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    Displaying items by tag: protein synthesis
    Wednesday, 23 October 2013 11:08

    Protein destroys lymphoma

    Hodgkin lymphoma cytology largeThe key in combating certain types of cancer is probably in the cessation of cell proliferation. Cell proliferation is a process of newly formed cells in the body by division. Researchers try to influence B-cell lymphoma using a similar mechanism.
     
    They reactivate gene that controls the natural process of aging of the cells, and thus prevent their replication. Researchers believe that the discovery could lead to the development of a new medicament for the treatment of tumor diseases.

    Scientists say they have discovered a new role of a protein called Smurf2, which is to suppress tumors. It assists in the process of aging of the cells of the subclass of diffuse B-cell lymphoma.
     
    The authors of the study explained that the recovery of Smurf2 expression on the body can bring benefits for the treatment of patients and help treatment in severe cases. This is possible, since it regulates the process of aging of the cells, and stops cell division and proliferation of B-cells.

    In people suffering from diffuse large B-cell lymphoma, however, protein Smurf2 is less pronounced.
     
    Diffuse B-cell lymphoma is the most common form of non-Hodgkin's lymphoma, - the group of cancers that begin from the lymph nodes and lymphoid system. Scientists believe that if they could develop a drug that increases the expression of Smurf2 protein in tumor cells, medicine can achieve a more effective treatment of the disease.

    Click here for more Smurf2 protein products by Gentaur

    Published in News

    madetoorderaProtein synthesis in the extensions of nerve cells, called dendrites, underlies long-term memory formation in the brain, among other functions. "Thousands of messenger RNAs reside in dendrites, yet the dynamics of how multiple dendrite messenger RNAs translate into their final proteins remain elusive," says James Eberwine, PhD, professor of Pharmacology, Perelman School of Medicine at the University of Pennsylvania, and co-director of the Penn Genome Frontiers Institute.
    Dendrites, which branch from the cell body of the neuron, play a key role in the communication between cells of the nervous system, allowing for many neurons to connect with each other. Dendrites detect the electrical and chemical signals transmitted to the neuron by the axons of other neurons. The synapse is the neuronal structure where this chemical connection is formed, and investigators surmise that it is here where learning and memory occur.
    Previous studies in the Eberwine lab have shown that translation of messenger RNAs (mRNAs) into proteins occurs in dendrites at focal points called translational hotspots. Local protein synthesis in dendrites, not in the cell body of nerves, provides the ability to respond rapidly and selectively to external stimuli. This ability is especially important in neurons that have highly polarized cell morphology, meaning one end of the cell has a very different shape from the other end.
    In dendrites and axons these rapid structural and functional changes occur concurrently – their length, size, shape, and number change to suit the needs of neuronal cell body communication.
    These structural and chemical changes – called synaptic plasticity—require rapid, new synthesis of proteins. Cells may use different rates of translation in different types of mRNA to produce the right amounts and ratios of required proteins.
    Knowing how proteins are made to order – as it were - at the synapse can help researchers better understand how memories are made. Nevertheless, the role of this "local" environment in regulating which messenger RNAs are translated into proteins in a neuron's periphery is still a mystery.
    Eberwine, first author Tae Kyung Kim, PhD, a postdoc in the Eberwine lab, and colleagues including Jai Yoon Sul, PhD, assistant professor in Pharmacology, showed that protein translation of two dendrite mRNAs is complex in space and time, as reported online in Cell Reports this week.
    "We needed to look at more than one RNA at the same time to get a better handle on real- world processes, and this is the first study to do that in a live neuron," Eberwine explains.
    At Home in the Hippocampus
    The team looked at two RNAs that make proteins that bind to glutamate, the dominant neurotransmitter in the brain. Using rat hippocampus neurons the researchers found a heterogeneous distribution of translational hotspots along dendrites for the two mRNAs.
    This finding indicates that RNA translation is dictated by translational hotspots, not solely when RNA is present. A translational hot spot is characterized by where translation is occurring in a ribosome at any one time in a discrete spot. Since hotspots are not uniform, understanding individual hotspot dynamics is important to understanding learning and memory.
    "It's not always one particular RNA that dominates at a translation hotspot versus another type of RNA," says Eberwine. "Since there are 1,000 to 3,000 different mRNA types present in the dendrite overall, but not 1,000 to 3,000 different translational hot spots, do the mRNAs 'take turns' being translated in space and time at the ribosomes at the hotspots?"
    The researchers engineered the glutamate receptor RNAs to contain different fluorescent proteins that are independently detectable, as well as a photo-switchable protein to determine when new proteins were being made. In the case of the photo-switchable protein studies, when an mRNA for the glutamate receptor protein is marked green, it means it has already been translated.
    When a laser is passed over the green protein, it changes to red as a way of tagging when it has been been translated, and new proteins synthesized at that hotspot would be green, which is visible by the appearance of yellow fluorescence (green + red, as measured by light on the visible spectrum). These tricks of the light allow the team to keep track of newly made proteins over time and space.
    "This is the first time this method of protein labeling has been used to measure the act of translation of multiple proteins over space and time in a quantitative way," says Eberwine. "We call it quantitative functional genomics of live cell translation."
    "Our results suggest that the location of the translational hotspot is a regulator of the simultaneous translation of multiple messenger RNAs in nerve cell dendrites and therefore synaptic plasticity," says Sul.
    Laying the Groundwork
    Almost 10 years ago, the Eberwine lab discovered that nerve-cell dendrites have the capacity to splice messenger RNA, a process once believed to take place only in the nucleus of cells. Here, a gene is copied into mRNA, which possesses both exons (mature mRNA regions that code for proteins) and introns (non-coding regions). mRNA splicing works by cutting out introns and merging the remaining exon pieces, resulting in an mRNA capable of being translated into a specific protein.
    The vast array of proteins within the human body arises in part from the many ways that mRNAs can be spliced and reconnected. Specifically, splicing removes pieces of intron and exon regions from the RNA. The resulting spliced RNA is made into protein.
    If the RNA has different exons spliced in and out of it, then different proteins can be made from this RNA. The Eberwine lab was successful in showing that splicing can occur in dendrites because they used sensitive technologies developed in their lab, which permits them to detect and quantify RNA splicing, as well as the translated protein in single isolated dendrites.
    Understanding the dynamics of RNA biology and protein translation in dendrites promises to provide insight into regulatory mechanisms that may be modulated for therapeutic purposes in neurological and psychiatric illnesses. The directed development of therapeutics requires this detailed knowledge, says Eberwine.

    Published in News

    newroleforprPioneering new research from a team of Indiana University Bloomington biologists has shown for the first time that a protein which has been long known to be critical for the initiation of protein synthesis in all organisms can also play a role in the regulation of gene expression in some bacteria, and probably land plants as well.
    The protein, called translation initiation factor 3, or IF3, is one of three proteins that make up the core structure of the machinery needed to guide the joining of messenger RNAs and ribosomes as protein translation commences. These three proteins have been widely considered to simply operate in a constitutive manner and play little, if any, role in regulating the expression of genes.
    The new findings, from the laboratory of David M. Kehoe, professor of biology in the Indiana University Bloomington College of Arts and Sciences, reveals that IF3, in addition to its well-accepted function during translation initiation, also regulates the expression of genes that encode components of the photosynthetic machinery in response to changes in the color of light in the surrounding environment, a process known as "chromatic acclimation."
    These photosynthesis genes produce red-pigmented proteins called phycoerythrin in cyanobacteria when the cells are grown in green light and allow these organisms to efficiently absorb the predominant ambient light color for photosynthesis. The team uncovered the novel function of IF3 while searching for mutants that incorrectly regulated phycoerythrin. The discovery of this mutant was at first surprising, because in all other bacteria that have been examined, mutations in infC (the gene that encodes IF3) are lethal.
    The team solved this puzzle by uncovering a second infC gene in Fremyella diplosiphon, the model organism for the study of light color responsiveness in cyanobacteria. While both IF3s, which have been named IF3a and IF3b, can act in the traditional role of translation initiation, only IF3a was found to also regulate photosynthetic gene expression.
    By exploring the genomes of hundreds of prokaryotes and eukaryotes in collaboration with members of the laboratory of Indiana University Distinguished Professor and Class of 1955 Professor Jeffrey Palmer, the group identified a wide range of species whose genomes appear to have the potential to encode multiple IF3s, with one organism apparently encoding five distinct IF3 family members. And since almost none of these species are capable of chromatic acclimation, Kehoe believes that multiple IF3s must be used to regulate a wide range of environmental and perhaps developmental responses in both prokaryotes and eukaryotes.
    "Particularly interesting was our finding that IF3 families exist in a number of plant species, including commercially important crops," Kehoe said. "This means that new approaches to the modification of traits in agriculturally significant plant species may be possible by manipulating the expression patterns of different IF3 family members."
    The discovery has generated excitement for an additional reason. Historically, scientists have had a difficult time studying IF3 because it is so essential for translation initiation that it can not be altered without causing death. In fact, it remains one of the few proteins involved in translation for which no effective antibiotic has been developed. But the ability of the Kehoe team to delete either of the two infC genes in F. diplosiphon without causing lethality will allow the group to modify both IF3a and IF3b at will.
    "Now that we know that F. diplosiphon contains two functionally different IF3s, and that each is nonessential, we have a unique opportunity to enhance our understanding of how the structural features of IF3 are related to its function," Kehoe said. "Advancing our understanding of the role of IF3 in translation is likely to provide opportunities to develop new antibiotics that are targeted to this class of proteins."
    "A unique role for translation initiation factor 3 in the light color regulation of photosynthetic gene expression" is now available in early online editions of the Proceedings of the National Academy of Sciences. Co-authors with Kehoe and Palmer were Andrian Gutu, a former Ph.D. student in the Kehoe lab who is now a Howard Hughes Medical Institute Postdoctoral Fellow at Harvard University; April Nesbit, a former postdoctoral researcher in the Kehoe lab who is now a lecturer at Purdue Northwest; and Andrew Alverson, a former postdoctoral fellow in the Palmer lab who is now a faculty member at the University of Arkansas. Primary funding for the work was provided by the National Science Foundation, with support provided to Nesbit by the National Institutes of Health.

    Published in News

     

    ExiProgen™ is a breakthrough in synthetic biology allowing for the synthesis and purification of one to 16 proteins per run. 
    DNA, in the form of plasmid or linear PCR product, is added to the system and Gentaur’s coupled transcription/translation E. coli extract then synthesizes the protein. 
    The crude protein extract is further purified, using His-Tag engineered into the proteins. 
    The net result is up to 100 ug of >90% pure Protein in about 6 hours. 
    ExiProgen™ can also purify Nucleic Acids from several sources, making it one of the most versatile systems available.

    Features and Benefits
    Built in protocols optimized for protein synthesis/purification and the extraction of a wide variety of nucleic acid samples
    ExiProgen™ has more contains over 900 protocols, each optimized for protein synthesis/purification and target nucleic acid type and source sample. This optimization enables the user to obtain reproducible results for every run, every day. The instrument software can also be upgraded through the network connection port so you can stay up-to-date with the best performing protocols
    Cooling Block
    ExiProgen™ has a built-in cooling block where the elution tube rack sits.
    Sample integrity is ensured by keeping the samples below 10°C.
    This allows for overnight runs and provides you with confidence in your results.
    Magnetic block & Heating block
    To increase extraction efficiency, the ExiProgen™ has an integrated combined magnetic/heating block. The combination of bead magnetization and sample heating reduces experiment time and increases elution efficiency, resulting in increased sample yield. The heating block’s precision temperature control also ensures reproducible results for protein synthesis reactions.
    Contamination Shield
    ExiProgen™ comes with a contamination shield designed to protect the assay from cross-contamination during instrument operation. Any time the pipette tips are moving, the contamination shield will slide under the tips, therefore eliminating the possibility of intra-assay cross-contamination which is a must when working with multiple samples.

    Easy to use LCD Touch screen
    The 3.5" touchscreen maximizes efficiency by offering an intuitive interface with simple push-button operation for processes such as selecting protocols and controlling the UV sterilization lamp.

    ExiProgen f04
    UV lamp
    ExiProgen™ has a powerful UV sterilization lamp that enables the user to sterilize the instrument chamber before and/or after every nucleic acid extraction or protein purification run. This prevents possible inter-assay cross-contamination that may occur on a busy work day.

    Experimental Procedure

    ExiProgen f05

     

    Principle of protein synthesis and purification
    ExiProgen™ Protein Synthesis Kit useds a E. coli extract to effect coupled transcription/translation of input DNA, which can be plasmid, or PCR generated DNA. The protein itself is generated with a His-Tag, which is then purified using the Ni-NTA magnetic bead provided. The result is high yields of protein that is >90% pure.

    ExiProgen f05 01

    Nucleic acid extraction principle
    ExiProgen™ DNA/ RNA Kits work on the principle of cell lysis, followed by bind, wash elute from silica magnetic beads. High yields of ultrapure DNA or RNA are obtained with OD260 readings of > 1.8 for DNA and 2.0 for RNA.

    ExiProgen f05 02

    And believe it or not it costs ONLY 15700 € !!!

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