Apoptsis Flashcards
what happens during apoptosis?
cytoskeleton collapses, nuclear envelope disassembles
nuclear DNA breaks into fragments
phosphatidylserine on cell surface causes phagocytosis
how can apoptosis be triggered?
extrinsic pathway- death receptor activation
intrinsic pathway- internal trigger
what does an active caspase do?
invoke apoptosis, digest certain proteins
how does a caspase get activated?
apoptosis signals clusters inactive caspases. inactive procaspases get their prodomains cleaved. this cleaves executioner caspases then cleave other substrates
how does DNA get cleaved?
executioner caspase cleaves inhibitory CAD and then the now active CAD cleaved DNA
explain extrinsic pathway
receptors binds with fas ligand thats on a killer lymphocyte. FADD adaptor protein’s death doman binds to receptors death domain. caspase 8’s death effector domain binds to FADD’s death effector domain. receptor+FADD+caspase=DISC. procaspases cluster and cleave each other, activating the caspases
explain intrinsic pathway
cytochrome c released from intermembrane space in mitochondria and binds to Apaf 1. CARD domain on Apaf 1 bind on other Apaf 1s and form a wheel looking shit called apoptosome. procaspase 9’s CARD domain binds to apoptosome’s and clusters to cleave each other
how is a procaspase different from a caspase?
a procaspase turns into a caspase when they cluster and cleave each other
what regulates release of cytochrome c in the intrinsic pathway?
Bcl-2 family
what are the 3 categories of the Bcl-2 family?
anti-apoptotic Bcl-2
pro-apoptotic effector
pro-apoptotic BH3-only
what are Bcl-2 homology domains?
areas where proteins look similar
anti-apoptotic Bcl-2 has what BHs?
all 4, BH4/3/1/2
pro-apoptotic effector has what BHs?
BH3/1/2
pro-apoptotic BH3-only protein has what BHs?
BH3
what does pro-apoptotic effector do?
apoptotic stimulus causes them to aggregate and cluster to releases cytochrome c