Concept explainers
To determine: What would be the difficulties of finding cancer drugs that works by inhibiting tyrosine kinase given that similar kinases also function in normal cells.
Introduction: Enzyme-linked receptor is a transmembrane protein with a binding site for signaling molecule outside the cell and an enzyme component inside the cell. An example of enzyme-linked receptor is tyrosine kinase. On binding of ligands with the enzyme-linked receptors, receptor protein comes close together in the plasma membrane and forms dimer which initiates activation of downstream molecules and causes cellular response.
To suggest: Whether it could be possible to develop such new medication through government-sponsored research. Why or why not.
Introduction: Enzyme-linked receptor is a transmembrane protein with a binding site for signaling molecule outside the cell and an enzyme component inside the cell. An example of enzyme-linked receptor is tyrosine kinase. On binding of ligands with the enzyme-linked receptors, receptor protein comes close together in the plasma membrane and forms dimer which initiates activation of downstream molecules and causes cellular response.
To suggest: Alternatives if it is not possible to develop new such medication through government-sponsored research.
Introduction: Enzyme-linked receptor is a transmembrane protein with a binding site for signaling molecule outside the cell and an enzyme component inside the cell. An example of enzyme-linked receptor is tyrosine kinase. On binding of ligands with the enzyme-linked receptors, receptor protein comes close together in the plasma membrane and forms dimer which initiates activation of downstream molecules and causes cellular response.
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Biology (MindTap Course List)
- Figure 9.8 HER2 is a receptor tyrosine kinase. In 30 percent of human breast cancers, HER2 is permanently activated, resulting in unregulated cell division. Lapatinib, a drug used to treat breast cancer, inhibits HER2 receptor tyrosine kinase autophosphorylation (the process by which the receptor adds phosphates onto itself), thus reducing tumor growth by 50 percent. Besides autophosphorylation, which of the following steps would be inhibited by Lapatinib? Signaling molecule binding, dimerization, and the downstream cellular response. Dimerization, and the downstream cellular response. The downstream cellular response. Phosphatase activity, dimerization, and the downsteam cellular response.arrow_forwardOf the steps listed below, which problem would take you the longest to realize you had a problem in your RTK (ie the highest number of earlier steps could still occur)? O the RTK cannot autophosphorylate O the RTK cannot phosphorylate downstream kinases the RTK cannot integrate into the membrane the extracellular ligand cannot bind to the RTKarrow_forwardRous Sarcoma Virus can cause cancer in infected cells. The tumor causing nature of the virus is linked to it harbouring a gene that codes for a unique receptor tyrasine kinase (RTK). What is it about the tyrosine kinase that accounts for the tumor-causing nature of the virus? O It is unrelated to any human kinase and thus is able to act uncontrollably in causing cell division. O It cantain activate downstream effectors without binding to a SH2 domain. O It lacks the carboxy-terminal regulatory domain that is present in RTKS of non-cancerous cells.arrow_forward
- How could we promote rapid or slow signaling for medical purposes? So there are many examples of slow and rapid signaling via coupled receptors. For an example, salivary gland secretion is rapid signaling and cell growth is slow signaling. These pathways could be twisted and used to resolve medical issues in a more natural and less damaging way. Are there any experiments that have or could be done to test out promoting rapid signaling to speed up slow processes such as cell growth in a severe wound? What experiments have or could be done to test out slowing down signaling that is fast like cells responding to their environment negatively (over-active allergies)? Thank you.arrow_forwarda) b) You walk into university and see that everyone has become a unicorn. You try to hide in bluezone only to figure out that everyone can sense you. You are kidnapped by a unicorn, and they ask you: "How do kinases work?" You wake up realizing it was all a dream, but you still wonder: how do kinases work? Hydrolyze the protein and then ATP to activate it First hydrolyze ATP and then transfer Pi to activate a protein Tranfer a free Pi and then hydrolyze ATP to make more free Pi Bind GTP after releasing GDP from the alpha subunitarrow_forwardSuppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: a. Which of the ligands, based on the table, has the highest specificity in binding to the target Protein J?arrow_forward
- Suppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: a. Which of the ligands, based on the table, may be expected to be the most potent or have the highest activity against cancer? Explain. b. Which of the ligands, based on the table, may be expected to be least toxic to normal cells? Explain.arrow_forwardSuppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: Describe the relative binding affinities of Ligand A to Protein K and to the active and inactive forms of Protein J. Determine which will Ligand A bind with the highest, medium, and lowest affinity.arrow_forwardCyclin-dependent kinases are a type of "microchip" protein that require multiple inputs (i.e., structural alterations) to be activated-- and thus are active only under specific conditions (as shown in the diagram below). How does limiting activity to when all conditions have been met help the cell function properly? INPUTS has this phosphate been removed? been added? has this is cyclin present? phosphatearrow_forward
- Working out the order in which the individual components in a signaling pathway act is an essential step in defining the pathway. Imagine that two protein kinases, PK1 and PK2, act sequentially in a kinase cascade. When either kinase is completely inactivated, cells do not respond to the normal extracellular signal. By contrast, cells containing a mutant form of PK1 that is permanently active respond even in the absence of an extracellular signal. Double mutant cells that contain inactivated PK2 and permanently active PK1 respond in the absence of a signal. Draw out the signaling pathway in a wild-type cell. What outcome is predicted for a double mutant cell with an activating mutation in PK2 and an inactivating mutation in PK1? Explain your reasoningarrow_forwardIf you have a protein kinase that is regulated by both small molecule inhibitors as well as by phosphorylation, and is part of a cooperative enzyme complex that works as part of a larger pathway involving kinase and GTPase proteins please explain where on this protein regulation could occur, how different types of inhibition could control the function of the protein as well as the function of the complex, and how the protein could regulate other proteins. (This question was previously answered but it was answered incompletely mentioning an herbicide developed in the 1950's. Apparently, it was a plagiarized excerpt from an NCBI article. This is a repost for a full and complete answer. Thank you so much for your help! :) )arrow_forwardYou are a scientist studying two related congenital diseases, Noonan syndrome and Tiger syndrome. People with these syndromes are characterized by differences in heart development and skeletal morphology. Individuals with either syndrome are also susceptible to certain types of cancer, such as leukemia. Some cases of Noonan syndrome are caused by dominant activating variants of the MAP kinase-kinase-kinase protein Raf. The genetic basis of Tiger syndrome is unknown. Your team is involved in a clinical trial, which finds that drugs that inhibit Raf are associated with improved outcomes in cancer patients with Noonan syndrome. You find that Tiger syndrome patients also respond to the treatment, so you sequence the Raf gene in several patients, but find no mutations. Based on what you know about the MAP kinase pathway, you sequence the Sos gene in Tiger syndrome patients. You find that 5 out of 10 patients in your trial have a SNP that changes the amino acid Thr266 to Lys (T266K).…arrow_forward
- Biology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher:Cengage LearningBiology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax