrin receptor number was seen. When HeLa cells were incubated with inducers of heme oxygenase (CoCl2, SnCl2, Co-protoporphyrin IX), transferrin receptor number also increased. The effects of all compounds which alter transferrin receptor number were dependent on the concentration of the supplement, as well as the duration of the supplementation. These experiments suggest that intracellular heme content may be an important signal controlling transferrin receptor number.

N2 - The number of diferric transferrin receptors on HeLa cells decreases when cells are grown in iron-supplemented media. The experiments reported here suggest that heme is the iron-containing compound which serves as the signal for receptor number regulation. When HeLa cells were grown in the presence of hemin, transferrin receptor number decreased to a greater degree than when cells were grown in equivalent amounts of iron supplied as ferric ammonium citrate. Incubation of cells in conditions which increased cellular heme content resulted in a decrease in cellular transferrin receptors. Incubating cells with 5-aminolevulinic acid (thus bypassing the rate-limiting step in heme biosynthesis, 5-aminolevulinic acid synthase) led to a decrease in transferrin receptor number. Incubation of cells with an inhibitor of heme oxygenase, Sn-protoporphyrin IX, also led to a decrease in transferrin receptor number. When cellular heme content was decreased by inhibiting heme synthesis with succinylacetone (an inhibitor of 5-aminolevulinic acid dehydratase), or by depriving cells of iron with deferoxamine, an increase in HeLa cell transferrin receptor number was seen. When HeLa cells were incubated with inducers of heme oxygenase (CoCl2, SnCl2, Co-protoporphyrin IX), transferrin receptor number also increased. The effects of all compounds which alter transferrin receptor number were dependent on the concentration of the supplement, as well as the duration of the supplementation. These experiments suggest that intracellular heme content may be an important signal controlling transferrin receptor number.

On the Mechanism of Delayed Inhibition of Protein Synthesis in Heme-Deficient Rabbit ..
Order now
  • Porphyria cutanea tarda (PCT) is the most common subtype of porphyria

    an inhibitor of heme synthesis

  • Citrinin is a mycotoxin which is often found in food

    Iron - Vegan Health Home Page

  • Cimetidine Tablets Drug Information

    Iron in Meat vs

Order now

Metabolism – Proteins | Biochemistry for Medics – …

AB - The number of diferric transferrin receptors on HeLa cells decreases when cells are grown in iron-supplemented media. The experiments reported here suggest that heme is the iron-containing compound which serves as the signal for receptor number regulation. When HeLa cells were grown in the presence of hemin, transferrin receptor number decreased to a greater degree than when cells were grown in equivalent amounts of iron supplied as ferric ammonium citrate. Incubation of cells in conditions which increased cellular heme content resulted in a decrease in cellular transferrin receptors. Incubating cells with 5-aminolevulinic acid (thus bypassing the rate-limiting step in heme biosynthesis, 5-aminolevulinic acid synthase) led to a decrease in transferrin receptor number. Incubation of cells with an inhibitor of heme oxygenase, Sn-protoporphyrin IX, also led to a decrease in transferrin receptor number. When cellular heme content was decreased by inhibiting heme synthesis with succinylacetone (an inhibitor of 5-aminolevulinic acid dehydratase), or by depriving cells of iron with deferoxamine, an increase in HeLa cell transferrin receptor number was seen. When HeLa cells were incubated with inducers of heme oxygenase (CoCl2, SnCl2, Co-protoporphyrin IX), transferrin receptor number also increased. The effects of all compounds which alter transferrin receptor number were dependent on the concentration of the supplement, as well as the duration of the supplementation. These experiments suggest that intracellular heme content may be an important signal controlling transferrin receptor number.

Clontech Laboratories, Inc. - Life Science Tools and …

Jordan PM (1990) The biosynthesis of 5‐aminolevulinic acid and its transformation into coproporphyrinogen in animals and bacteria. In: Dailey HA (ed.) Biosynthesis of Heme and Chlorophylls, pp. 55–121. New York: McGraw‐Hill.

Curcumin | Linus Pauling Institute | Oregon State …

Handschin C, Lin J, Rhee J, et al. (2005) Nutritional regulation of hepatic heme biosynthesis and porphyria through PGC‐1alpha. Cell 122 (4): 505–515.

Order now
  • Kim

    "I have always been impressed by the quick turnaround and your thoroughness. Easily the most professional essay writing service on the web."

  • Paul

    "Your assistance and the first class service is much appreciated. My essay reads so well and without your help I'm sure I would have been marked down again on grammar and syntax."

  • Ellen

    "Thanks again for your excellent work with my assignments. No doubts you're true experts at what you do and very approachable."

  • Joyce

    "Very professional, cheap and friendly service. Thanks for writing two important essays for me, I wouldn't have written it myself because of the tight deadline."

  • Albert

    "Thanks for your cautious eye, attention to detail and overall superb service. Thanks to you, now I am confident that I can submit my term paper on time."

  • Mary

    "Thank you for the GREAT work you have done. Just wanted to tell that I'm very happy with my essay and will get back with more assignments soon."

Ready to tackle your homework?

Place an order