transduce this Flashcards

1
Q

Difference between intracellular and intercellular?

A

intercellular is communication between cells, intracellular is within a single cell

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2
Q

4 functions of intercellular signaling

A

signaling can tell a cell to survive,
divide,
differentiate,
die or increase/decrease functioning (change kinetics).

A single signaling molecule can perform multiple tasks (ex: acetylcholine has multiple functions). A signaling molecule can exist as a gas

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3
Q

Where are receptors located on cells? For intracellular? For intercellular?

A

intracellular vs. extracellular
Intracellular are within cell, usually for steroid hormones via endocrine function.
Extracellular receptors are on the outside of a cell

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4
Q

What are the 3 types of extracellular receptors? Examples of each?

A

Extracellular receptors are on the outside of a cell and have three types:

  1. Ionotropic receptor
    a. Nicotinic AChR main one mentioned in slides
  2. Metabotrophic receptor
    a. Tyrosine kinase and all g-protein coupled receptors are metabotrophic
  3. Enzyme-linked receptor
    a. Insulin, nerve growth factor, brain derived neurotrophic factor, epidermal growth factor, platelet derived growth factor
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5
Q

What is an inotropic receptor?

A

also known as ligand gated ion channels, allow ions into the cell in response to the binding of a chemical messenger

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6
Q

What is a metabotrophic receptor?

A

function through a secondary messenger, are indirectly linked with ion channels on plasma membrane. When a metabotrophic receptor is activated, a series of intracellular events are triggered, which may result in an ion pathway opening but you need a lot of secondary messengers to make that happen

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7
Q

What is an enzyme receptor?

A

binding of extracellular ligand causes enzymatic activity within a cell

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8
Q

Intercellular receptors can take 4 different forms, what are they?

A
  1. Contact dependent: receptor on one cell must bind to signal molecule on another cell
  2. Paracine: signaling cell sends out signaling molecules to neighboring cells
  3. Synaptic: in neurons, neurotransmitters act on target cells thru axons
  4. Endocrine: cells send hormones out to blood stream to affect other cells
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9
Q

Can one signaling molecule perform multiple functions?

A
yes
Example: Acetylcholine can be used for 
-Decreasing rate of force of contrxn in heart muscle cells
-Contraction in skeletal muscle cells
-Secretion in salivary gland cells
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10
Q

What is the pathway for how signaling occurs through cascade of intermediate signaling complexes? There are 6 steps

A
  1. Signaling molecule
  2. Cell surface receptor
  3. G-Protein
  4. Enzyme
  5. Intracellular mediator
  6. Target protein
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11
Q

____ ___ and ___ are types of ligands interact with intracellular receptors, they usually bind to intracellular receptors.

A

steroid hormones and IP3

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12
Q

you can inactivate a receptor by ___it, ___ ___ it, or producing an __ __

A

sequestering it; down-regulating, inhibitory protein

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13
Q

G-protein coupled receptors: sense molecules outside the cell and then activate inside __ ___ pathways, only in ___, two major pathways: ___ and _____

A

signal transduction; eukaryotes; cAMP and phosphatidylinositol

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14
Q

____ units dissociate when stimulated

A

G-protein

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15
Q

The cAMP pathway is a __ __ coupled receptor triggered signaling cascade used in cell communication.

A

G protein

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16
Q

The cyclic AMP cascade, 3 main steps

A
  1. cAMP activates protein kinase A (PKA)
  2. which causes the catalytic units of PKA to phosphorylate substrate proteins.
  3. PKA does a ton of stuff: can turn enzymes on/off, bind to DNA to increase gene expression, act directly on ion channels
17
Q

What is PKA?

A

family of enzymes who’s activity is dependent on cAMP levels in cell

18
Q

What are the steps involved in PKA activation

A
  1. Cytosolic cAMP increases
  2. Two cAMP molecules bind to each PKA regulatory subunit
  3. The regulatory subunits move out of the active sites of the catalytic subunits and the R2C2 complex dissociates
  4. The free catalytic subunits interact with proteins to phosphorylate Ser or Thr residues.
19
Q

__ and ___ are secondary messengers used in signal transduction and lipid signaling. They work together to activate protein kinase C. ___ can travel to the endoplasmic reticulum where they stimulate release of Ca++ to cytoplasm.

A

IP3 and DAG; IP3;

20
Q

___ ___ ___ are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. Two of these receptors may be linked to create a dimer. This process leads to rapid activation of the ___ ___ domains by triggering neighboring __ ___ ___.

A

Receptor tyrosine kinases (RTK); cytoplasmic kinase; RTKs

21
Q

2 examples of receptor tyrosine kinases

A

Example: PDGF and insulin receptor

22
Q

tyrosine kinase domains come together and ____.

A

autophosphorylate

23
Q

__ __ are small G-proteins, involved in cell signaling, when switched on it subsequentely switches on other proteins that turn on genes.

A

Ras proteins

24
Q

Ras proteins are involved in __ __, ____ and ____.

A

cell growth; differentiation; survival

25
Q

Overactive Ras proteins can cause ____. They are GTP dependent (when GTP is bound ras is active) and activate ____ kinases, which change protein activity or gene expression.

A

cancer; MAP

26
Q

A ___ ___ is a sequence of events where one enzyme phosphorylates another, causing a chain reaction leading to the phosphorylation of thousands of proteins.

A

phosphorylation cascade

27
Q

__-___ is a protein complex that controls transcription of DNA, cytokine production and cell survival.

A

NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells)

28
Q

What is the pathway of activation for NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells)? There re 4 steps

A
  1. Cell surface TNF receptor activated
  2. NFkB is inactive in cytoplasm with IkB
  3. Kinase removes IkB
  4. NFkB moves to nucleus and target genes are transcribed
29
Q

Start codon, the most common is ___, codes for ___in eukaryotes and ___ ___ in prokaryotes

A

AUG; methionine ; modified methionine

30
Q

DNA is read in triplets, changing __ __ will change the codons thus changing __ __

A

reading frame; protein stucture

31
Q

Structure of transfer RNA

A

clover leaf shaped with a D loop (closest to 5’ end), an anticodon loop and a T loop (closest to 3’ end)

32
Q

__-__ is an amino acid the tRNA codes for is attached on the 3’ O

A

Aminoacyl-tRNA

33
Q

What are the 3 ribosome domains?

A

Ribosome domains:
A: aminoacyl-tRNA
P: Peptidyle-tRNA
E: Exit

34
Q

Stop codon: nucleotide triplet that signals the termination of translation: __, ___, and ___ are the most common

A

UAA, UAG, UGA

35
Q

Importance of protein folding

A

if they are fucked up then horrible things happen such as prion diseases (Creutzfeldt-Jakob and mad cow disease)

36
Q

Function of proteasome

A

The main function of the proteasome is to degrade unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds

37
Q

The addition of ____ to a substrate protein is called ___ or _____.

A

ubiquitin; ubiquitination or ubiquitylation

38
Q

Ubiquitination can affect proteins in many ways (3):

A
  1. it can signal for their degradation via the proteasome alter their cellular location
  2. affect their activity
  3. promote or prevent protein interactions.