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Protein Synthesis; Role of Golgi ..

Describe how interference in protein synthesis can result in disruption of cellular and bodily processes....

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Rough ER- Protein synthesis 2) ..

Examples of protein synthesis by the rough endoplasmic reticulum are the proteins produced in secretory cells. These include the digestive produced in the stomach and the protein hormones like insulin produced in the pancreas. Organ systems which produce many proteins have cells with a large amount of rough endoplasmic reticulum.

20/12/2014 · What is the role of endoplasmic reticulum in protein synthesis

The ribosomes on the rough endoplasmic reticulum manufacture which enter the channels of the endoplasmic reticulum and move to places where they can create pockets. These pockets can then break off as to transport their protein cargo to the for distribution.

Explain the role of DNA and mRNA in protein synthesis

Before the process of protein synthesis can be described, a person must know what proteins are made out of.

T1 - Endoplasmic reticulum ribosome-binding protein 1 (RRBP1) overexpression is frequently found in lung cancer patients and alleviates intracellular stress-induced apoptosis through the enhancement of GRP78

Lung cancer is the leading cause of cancer deaths and is the most occurring malignancy worldwide. Unraveling the molecular mechanisms involved in lung tumorigenesis will greatly improve therapy. During early tumorigenesis, rapid proliferating tumor cells require increased activity of endoplasmic reticulum (ER) for protein synthesis, folding and secretion, thereby are subjected to ER stress. Ribosome-binding protein 1 (RRBP1) was originally identified as a ribosome-binding protein located on the rough ER and associated with unfolding protein response (UPR). In this report, we investigated the role of RRBP1 in lung cancer. RRBP1 was highly expressed in lung cancer tissue, as compared with adjacent normal tissues as assessed by immunohistochemistry (IHC) using lung cancer tissue array (n=87). Knockdown of RRBP1 by short-hairpin RNAs caused ER stress and significantly reduced cell viability and tumorigenicity. This effect was associated with a significant reduction in the expression of glucose-regulated protein 78 (GRP78). UPR regulator GRP78, an anti-apoptotic protein that is widely upregulated in cancer, has a critical role in chemotherapy resistance in some cancers. According to our results, cells with a higher level of RRBP1 were more resistant to ER stress. Ectopic expression of RRBP1 alleviated apoptosis that was induced by the ER-stress agent tunicamycin, 2-deoxy-D-glucose (2DG) or doxorubicin via enhancing GRP78 protein expression. A strong correlation was observed between the expression of RRBP1 and GRP78 in tumor biopsies using the database GSE10072. Our results also indicated that RRBP1 may involve in the regulation of mRNA stability of UPR components including ATF6 and GRP78. Taken together, RRBP1 could alleviate ER stress and help cancer cell survive. RRBP1 is critical for tumor cell survival, which may make it a useful target in lung cancer treatment and a candidate for the development of new targeted therapeutics.

ER definitely plays a major role ..

N2 - Lung cancer is the leading cause of cancer deaths and is the most occurring malignancy worldwide. Unraveling the molecular mechanisms involved in lung tumorigenesis will greatly improve therapy. During early tumorigenesis, rapid proliferating tumor cells require increased activity of endoplasmic reticulum (ER) for protein synthesis, folding and secretion, thereby are subjected to ER stress. Ribosome-binding protein 1 (RRBP1) was originally identified as a ribosome-binding protein located on the rough ER and associated with unfolding protein response (UPR). In this report, we investigated the role of RRBP1 in lung cancer. RRBP1 was highly expressed in lung cancer tissue, as compared with adjacent normal tissues as assessed by immunohistochemistry (IHC) using lung cancer tissue array (n=87). Knockdown of RRBP1 by short-hairpin RNAs caused ER stress and significantly reduced cell viability and tumorigenicity. This effect was associated with a significant reduction in the expression of glucose-regulated protein 78 (GRP78). UPR regulator GRP78, an anti-apoptotic protein that is widely upregulated in cancer, has a critical role in chemotherapy resistance in some cancers. According to our results, cells with a higher level of RRBP1 were more resistant to ER stress. Ectopic expression of RRBP1 alleviated apoptosis that was induced by the ER-stress agent tunicamycin, 2-deoxy-D-glucose (2DG) or doxorubicin via enhancing GRP78 protein expression. A strong correlation was observed between the expression of RRBP1 and GRP78 in tumor biopsies using the database GSE10072. Our results also indicated that RRBP1 may involve in the regulation of mRNA stability of UPR components including ATF6 and GRP78. Taken together, RRBP1 could alleviate ER stress and help cancer cell survive. RRBP1 is critical for tumor cell survival, which may make it a useful target in lung cancer treatment and a candidate for the development of new targeted therapeutics.

PPI plays a big role in the cell-signalling cascade; for instance, dephosphorylation of glycogen synthase by protein phosphatase-1 results in glycogen synthesis.

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  • Endoplasmic Reticulum Flashcards | Quizlet

    12/06/2010 · What is the role of the endoplasmic reticulum in protein synthesis

  • Start studying Endoplasmic Reticulum

    15/01/2018 · Examples of protein synthesis by the rough endoplasmic reticulum are ..

  • ribosomes that are associated with the rough ER

    Assess your understanding of protein synthesis and the rough ER with this combination of assessments

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and what role do they play in protein synthesis?

Subsequently, the uncoupling effect as well as the physiological role of the first uncoupling protein, UCP1, is well established when researchers at the time, were devoting their focus on the thermogenic capacity of brown adipose tissue or BAT.

5 micrometers .ribosomes rough endoplasmic reticulum 0

The experiment that was carried out was able to turn a previously inactive protein into one with catalytic activity through the manipulation of the amino acids of a binding site.

endoplasmic reticulum Flashcards | Quizlet

These proteins each of them have various roles that have physiological importance in the apoplast and overall fundamental impact in plant cell function.

is not involved in protein synthesis

The smooth endoplasmic reticulum plays a major role in synthesizing by means of enzymes embedded in these smooth membranes. It produces the and used in membrane formation, and along with the membrane proteins produced by the rough ER it can synthesize more membrane for itself, for the Golgi complex, the , , and others.

the rough endoplasmic reticulum changes ..

The endoplasmic reticulum is a multifold membranous structure within eukaryotic which plays a major role in the synthesis of the complex molecules required by the cell and the organism as a whole. Often the membranes of these structures are lined with on their outer surfaces, giving them a rough appearance. These parts are called the rough endoplasmic reticulum to contrast them with the smooth endoplasmic reticulum where there are no attached ribosomes.

Endoplasmic Reticulum (Rough and Smooth) - BSCB

AB - Lung cancer is the leading cause of cancer deaths and is the most occurring malignancy worldwide. Unraveling the molecular mechanisms involved in lung tumorigenesis will greatly improve therapy. During early tumorigenesis, rapid proliferating tumor cells require increased activity of endoplasmic reticulum (ER) for protein synthesis, folding and secretion, thereby are subjected to ER stress. Ribosome-binding protein 1 (RRBP1) was originally identified as a ribosome-binding protein located on the rough ER and associated with unfolding protein response (UPR). In this report, we investigated the role of RRBP1 in lung cancer. RRBP1 was highly expressed in lung cancer tissue, as compared with adjacent normal tissues as assessed by immunohistochemistry (IHC) using lung cancer tissue array (n=87). Knockdown of RRBP1 by short-hairpin RNAs caused ER stress and significantly reduced cell viability and tumorigenicity. This effect was associated with a significant reduction in the expression of glucose-regulated protein 78 (GRP78). UPR regulator GRP78, an anti-apoptotic protein that is widely upregulated in cancer, has a critical role in chemotherapy resistance in some cancers. According to our results, cells with a higher level of RRBP1 were more resistant to ER stress. Ectopic expression of RRBP1 alleviated apoptosis that was induced by the ER-stress agent tunicamycin, 2-deoxy-D-glucose (2DG) or doxorubicin via enhancing GRP78 protein expression. A strong correlation was observed between the expression of RRBP1 and GRP78 in tumor biopsies using the database GSE10072. Our results also indicated that RRBP1 may involve in the regulation of mRNA stability of UPR components including ATF6 and GRP78. Taken together, RRBP1 could alleviate ER stress and help cancer cell survive. RRBP1 is critical for tumor cell survival, which may make it a useful target in lung cancer treatment and a candidate for the development of new targeted therapeutics.

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