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22 Cards in this Set

  • Front
  • Back
where do hormones come from and how do they travel
hormones are secreted by endocrine cells, they travel in the blood stream
describe steroid hormones
small, hydrophobic molecules (lipid soluble) related in structure to cholesterol that can cross the plasma membrane
Describe steroid hormones receptors (SHR)
intracellular proteins that function directly as transcription factors, they can activate or repress genes in the nucleus. The signal is direct, the hormone binds directly to the protein that will regulate changes in transcription
where do hormones come from and how do they travel
hormones are secreted by endocrine cells, they travel in the blood stream
describe steroid hormones
small, hydrophobic molecules (lipid soluble) related in structure to cholesterol that can cross the plasma membrane
Describe the general structure of SHRs
1. The N terminal region is the transcription activating domain
2. DNA binding domain
3. The c terminal is the hormone binding domain (c= capture)
Describe the state of SHRs in the absence of hormone
they an inactive and complexed to an inhibitory protein
Describe steroid hormones receptors (SHR)
intracellular proteins that function directly as transcription factors, they can activate or repress genes in the nucleus. The signal is direct, the hormone binds directly to the protein that will regulate changes in transcription
Describe the general structure of SHRs
1. The N terminal region is the transcription activating domain
2. DNA binding domain
3. The c terminal is the hormone binding domain (c= capture)
Describe the state of SHRs in the absence of hormone
they an inactive and complexed to an inhibitory protein
Describe what happens to and SHR when the hormone binds
The SHR changes conformatin and the inhibitory complex is released exposing the DNA binding domain. The SHR can now bind to its sequences within the promoters of the target genes and regulate transcription
How do peptide (water soluble) hormones initiate a signal
they cannot cross the plasma membrane so thyey initiate a signal cascade by binding to receptors at the cell surface
Describe the insulin receptor
an enzyme linked receptor (tyrosine kinase). In response to insuling binding the tyrosine kinase phosphorylates other proteins and changes their activities
What are the 6 steps of the G protein mechanism of action
1. hormone binds to G linked receptor
2. the active receptor activates the trimeric G protein
3. the G protein activates adenylyl cyclase
4. adenylyl cyclase makes cAMP from ATP
5. cAMP activates PKA (aka A kinase or cAMP dependent protein kinase A)
6. PKA phosphorylates target proteins
Describe the structure of a G protein
3 subunits, alpha, beta, gamma.
describe the resting state of a g protein
alpha, beta, and gamma subunits are all bound, the alpha subunit has GDP bound
What happens to the G protein when it becomes active
the alpha subunit exchanges GDP for GTP and disassociates from the beta gamma units. The GTP bound alpha subunit activates adenylyl cyclase
WHat happens to the alpha subunit of a g protein after it turns on adenylyl cyclase
THe intrinsic GTPase activity hydrolyses the GTP to GDP and the alpha subunit disassociates from the adenylyl cylcase and regoins the beta/gamma subunit. This returns the protein to the rested state.
what enzyme is repsonsible for taking cAMP to AMP in order to "reset" the cell
cAMP phosphodiesterase
Describe the cascade that activates PEPCK
PKA binds to a DNA binding protein called CREB, CREB binds to the DNA elements in the promoter region of the PEPCK gene to activate transcription
How is it possible for a cell to respond to such small amounts of hormone in the blood?
the signal is amplified during the cascade
For a cell to remain responsive, a signal cascade pathway must be reversible. What are the 3 ways that a G protein system can be reversed?
1. GTPase activity of the trimeric G protein that is stimulated by adenylyl cyclase
2. hydrolysis of cAMP to AMP by cAMP phosphodiesterase
3. Ser/thr phosphatases dephosphorylate redsidues on target proteins that were phosphorylated by PKA