Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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How does an intracellular receptor regulate gene expression in the cell? Describe briefly what happens when a ligand like a hormone binds to one of these receptors
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- Does adenylate cyclase become more active when the inhibitory (Gia) protein is mutated and increases its intrinsic GTPase activity?arrow_forwardA study is conducted to assess the molecular mechanisms of hormone X. A radioactively labeled form of this hormone is incubated with human cells in tissue culture for 30 minutes, and then incubated briefly with a cross-linking agent. The plasma membrane, cytosolic, and nuclear fractions are isolated from the cell lysate, and the subcellular proteins are separated from these fractions by gel electrophoresis. The only protein bound to the labeled hormone is identified in the new clear fraction. Hormone X is most likely which of the following? Epinephrine Glucagon Growth hormone Insulin Thyroxinearrow_forwardThe figure from Moore (2020) shows a G protein-coupled receptor in a membrane. Note that "out" means outside the cell and "in" means facing the cytoplasm. The three amino acids "DRY" in loop I2 are required for protein targeting. What is the name of this kind of sequence, and what is its function? What protein targeting sequence is no longer included in this diagram? Why? The sequence "QXXNK" (where X is any amino acid) found in loop I3 has been identified based on its enzymatic activity. What is this activity? What particular domain would you expect to find in either Loop E1, E2, or E3? The gene that codes for this protein is a member of a family of genes that has arisen over evolutionary time. If you compared several of the genes in this family, would you expect their sequences to be most homologous (similar) in the region you describe in #3 above or #4 above? Why?arrow_forward
- What is the difference between a protein kinase and a secondmessenger? Can both operate in the same signal transduction pathway?arrow_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_forwardHow 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_forward
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