Familial hypercholesterolemia is a genetic condition characterized by an absence of functional LDL receptors on the surface of cells. Patients who are homozygous for familial hypercholesterolemia usually die of coronary artery disease in childhood. Which of the following disorders could mimic the symptoms of familial hypercholesterolemia?
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Familial hypercholesterolemia is a genetic condition characterized by an absence of functional LDL receptors on the surface of cells. Patients who are homozygous for familial hypercholesterolemia usually die of coronary artery disease in childhood.
Which of the following disorders could mimic the symptoms of familial hypercholesterolemia?
(A) LDL receptor endocytosis machinery is non-functional (B) lack of ATP allosteric site on AMPK
(C) Golgi proteases that cleave SREBP are not synthesized (D) mutation in the HMG CoA reductase SRE sequence. (E) inability to secrete VLDL from the liver
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- What do mutations in the cytoplasmic domain of the LDL receptor that cause familial hypercholesterolemia reveal about the receptor-mediated endocytosis pathway?As we focused on the translation of mRNA into proteins as well as on protein structure and function. Along the way, we found many opportunities to consider the methods and reasoning by which much of this informationwas acquired. From the explanations given in the chapter,what answers would you propose to the following fundamentalquestion How do we know, based on studies of Neurospora nutritionalmutations, that one gene specifies one enzyme?As a researcher who studies cytoskeletal dynamics, you create a microtubule subunit that cannot hydrolyze GTP. How would the critical concentration for the minus end of a polymer formed by these mutant subunits compare to that of the minus end of a fiber formed by normal microtubule subunits? Why? How would the critical concentration for the minus end of a fiber formed by these mutant subunits compare to that of the plus end of a fiber formed by normal microtubule subunits? Why?
- As we learned when studying protein trafficking, proteins need a nuclear localization signal in order to move from the cytosol into the nucleus via the nuclear pore complex. Protein A contains a typical nuclear localization signal but surprisingly is usually found in the cytosol. When the cell is exposed to a certain hormone, protein A moves from the cytosol into the nucleus, where it turns on genes involved in cell division.When you purify protein A from cells that have not been treated with the hormone, you find that protein B is always complexed with it. To determine the function of protein B, you engineer cells lacking the gene for protein B. You compare normal and gene B deletion cells by separating and isolating the proteins found in the cytoplasm and those found in the nucleus. You then run these proteins on a protein electrophoresis gel to separate them by size. You identify the presence of protein A and protein B by looking for their characteristic bands on the gel (which is…Can you suggest a reason why ribosomes in all living organisms consist of two subunits and not one supramolecular complex?Consider a transmembrane protein that forms a hydrophilic pore across the plasma membrane of a eukaryotic cell, allowing Na+ to enter the cell when it is activated upon binding a specific ligand on its extracellular side. It is made of five similar transmembrane subunits, each containing a membrane-spanning α helix with hydrophilic amino acid side chains on one surface of the helix and hydrophobic amino acid side chains on the opposite surface. Considering the function of the protein as a channel for Na+ ions to enter the cell, propose a possible arrangement of the five membrane-spanning α helices in the membrane.
- For each of the following situations, provide a plausible explanation for how it could lead to unrestricted cell division.(a) Colon cancer cells often contain mutations in the gene encoding the prostaglandin E2 receptor. PGE2 is a growth factor required for the division of cells in the gastrointestinal tract.(b) Kaposi sarcoma, a common tumor in people with untreated AIDS, is caused by a virus carrying a gene for a protein similar to the chemokine receptors CXCR1 and CXCR2. Chemokines are cell-specific growth factors.(c) Adenovirus, a tumor virus, carries a gene for the protein E1A, which binds to the retinoblastoma protein, pRb. (d) An important feature of many oncogenes and tumor suppressor genes is their celltype specificity. For example, mutations in the PGE2 receptor are not typically found in lung tumors. Explain this observation. (Note that PGE2 acts through a GPCR in the plasma membrane.)What would be the effect on an organism’s ability to use glucose as an energy source if a mutation inactivated glucose 6-phosphatase in the liver?Imagine that a mutation has been discovered in the HBA1 gene, where amino acid residue # 1 in the alpha subunit is changed from valine to lysine. The structure of these two amino acids is shown below. How would this mutation affect the mobility of HbA in the gel?a) HbA with this mutation would have the same mobility as normal HbAb) HbA with this mutation would have the same mobility as HbSc) HbA with this mutation would have a faster mobility than normal HbA O d) HbA with this mutation would have a mobility somewhere in between HbS and normal HbA
- Many neurodegenrative diseases are thought to be caused by increased levels of unfolded proteins. Which of the following conditions would you expect to increase unfolded protein levels (select all that apply)? A. Reduced expression of chaperone proteins B. A mutation that inactivates the proteasome C. Increased levels of ubiquitin D. Inactivating mutation in ubiquitin ligase, an enzyme necessary for attaching ubiquitin to proteins in cytosol E. Mutation of N-terminal amino acid from Methionine to ArginineTrue or false: In the ribosome, a protein enzyme is responsible for connecting the two amino acids attached to tRNAs in the A and P sites?Lactose permease, a protein of E. coli, is composed of a single polypeptide that is 417 amino acids in length. By convention, the amino acids within a polypeptide are numbered from the aminoterminus to the carboxyl-terminus. Are the following questions about lactose permease true or false? A. Because the 64th amino acid is glycine and the 68th amino acid is aspartic acid, the codon for glycine, 64, is closer to the 3′ end of the mRNA than the codon for aspartic acid, 68. B. The mRNA that encodes lactose permease must be greater than 1241 nucleotides in length.