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PSY 115 > Midterm Objectives > Flashcards

Midterm Objectives Flashcards

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1
Q

define pharmacology

A

the science of how drugs affect the body

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2
Q

compare and contrast the two subfields of pharmacology relevant to psychology

A

psychopharmacology: how drugs change behavior
neuropharm: how drugs affect brain/neuronal function

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3
Q

definite pharmacokinetics and pharmacodynamics

A

pharmacokinetics - basic principles of drug absorption, distribution, metabolism and excretion: what body does to drug
pharmacodynamics - interactions between the dugs and their binding sites that lead to an effect - what drug does to body

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4
Q

Define site of action, mechanism of action, and receptor

A

site of action - where the drug interacts to produce an effect
mechanism of action - how the drug alters function at the site of action to produce an effect
receptor - tissue element, typically a protein, that a drug can act on to produce an effect

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5
Q

Describe Ehrlich’s receptor theory of drug action

A

a drug must interact by binding to the receptor at the site of action in order for a series of events to occur that produce a biological effect

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6
Q

What are the 4 sources that are involved in drug-receptor interactions

A

ionic - electrostatic attraction: transfer of electrons. can occur across distance
covalent - sharing pair of electrons. accounts for most stability
hydrogen - type of ionic bond
Van der Waals - weak interactions that operate in close range

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7
Q

Define dose and explain why a dose of a drug foes not usually reflect the concentration of a drug at the site of action

A

dose - amount of drug necessary at a given time to see a biological effect
concentration at site of action can be different because of the time it takes to get to the site of action

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8
Q

Apply the law of mass action to drug-receptor binding

A

rate of chemical reaction is proportional to the amount of reactants and products
[drug] + [receptor] == [receptor/drug complexes]
magnitude of the effect of the drug is proportional to the concentration of receptors available for the drug

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9
Q

list the 4 assumptions of AJ Clark’s quantification of dose-response functions

A
  1. law of mass action is applicable to drug + receptor interactions bc it is reversible
  2. all receptors are identical and equally accessible to the drug (false)
  3. intensity of the response to a drug is directly proportional to the number or receptors occupied by the drug
  4. amount of drug that interacts with the receptor is negligible when compared to the concentration of drugs that the receptors are exposed to
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10
Q

Define Kd and Bmax and describe the types of experiments that one can run to derive these measures

A

Kd - dissociation constant: 50% maximum binding for the drug-receptor
Bmax - maximum drug-receptor binding
Radioligand binding assays

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11
Q

Describe the process of using radioligand binding assays

A

gives an estimate amount of receptors in a tissue and gives the affinity of the receptor

  1. grind up tire
  2. give tissue increasing [radioactive drug] that binds to receptor
  3. in control tissue, add radioactive drug + high [non-radioactive drug] - non-specific binding control
  4. rinse
  5. measure radioactivity in both samples and create total and non specific binding control curves
  6. subtract nonspecific from total = [specific receptors]
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12
Q

Describe how one can employ dose-response functions (log or semi log) to gain inside into mechs of drug action and determine relative affinity/potency of drug

A

Bmax - maxes our on both curves
Kd - semi log - where the curve switches
measures affinity: lower Kd, lower [x] needed for effect, higher affinity
potency - dose needed to produce particular effect of given intensity
- think pain killers: more shifted right, less potent

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13
Q

Compare and contrast “affinity” and “potency”

A

affinity - the ability of a drug to bind to its receptor
potency - the amount of drug needed to get a specific effect of specific intensity
- dependent on Kd

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14
Q

Compare and contrast agonies, partial agonist, and full inverse agonist.

A

agonist - a drug that produces a biological effect when it binds to a receptor
partial agonist - a drug that produces a biological effect, but the efficacy (magnitude of response) is reduced
- affinity better, but efficacy lower
full inverse agonist - a drug that binds to the receptor and creates a response opposite to the biological effect of the traditional agonist

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15
Q

What is the relationship between efficacy and affinity?

A

independent

- something can bins a lot (high affinity) but does not mean it’s the most effective

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16
Q

Compare and contrast “competitive” and “non-competitive” agonist

A

competitive - binds to the same site as the agonist
- “competes” to bind to the receptor, decreases the amount of receptor available for agonist

non-competitive - binds to a site other than the agonist - changes f(x) of receptor
- reduces efficacy

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17
Q

Explain how the two types of agonists affect the dose-response function graph

A

competitive - shifts to the right

  • need much higher [agonist] to see same effect, increasing outcompetes
  • Ki: [drug] that results in 50% reception of ligand binding = lower Ki, better competitive agonist

non-competitive: decreases number of available functional receptors that the agonist can bind - shifts curve little to the right
- large reduction in slope = greater the NCA

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18
Q

explain why a full inverse agonist might be mistaken for a competitive agonist

A

since the effect of the full inverse agonist is the opposite of the traditional agonist
the mechanisms are completely different
make a receptor signal without the agonist:
- antagonist: receptor f(x)s
- full inverse agonist: receptor stops signaling

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19
Q

how are interneurons different from other neurons

A

interneurons don’t have long axons, only communicate with cells close

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20
Q

What is a dendritic spine and what is its role in the integration of multiple neurotransmitter inputs?

A

dendritic spines - protrusions from the dendrites where neurons/NT can make contact
they take in all the signals from the spines and integrates them

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21
Q

Describe the mechanism through which a NT is transported into the terminal

A
  1. vesicle formed in golgi apparatus
  2. transported down the axon by microtubules
  3. reaches the axon terminal, bind to the membrane and release NT
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22
Q

Define a varicosity and explain how NT release through varicosities differ from pt-to-pt synaptic contact

A

Varicosity - protrusions that contain vesicles of NTs
instead of releasing NTs at the axon terminal, they release them along the axon
- non-directional release: more widespread effect of the NT

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23
Q

define “active zone” and “postsynaptic density”

A

active zone - contain the docking machinery for vesicular release
- membrane fusion, NT release, high in Ca channels
postsynaptic density - complex of 100+ proteins
- receptors, intracellular signaling mechanisms and ion channels

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24
Q

List basic steps involved in vesicle docking and NT release. Describe roles of v-SNARE and t-SNARE

A

v-snare: located on vesicle
- synaptobrevin/VAMP: anchored to vesicle and helps dock to membrane
t-snares: located in the active zone/terminal
- syntaxin: anchored to membrane
- SNAP 25: soluble protein located near terminal

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25
Define the role for synapsins, complexins, and synaptotagmin for NT release
synapsins - bind to vesicles and anchor them to actin, kinases remove this anchor for movement to AZ complexins - regulate synaptotagmins synaptotagmins - provides platform for proteins to help vesicle-membrane fusion: sensitive to Ca and anchored to membrane of vesicle
26
What are the 3 major mechanisms for terminating NT signaling
1. reuptake: transporters take NT back inside neuron - requires transport, but does not require ATP 2. enzymatic degradation: enzymes in synaptic cleft break down NT 3. diffusion: NTs move out of the synapse
27
What is an autoreceptor and what is its role in regulating NT release
autoreceptor - receptor sensitive to the NT that the same cell released - located at the edges of active zone for NT spill over - work by regulating the Ca channels and the machinery involved in exocytosis - inhibitory intracellular signaling
28
Describe the distribution of ions across the neuron membrane at rest
Charge in cell at rest: v negative Na at rest: [low] in cell, electrostatic and [gradient] wants it inside K at rest: [high] in cell, wants outside. EP wants it inside Cl at rest: [low] in cell, wants inside. EP wants it out
29
describe the movement of Na and K during the phases of an action potential
Rising phase: Na rushes into cell, K channels begin to open, slowly trickles out Repolatization: Na channels begin to close, Na-K pump pushes Na out of cell, K channels still open Hyperpolarization: when cell reaches resting potential, K channels begin to close
30
how do anesthetic drugs exert their numbing effects
block Na channels by forming a pore in the membrane, preventing APs from firing
31
How do myelination and saltatory conduction help APs travel?
myelination: wrapping around axons that help speed up AP electrical signaling saltatory conduction: jumping of electrical signals from node to node
32
Why is ionotropic signaling fast while others are considered slow?
ionotropic: NT can bind and immediately change conformation of receptor others: cause signaling cascades, not as fast
33
describe the structure and function of ionotropic receptors
5 heterogeneous subunits form a central pore | M2 domain lines the pore and determines ion selectivity
34
Describe the structure and function of G-protein coupled receptors
7 transmembrane spanning regions extracellular N terminus intracellular C terminus subunits: - alpha: bound to GDP, gets activated by GTP - beta + gamma: can activate 2nd messenger systems
35
What are the 4 general patterns of signal transduction within a neuron
1. direction ionopore activation - ion flux 2. GPCR activation - stimulation of 2nd messenger 3. neurotrophic receptor activation - tyrosine kinase activity 4. Steroid receptor activity
36
Explain how RGS and AGS regulate G protein signaling
RGS - regulators of G protein signaling - GTPase removes GTP from active alpha subunit in the middle of signal AGS - activator of G protein signaling - binds SELECTIVELY to alpha-i, prolongs activation of subunit - in long run, cannot reform and cannot send next signal
37
What is cAMP and what are its roles in the cell
cAMP - cyclic nucleotide derived from ATP that acts as a second messenger - formed by AC - degraded by phosphatases
38
Describe the common feature of ACs and list how they can be distinguished
common: membrane bound, stimulated by G-alpha-s and forskolin, uses ATP to make cAMP distinctions: - expression in brain/peripheral tissues - can be regulated by: Ca/calmodulin, G-alpha-i/o, phosphorylation
39
Describe the basic structure of an AC
M1 and M2 regions - 6 transmembrane spanning domains variable N terminus C terminus - contains cytoplasmic domains C1 & C2: - subdomain a - catalytic domain & nucleotide binding site - subdomain b - regulates catalytic domain
40
compare and contrast the cAMP and cGMP signaling pathways
similarities: both degraded my phosphodiesterases (PDEs) and have similar pathways cGMP: GC can be in the membrane and the cytosol
41
Define PDE and describe their general structure
PDE - phosphodiesterases - regulate metabolism of cAMP and cGMP through hydrolysis of 3-phosphodiester bond - regulated by PKA, PKC, and PKG binding
42
What are the major receptors which can lead to phosphionsitide signaling
tyrosine kinase, steroid, and Gq-coupled receptors
43
What are the 3 major phosphoionsitides in the brain
Pi, PIP2, PI4P
44
Provide a putatuve therapeutic mechanism for the anti OCD drug Li
Li blocks phosphatases that prevent the removal of phosphate groups from IP3, which would prevent the creation on inocitol
45
Describe the function if PI4K and PI5K and explain what might happen to Pi signaling if they were inhibited
they both add a P group to create PIP2 | - if you don't generate PIP2, it can't be cleaved into DAG or IP3, which are important signaling molecules
46
Define PI3K and explain what might happen if you blocked its function
PI3K adds phosphates to DAG to regenerate PIP2
47
Define an isozyme
isoform of an enzyme
48
Describe the PH domain of a PLC
pleckstrin homolgy - in charge of anchoring the PLC enzyme to the membrane - does not have any transmembrane domains
49
explain how the structure of PLC-gamma enables it to interact specifically to RTKs
RTKs and PLC-gammas both have SH2/3 domains that can cross phosphorylate each other
50
What are the three mechanisms of activation of PLCs?
RTK activation - can activate PLC-gamma Gq receptor - alpha-q subunit can activate PLC-gamma (PLC B1/3) Gi receptor - beta/gamma can activatie PLC-beta-3
51
Describe how the activation of PLC can lead to stimulation of PKC and Ca2+ dependent intracellular signaling pathways
DAG - with calcium, can bind to PKC to activate it | IP3 - bind to IP3 receptors to open Ca channels
52
Describe the major features of the IP3 receptor and how they contribute to Ca2+ release from internal stores
regulate Ca2+ from internal stores in the ER 3 domains: ligand binding - amino terminal regulatory domain - P sites for PKC/PKA, ATP binding site that modulates affinity for IP3 transmembrane-spanning channel domain: opening results in Ca movement into cytoplasm
53
describe the major functions of polyphosphate-5-phosphatases and insitol monophosphatase
Polyphosphate-5-phosphatases: terminated PI signaling | Inositol monophosphatase: removes the last P group to generate inositol
54
Describe the 2 major plasma membrane transport mechanisms that determine the steady-state internal Ca2+ levels and explain how they function
``` Ca-ATPase pump: - enables efflux against [Ca] gradient - PM - controlled by Ca/calmodulin - ER - SERCA pimp Na-Ca exchanger - found in neurons/muscles - drives Ca out of cells, Na in - both against [gradients] ```
55
Explain how the ER and the mitochondria contribute to the regulation of internal Ca2+ signaling
ER - major site of Ca storage, buffering, and signaling - provides rapid means of elevating Ca2+ Mitochondria - employ electrogenic Ca channels to store Ca - uses energy from the ETC to uptake Ca - great storage - not source of Ca signaling
56
Describe the two major sources of Ca2+ that are involved in Ca2+ signaling
IP3 Receptors in ER - PLC - IP3 - IP3R simulation - rise in Ca Ryanodine receptors on the ER - CICR - calcium induced calcium release: requires that calcium is bound to release Ca
57
Describe the 2 major sources of Ca2+ entry from the extracellular fluid
VG-ca channels: activated by membrane depolarization - similar to VG-Na channels LG-Ca channels: non-specific cation channels - ionotropic Ca channels that are gated by binding an agonist
58
What are the three major types of protein kinases and how are they similar?
serine-threonine, tyrosine, dual-function all convert dephosphorylater protein into a phosphorylated protein - transfer terminal P of ATP to hydroxyl group of AA - requires Mg - phosphorylation changes the charge = function of substrate
59
Describe the major functions of the 4 conserved regions of PKC isoforms
C1 - where DAG binds to activate - connected to psedosubstrate binding site - forms loop with C4 to inhibit function - DAG disconnects the 2 C2 - determines Ca sensitivity C3 - ATP binding site C4 - substrate binding site - recognizes AAs
60
Define AKAP and its role in PKA function
AKAP - A Kinase Anchor Proteins - bind to the regulatory subunits of PKA - keeps PKA in close proximity to signal transduction molecule that it can phosphorylate
61
Define RACK and how it effects PKC function
RACK - receptors for activated C kinase - when PKC is activated, the kindases tend to move from the cytoplasm to the plasma membrane - PKC binds to RACKs that are aligned at the plasma membrane so the PKC can get closer to the substrates
62
How are the PKA/PKG/PKC activation pathways different from CaMK?
CaMK can continue signaling because of 2nd autophosphorylation - independent signaling witout CaM
63
Describe how MAPKs differ from the 2nd messenger-dependent kinases in terms of their activation
MAPK activation: activated by receptor tyrosine kinases (RTKs) - RTKs activate small G proteins (GTPase activity, changes affinity when GTP bound)
64
What happens when GRKs are at low stimulation?
GRK - g protein receptor kinase when activated, it can phosphorylate the receptor at the alpha subunit - negative charge prevents the alpha subunit from sending another signal
65
What happens when GRKs are at high stimulation?
PKA phosphorylates distal sites on the tail of the receptor - extremely negative this recruits arrestin - attracted to negative charge - does NOT allow alpha subunit to bind - can eventually remove the receptor
66
What regulates small G proteins?
GEF (guanine nucleotide exchange factor) - increases activity: facilitates GDP-GTP exchange - activates more small g protein GAPs (GTPase-activating proteins) - inhibits - similar to RGS, it removes the GTP while the small g protein is signaling GIPs (GTPase-activating proteins) increase activity then decrease it (AGS3-like) - prevents conversion of GTP to GDP - cannot send another signal
67
Describe the localization and activation of RTKs
ligand binds - receptor dimerizes - auto/cross P on tyrosine - catalytic activity - recruits SH2 containing molecules - localized in the plasma membrane
68
describe the localization and activation of NRTKs
distributed in different cellular compartment on the SH1 domain, there is a C terminal that has a regulatory domain and controls activity - allows kinase to bind and find other molecules with SH - enables proteins to interact and P tyrosine
69
Explain how the different SH domains of Src contribute to its function and localization
SH1 - C terminal - catalytic, regulatory domain of the NRTK SH2 - molecular adhesive domain, recognizes P-Tyr SH3 - molecular adhesive domain, recognizes proline rich sequences SH4 - membrane anchor
70
Describe factors that can influence NRTK activity
ser/thr kinases activation of the receptors that contain SH2 domain autophosphorylation that occurs if two NRTKs come into contact
71
describe the structure and functional aspects of RTKs
extracellular domain - contains ligand binding site transmembrane domain - anchors receptor to membrane cytoplasmic domain - catalytic domain (SH1) and various autophosphoylation sites
72
What are ser/thr phosphatases like
AKA PP PP1 - most prevalent in animals: inhibited by DARPP-32 PP2A - cytoplasmic and in nucleus PP2b - Ca2+/calmodulin-depend, binds to AKAPs (anchoring molecule)
73
what are tyrosine phosphatases like
AKA PTPs - outnumber PTK by 10-1000 times NRTPs - catalytic domains unrelated to Ser/Thr phosphatases - sites that attack the P on Tyr - subdomain that confers specifically to the substrate - SHPs - SH2 domains RTPs - have all 3 domains like RTKs
74
Describe how a phosphatse inhibitor like DARPP-31 influences receptor signaling
DARPP-32 is a phosphatase inhibitor - activated by PKA - inactivated by calceneurin When activated, it inhibits PP1 activity which allows the PKA to do whatever - kinase activity enhanced
75
Define a SHPs and how they can affect RTK activity
SHP - like the Sh regions of NRTKs, but on NRTPs - SHP1 - dephosphorylates the authophosphorylation of RTK - inactivates it SHP2 - recruits Grb2 to the RTK - activates the MAPK pathway
76
What are the 3 types of RNA
mRNA - messenger RNA: codes for protein, message from DNA to ribosome rRNA - ribosomal RNA: helps build the ribosomes that make proteins, recognizes start and stop proteins tRNA - transfer RNA: carries AAs to a protein under construction
77
Define RNA halozyme and polymerase
RNA polymerase - synthesizes RNA from DNA | RNA holoenzyme - transcriptional apparatus formed when RNA polymerase binds to core promoter
78
explain how the activation of gene transcription can occur across a relatively large stretch of DNA
activation of transcription can occur across long distances bc of loops
79
How does CREB regulate gene transcription?
initiates it binds to CRE phosphorylated by PKA, MAPK, and CAMKs looks for a specific palindrome sequence
80
how do CREB-like transcriptional factors regulate gene transcription?
bind to CRE (like CREB) includes: activating transcription factors (ATFs_ and CRE modulators (CREM) some CREM isoforms can inhibit transcription
81
How do AP1 transcriptional factors regulate gene transcription?
"activator proteins" respond to PKA, MAPKs, CaMKs heterodimers that recognize palindrome sequence specific to AP1 typically encoded by immediate early genes - mRNA peaks realy, the protein will peak 2 hrs later

PSY 115 (2 decks)

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