Some cancers are caused by the overexpression of receptor tyrosine kinases (RTKS). It is known that RTK signaling pathways commonhi stimulate cell diyision. Why would the overexpression of receptor tyrosine kinases lead to cancer development? rface it is nossible
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- The G protein coupled receptor (GPCR) pathway elicits diverse intracellular responses in different cells. The basic steps of GPCR signaling are outlined in this diagram. Which of the following statements correctly describes the process of GPCR signaling? The GPCR activation is reversible after the signal of the ligand diminishes. The membrane-embedded enzyme uses GTP as a secondary messenger to initiate gene expression. The ligand attaches to both the GPCR and the membrane-embedded enzyme to activate the GPCR pathway. The ligand-bound GPCR sends a GTP molecule to an enzyme in the membrane and switches it into an active state.Continuous exposure of a Gαs protein coupled receptor to its ligand leads to a phenomenon known as desensitization. Describe several molecular mechanisms for receptor desensitization. How can a receptor be reset to its original sensitized state? What effect would a mutant receptor lacking serine or threonine phosphorylation sites have on a cell?When epidermal growth factor (EGF)—the ligand for the epidermal growth factor receptor (EGFR)—binds EGFR on the cell surface, the intracellular domain of the receptor changes shape into an "active state.” The receptor then induces a cascade of kinases in the cytoplasm, resulting in the activation of mitogen-activated protein kinase (MAPK). One effect of EGFR signaling is the stimulation of cell proliferation. Overactive EGFR is frequently found in cancer cells. One strategy for developing anticancer drugs is to target the overactive signaling proteins found in cancer cells. Antibodies are proteins made by immune cells that only recognize specific biomolecules, called antigens. The major component of an anticancer drug is an antibody that specifically recognizes and binds EGFR. Which of the following will most likely happen when this anticancer drug is applied to a tumor that has a high level of EGFR? Tumor cells with active EGFR will increase and MAPK activity in the tumor will…
- Steroid hormones are required by the body at puberty and into adolescence to regulate growth and cell division at more rapid pace than in later life. This regulation occurs via their interaction with cellular receptors and the signaling cascades/pathways that follow. Describe for me the difference between the two major classes of steroids, anabolic and catabolic steroids. What might you expect the result of signaling cascades to be in cells receiving either anabolic or catabolic “signals”? (B) At some point in late adolescence, steroid production decreases by almost 100 fold, as we transition into “adulthood”. Why might we wish to stop these signals from constantly being in our blood stream, (like, Say, between 17-24 years of age)? What result might these steroids have on cancer cells where abhorrent signaling is already causing an increased rate of cell division/growth? Could steroid use result in Cancer?3) The “Met" receptor is a membrane receptor protein responsible for initiating signal transduction pathways that cause cells to divide, among other things. After the Met receptor has been stimulated by its specific growth factor, another protein called c- Cbl will bind to the Met receptor. C-Cbl will then attach a chain of small proteins called ubiquitin to the Met receptor. These chains of ubiquitin help the cell recognize that the Met receptor should undergo receptor-mediated endocytosis, which eventually leads to the destruction of the Met receptor. Circle any answer or answers that include mutations that could cause the cell to potentially become a cancer cell. A) a mutation causing there to be too much ubiquitin protein produced. B) a mutation causing c-Cbl to be inactivated. C) a mutation causing ubiquitin to be inactivated. D) a mutation causing there to be too few Met receptors produced. E) a mutation causing the Met receptor to no longer be able to bind to its growth factor.…RAS is a signal transducer that acts as a switch for turning on cell division. Drag the descriptions below to their proper places on the figure to show the sequence of events. When growth factor binds to the receptor, the intracellular domain activates RAS by facilitating exchange of GDP for GTP. When no growth factor is bound to the extracellular receptor, RAS is bound to GDP and is inactive. RAS activates the first of three sequential kinase proteins termed the MAP kinase cascade. Cell proliferation proceeds as the machinery for cell division is set in motion. The end result of the MAP kinase cascade is activation of a transcription factor. Receptor 1 Ras GDP 2 4 5 Growth factor Ras GTP
- A mutated form of the α subunit of the heterotrimeric G protein has been identified; this form readily exchanges nucleotides even in the absence of an activated receptor. What would be the effect on a signaling pathway containing the mutated α subunit?G protein coupled receptors play an important role in signal transduction in many cells. Label the four essential components of the G protein coupled receptor signaling system (blanks a-d in the picture) by choosing from the menus below. a b b Each answer will be used at most once, while some will not be used at all (select one for each): Group of answer choices transcription factor с transcription factor Show Transcribed Text d transcription factor B C. transcription factor G protein second messenger G protein second messenger IE G protein second messenger G protein second messenger receptor receptor receptor receptor enzyme enzyme enzyme enzyme steroid hormone steroid hormone steroid hormone steroid hormoneGTP binding proteins are molecular switches. How do GTP binding proteins work? Provide two examples of GTP binding proteins that function in intracellular protein transport. Make a drawing that illustrates the function of each of these proteins in their respective roles. Predict the direct outcome of a mutation that: Inhibits GTPase activity Inhibits interaction with the GEF
- I just read an abstract of the paper “Disulfide bond-disrupting agents activate the tumor necrosis family-related apoptosis-inducing ligand/death receptor 5 pathway” and noted that “DDAs and TRAIL synergize to kill cancer cells and are cytotoxic to HER2+ cancer cells with acquired resistance to the EGFR/HER2 tyrosine kinase inhibitor Lapatinib.” For the last sentence, I am not sure the meaning of the “acquired resistance to the EGFR/HER2 tyrosine kinase inhibitor Lapatinib”. Is the “acquired resistance ... to inhibitor” a good thing or bad thing, as far as the synergize effect of DDAs and TRAIL”? Hope that expert can help.Receptor tyrosine kinases such as the epidermal growth factor (EGF) receptor can basically be broken down into three domains: (1) An extracellular, ligand binding domain, (2) A transmembrane domain that must cross through the cell membrane, and (3) an intracellular domain. Match the amino acid with the domain that it would MOST LIKELY be associated with. Lysine (choose (1), (2), or (3) from above) A tyrosine residue capable of being phosphorylated on its hydroxyl group (choose (1), (2), or (3) from above) Isoleucine (choose (1), (2), or (3) from above)Why do signaling responses that involve changesin proteins already present in the cell occur in millisec-onds to seconds, whereas responses that require changesin gene expression require minutes to hours?