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113 Cards in this Set

  • Front
  • Back
Endocrine Signaling
long distance, long lasting. e.g. hormones
Paracrine signaling
*signaling to cells relatively close by
*result doesn't have to last as long
*e.g. ovulation
Autocrine signaling
cell secretes signal into extracellular space, and then binds to it
*e.g. cancer cells secrete own growth factors
what is a big reason cancer cells grow so rapidly?
they can secrete their own growth factors.
Signal transduction:
message changes form along its path
Chemical messenger:
something that dissolves in water and is carried across some distance to transmit a signal (SOLUBLE!!)
ligand (primary messenger):
something a receptor binds to, typically that comes from outside the cell
second messenger:
generally refers to an element in a signaling pathway that is NOT a protein (loose definition)
what are the two typical places to find receptors?
* on cell surface (plasma membrane)
* in the cytosol
How would you distinguish between cytosolic and surface receptors?
by seeing how soluble in water, i.e. how easily signal passes through membrane
how does endo/exocytosis regulate receptors?
regulates the number of surface receptors a cell has
what are two ways of receptor regulation?
*endo/exocytosis
*modification of receptor
Give two examples of receptor modification:
*drug tolerance
*tuning out background noise
glycogen phosphorylase
breaks glycogen apart and phosphorylates it
how many molecules of glycogen phosphorylase are activated by a single epinephrine signal?
10^6
how many glucose released from single epinephrine molecule?
10^8
what is epi --> glucose an example of?
signal amplification
GPLR
G Protein-Linked Receptor
How many transmembrane domains doe a GPLR have?
7 transmembrane domains
What part of the GPLR interacts with the G Protein?
The cytosolic loop between the 5th and 6th transmembrane domain
where on the GPLR is the messenger-binding site?
extracellular loop between the 6th and 7th transmembrane domain
a G Protein with three subunits:
Heterotrimeric G Protein
What three subunits make up a heterotrimeric g protein?
alpha, beta, gamma
what causes the G protein to split apart and release from GPLR?
G protein cleaves from GDP and binds to GTP
Which two subunits never split apart?
beta and gamma are always bound to each other
G protein
a signaling protein that transfers information, and it does so by binding to GTP when it's active, and cleaving to GDP to turn itself off.
which subunit of a heterotrimeric g protein does GDP/GTP bind to?
the alpha subunit
adenylyl cyclase (adenylate cyclase)
converts ATP --> Cyclic AMP (cAMP)
what type of messenger is adenylyl cyclase?
secondary
what enzyme deactivates cAMP?
phosphodiesterase
cAMP
Cyclic Adenine Mono-Phosphate
PKA
Protein Kinase A
What role does PKA play in the liver to release glucose?
after being activated by cAMP, PKA activates Phosphorylase Kinase, which then phosphorylates glycogen phosphorylase
phosphorylase kinase
*activated by PKA
*activates glycogen phosphorylase
PKA is a generic signaling protein
PKA can phosphorylate multiple proteins in multiple cell types
Can PKA go into the nucleus?
YES! e.g. activates CREB --> controlling gene transcription
G alpha s
G alpha stimulus
G alpha i
G alpha inhibitory
why do signals enter the nucleus?
to control gene expression
PLC
Phospholipase-C
how does cholera toxin affect the cell?
ADP-ribose binds to adenylyl cyclase, locking it in "on" position --> endless cAMP--> phosphorylates CFTR --> dehydration
CFTR
a Chloride pump
what would you use to rehydrate someone with cholera?
Gatorade!
CRE
cAMP Response Element
what does PLC do?
cleaves a phospholipid in two
Which phospholipid does PLC cleave?
phosphatidyl inositol
phosphatidyl inositol
*phospholipid with an inositol head group
*cleaved by PLC
inositol
a sugar which is the headgroup of phosphatidyl inositol
why is phosphatidyl inositol always facing the cytosol
phosphatidyl inositol has NO FLIPASE
Which carbon of inositol is the phosphate attached to which links it to the glycerol?
1' (one prime) carbon
PI kinase
phosphatidyl inositol kinase, phosphorylates phosphatidyl inositol
likey tagets (carbons) for phosphorylation of inositol
3', 4', and 5'
where does PLC cleave PIP2?
between the phosphate group and the oxygen linking it to the glycerol
DAG
diacylglycerol
PIP2
Phosphatidylinositol-4,5-bisphosphate
IP3
Inositol-1,4,5-trisphosphate
how does IP3 control release of calcium?
IP3 binds to a ligand gated calcium channel in the ER
non-protein molecule in a signaling pathway
second messenger e.g. IP3, PIP2, Ca+2
PKC
Protein Kinase C
what happens to gap junctions if Ca is present for too long?
the gap junctions close
What role does Ca+2 play in the action of nitroglycerin taken for heart trouble?
Ca+2 controls the releas of the nitric Oxide
Ca+2 + Calmodulin --> NO Synthase
PKLR
Protein Kinase Linked Receptor
what are the two types of protein kinases?
*target tyrosine
*target serine and threonine
What do tyrosine, serine, and threonine have in common?
They are the only 3 amino acids with an -OH on their side groups
where is a phosphate group going to be added?
at a hydroxy (-OH) group
EGF
Epidermal Growth Factor
SH2 domain
binds to phosphotyrosine
what kind of protein is Ras?
A G-Protein
GAPs
GTPase Activating Proteins
*deactivates Ras
GEFs
Guanine nucleotide Exchange Factors
Encourage GTP binding e.g. Sos
MAPK
Mitogen Activated Protein Kinase
FAK
Focal Adhesion Kinase, FAK is a tyrosine Kinase!
TGFbeta
Transforming Growth Factor beta
PBD
Protein Binding Domain (selective for active G-proteins)
epinephrin binds to beta-adrenergic receptor
smooth muscle relaxation, vasodilation
epinephrine binds to alpha-receptor
smooth muscle contraction, vasoconstriction (Galpha p)
PLC gamma
PLC with SH2 domain
PLC beta
activated by G alpha p
3 ways to bind DNA
*go in, direct binding to DNA
*go in, held away until activated
*go in, bind with help of another transcription factor
transcription factor
a protein that controls the expression of a gene
Ets and Jun
transcription factors that promote expression of Cyclins and Cdks
what activates Ets and Jun?
MAPK
how do cdk-cyclin complexes trigger passage from G1 into S phase?
phosphorylation of Rb
What does Akt inhibit?
*Apoptosis
*cell-cycle arrest
____response element
DNA sequence bound by/activated by ______
What binds to Rb when it is inactive?
E2F
where do transcription factors bind to DNA?
at the Promoter sequence
what direction is RNA synthesized?
5' --> 3'
What direction is DNA read?
3' --> 5'
Where is the TATA box?
In the core promoter sequence
What are the GC box and the CAAT box?
Proximal Control Elements
Enhancer
the name of the DNA secuence where TFs bind
Activator
proteins that bind to the Enhancer sequence
mediator
*activated/bound to by Enhacer/activator
*binds to polymerase
Polymerase II (POL2)
Polymerase responsible for making mRNA
why must there be a small number of regulatory transcription factors?
there are not enough genes for each gene to have it's own transcription factor
How is the glucocorticoid receptor activated
*bound by steroid hormone
*release Hsp!!!
cDNA
complimentary DNA
PCR
Polymerase Chain Reaction
what is needed for RT-PCR
Reverse Transcriptase
prohormone
a signal peptide that has not been cleaved from a protein yet
What two things activate insulin release?
* increased blood glucose levels
* triggered stretch receptors
proinsulin
*made from preproinsulin
*precursor of insulin
catecholamines
made by modifying the side group of tyrosine
what is insulin's effect on the liver?
stimulates glucose uptake
what is insulin's effect on muscle and fat cells?
stimulates release of more glucose transporters into the plasma membrane
Beta pancreatic cells
responsible for secreting insulin
totipotent
can give rise to an entire organism
pluripotent
can give rise to any of an organism's cells, but cannot form the trophoblast (placenta)
trophoblast
placenta
what are the only totipotent cells?
fertilized eggs and division up to eight cells
SCNT
Somatic Cell Nuclear Transfer
FACS
Fluorescence Activated Cell Sorter (Flow Cytometry)