Apoptosis/Stem Cells Flashcards

1
Q

complexes with cytochrome c and ATP to activate caspase-9

A

Apaf-1

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2
Q

Apaf-1/ATP/Caspase-9/cytochrome c complex

A

Apoptosome

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3
Q

Bcl-2 family members that induce apoptosis by inhibiting activity of anti-apoptotic proteins

A

Bad and Bid

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4
Q

Bcl-2 family member that induces apoptosis when translocated to mitochondria

A

Bax

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5
Q

family of genes involved in apoptosis; some inhibit apoptosis and others promote apoptosis

A

Bcl-2

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6
Q

formation of irregular bulges in the plasma membrane of a cell during apoptosis

A

blebbing

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7
Q

proteases involved in apoptosis; contain cysteine residue at active site and cleave after aspartate in substrate

A

caspases

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8
Q

amino acid sequence present on C-terminus of both Fas and FADD

A

death domain

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9
Q

Amino acid sequence present on N-terminus of both FADD and pro-caspase-8

A

DED

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10
Q

complexes to fas and pro-caspase-8 when fas is stimulated

A

FADD

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11
Q

Cell surface receptor in immune cells that binds a ligand leading to apoptosis

A

Fas

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12
Q

negative regulator of apoptosis

A

FLIP

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13
Q

inhibitor of apoptosis protein

A

IAP

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14
Q

pro-apoptotic proteins released from mitochondrion that inhibit action of IAPs

A

Smac/Diablo

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15
Q

True or false: apoptosis is reversible once the process has started

A

false

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16
Q

what signals for apoptosis

A

phosphatidylserine

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17
Q

phagocytose apoptotic cells

A

macrophages and neighboring cells

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18
Q

how are caspases activated?

A

the inactive form is cleaved by other caspases

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19
Q

_____ caspases activate ____ caspases, which can then activate other ____ caspases

A

initiator; executioner; executioner

20
Q

Four things caspases cleave

A

1) inhibitors of DNase that cleave genomic DNA between nucleosomes
2) nuclear lamin
3) cytoskeletal proteins
4) inhibitors of apoptosis

21
Q

Two apoptotic pathways

A

1) Intrinsic/stress

2) extrinsic/death receptors

22
Q

How do antiapoptotic proteins work

A

they sequester pro-apoptotic proteins

23
Q

How do the proapoptotic proteins Bad/Bid work

A

block Bcl-2 and Bcl-xL interaction with pro-apoptotic proteins

24
Q

Two antiapoptotic members of the Bcl-2 family

A

Bcl-2 and Bcl-xL

25
Q

Two proapoptotic members of the Bcl-2 family

A

Bad, bid

26
Q

How do the proapoptotic proteins Bak/Bax work

A

translocate to the mitochondria, where they insert in the membrane and disrupt its integrity, allowing cytochrome c to be released

27
Q

Causes dimerization of procaspase-9, creating active caspase-9 dimers

A

apoptosome

28
Q

Catalyzed by proteolytic activation by capase-9, these two proteins lead to the death of the cell in the intrinsic/mitochondrial pathway

A

Caspase-3 and caspase-7

29
Q

How does Fas trimerize in the extrinsic pathway?

A

membrane-bound FasL (ligand) on surface of one cell binds to Fas on target cell, recruiting adaptor FADD (bound via death domain on both)

30
Q

What does the FADD death effector domain at the N-terminus (aka not bound to Fas) bind to to activate?

A

pro-caspase 8

31
Q

Where is the death domain and where is the death effector domain?

A

death domain: C-termini of both Fas and FADD adaptor

death effector domain: N-terminus of FADD and caspase-8

32
Q

when activated what is removed from caspase-8

A

N-terminal DED

33
Q

What does caspase-8 do at the end of the extrinsic pathway?

A

activate downstream caspases

34
Q

Besides its role in the extrinsic pathway, what does caspase-8 activate?

A

Caspase-1 (which leads to other caspases and cell substrates) and Bid

35
Q

Bid is normally inactive in the cytosol but when its cleaved it translocated to…

A

the mitochondria, where it disrupts the membrane to let cytochrome c out and feed into the intrinsic pathway

36
Q

They bind to procaspases to prevent their activation and bind to caspases to inhibit their activity

A

Inhibitors-of-Apoptosis Proteins (IAPs)

37
Q

What do Reaper, Hid, and Grim do?

A

Inhibit IAPs

38
Q

Similar in structure to caspase-8 but lack catalytic residues. Compete with caspase-8 for binding to FADD. . Negative regulator of apoptosis

A

FLIPs

39
Q

Bind to apoptosis-inducing ligand but cannot transduce apoptotic signal.

A

Decoy receptors

40
Q

Initiates transcription of pro-apoptotic genes PUMA and Noxa after being activated by DNA damage

A

p53

41
Q

Phopsphorylate, activate, and stabilize p53

A

ATM and Chk2 protein kinases

42
Q

Excessive/inappropriate apoptosis can lead to (5)

A
  1. neurodegenerative diseases
  2. immune deficiency diseases
  3. cardiovascular disease
  4. emphysema
  5. AIDS
43
Q

Too little apoptosis can lead to (2)

A
  1. cancer

2. autoimmune diseases

44
Q

Two ways cancer affects the apoptotic pathways

A

IAP expression increased and anti-apoptotic Bcl-2 protein levels increased

45
Q

Cancer treatment strategies involving reactivating apoptosis (3)

A
  1. BH3 mimetics
  2. XIAP antagonists
  3. FasL mimetics and Fas activators