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EOM 1 - Test 1 > Lecture 18: Blood Coagulation > Flashcards

Lecture 18: Blood Coagulation Flashcards

1
Q

What is importance of antiproteases?

A

Regulates (inactivates) enzymes activated by proteolysis–shit can get wonky fast if you don’t keep and eye on these bad boys

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2
Q

What is the inactive form of thrombin (2a)?

A

Prothrombin (2)

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3
Q

What is the final role of thrombin (2)?

A

Cleaves fibrinogen (1) to fibrin (1a)

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4
Q

Where are digestive enzymes made?

A

Salivary glands, stomach, pancreas, small intestine

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5
Q

What is the activator for pepsinogen?

How is it activated?

A

Low pH (2) of stomach acid

Spontaneously–autocatalytic

Acidic amino acids are pronated, salt bridges become broken–conformational change

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6
Q

Where are majority of zymogens produced?

A

Pancreas

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7
Q

What activates trypsinogen?

What changes in the molecule?

A

Enteropeptidase or trypsin

Active site completed following conformational change

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8
Q

What is trypsin able to activate following its activation?

A

Other trypsinogen molecules + chymotrypsin, procarboxypeptidase, proelastase

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9
Q

What is an enzyme cascade?

A

When a small amount of enzyme can cycle back and further activate its own molecules

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10
Q

How is the digestive enzyme cascade regulated?

A

Self-Regulating, enzymes destroyed by other enzymes in the pathway

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11
Q

What does floppy mean in the silly world of enzymes?

A

Unordered

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12
Q

How is chymotrypsinogen activated?

A

Trypsin cleaves a peptide bond, yielding pi-chymotrypsin, which further autocleaves itself to eventually form alpha-chymotrypsin which is held together by 2 di-sulfide bonds

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13
Q

What is formed in the final step to yield alpha-chymotrypsin?

A

New N-Terminal Amino Acid, which H-bonds of the Charge Relay System–yielding the oxyanion pocket

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14
Q

When does activation of chymotrypsin occur?

A

When cleavage allows alignment of the catalytic site

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15
Q

What inhibitor protects pancreas enzymes from self destruction? What does it act like?

A

Pancreatic Trypsin Inhibitor (PTI)

Competitive Inhibitor (gets stuck)

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16
Q

What is the cause of emphysema?

Who is at greatest risk?

A

Genetic change in alpha1AP protein, which reduces secretion. Elastase destroys tissues.

Homozygotes, or heterozygotes who smoke them marlboro reds all day, every day

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17
Q

What is the contact system?

A

Intrinsic Pathway (circulating in blood)

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18
Q

What is the damaged tissue system?

A

Extrinsic Pathway (Fast!)

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19
Q

What is the order of the Intrinsic Pathway

A 
HMWK+Kallikrein+F12
F11
F9
F8
Converge at F10
20
Q

What is the order of the Extrinsic Pathway

A

TF3
F7
Converge at F10

21
Q

What is the order of the Common Pathway

A 
F10
F5
F2 (Thrombin)
F1 (Fibrin)
F13 (Fibrin-Meshwork)
22
Q

What can increase F7?

A

F7a, F9, F10a

23
Q

What does activated kallikrein activate?

A

F12

24
Q

What does Thrombin activate?

A

F8, F5

F1i to F1a

F13 (Fibrin Cross Links)

Protein C

25
Q

What does Protein C inactivate?

A

F5

F8

26
Q

What does Fibrinogen contain many of?

What is the result?

A

Negatively charged AA

Increased repulsion and solubility

27
Q

What does Thrombin activation of Fibrinogen accomplish?

A

Peptide removal, lowering negative charge driving aggregation

28
Q

What AA does F13a act on?

A

K/Q

29
Q

What do the granules of platelets contain?

A

Clotting factors, adenine, serotonin, growth factors

30
Q

What does phos-serine on exterior surface provide?

A

Binding site for clotting factors

31
Q

What is role of vWF?

What if it is absent?

A

Links b/t platelet surface glycoprotein and ECM

Carrier for F8

Cross-links can’t form

32
Q

What limits clotting activity?

A

Dilution, liver removes factors from circulation, proteases degrade factors, plasma inhibitors block protease activity

33
Q

What is role of Antithrombin3 (AT3)?

A

Serpin inhibits thrombin by forming complex with it

34
Q

What is role of Heparin?

A

Inhibition of thrombin by increase of AT3 formation

35
Q

What is the Clot Buster?

What activates it?

A

Plasminogen

TPA (activates to Plasmin)

36
Q

What are the three critical site residues for all SERPINs?

A

His Asp Ser

All serpins HAspS same 3 sites

37
Q

What proteases require Calcium (Vitamin K)?

What is unique about them?

What does the Calcium serve as?

A

F2
F9
F10
F7

“1972”

Gla Domain of Glu residues modified to contains a second carboxyl group in their side chain – gamma-carboxyglutamate

Bridge for phospholipid binding

38
Q

What is unique about F2 in its Gla domain?

A

It is removed during activation

39
Q

What does mod of Glu to Gla require?

Is this required for activity?

A

Vitamin K

No, required to localize enzymes/substrates

40
Q

What medication is a Vitamin K antagonist?

A

Warfarin

41
Q

What is hemophilia (A/B) a disease in?

A 
A = F8 (Ay-te)
B = F9
42
Q

Aspirin

A

Inhibits Platelet Activation (irreversible)

43
Q

Clopidrogel

A

Inhibits platelet Activation (irreversible)

44
Q

Coumadin

A

Inhibits Vit K dep factors/enzymes

Warfarin discovered in 1972

45
Q

Dabigatran

A

Inhibits Thrombin

Reversible

46
Q

Heparin Sodium

A

Activates AT3 (inactivates 10/2)

47
Q

Rivaroxaban

A

Inhibits 10

“X” in middle

EOM 1 - Test 1 (16 decks)

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