4) RBC metabolism Flashcards

1
Q

4 things an RBC must do during its lifespan that require energy

A
  1. keep hgb in reduced form (Fe2+)
  2. operate Na-K pump to maintain volume
  3. keep membrane deformable
  4. produce NADPH
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

prinicipal, almost exclusive source of RBC energy

A

glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

4 RBC metabolic pathways

A
  • Embden-Meyerhoff pathway (glycolysis)
  • Luebering-Rapaport pathway (2,3-DPG pathway)
  • Hexose monophosphate shunt (PPP)
  • Methemoglobin reductase pathway
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

90% of glucose metabolism occurs via the…

produces what?

A

EM pathway

pyruvate or lactate, ATP, and NADH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

ATP needed in RBC for…

A
  • maintaining shape and deformability
  • operate Na/K pumps
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

NADH is needed in RBC for…

A

reduction of methemoglobin to hemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

no net energy produced from glycolysis

A

if LR pathway is used

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

accounts fo 2/3 of RBC phosphorus
chief regulator of O2 transport and delivery

A

2,3-diphosphoglycerate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

10% of RBC glucose is metabolized through the…

A

HMS/PPP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

2 ways of reducing methemoglobin

A
  • nonenzymatically via glutathione
  • enzymatically via methemoglobin reductase
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

sequence of events when RBC is exposed to oxidant drugs

A
  • GSH is oxidized to GSSG
  • Fe3+ is oxidized to Fe2+
  • sulfhydryl groups of hgb are oxidized
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

if oxidative stress continues, ———– attach themselves to the cell membrane and are removed by spleen, which can cause…

A

Heinz bodies (aggregates of oxidated globin chains)

hemolytic anemia

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

2 ways oxidation can affect RBC, and the pathway that responds

A
  1. oxidation of Fe2+ to Fe3+ (methemoglobin)—MRP
  2. oxidation of globin chains (Heinz bodies)—HMS/PPP
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

cause accumulation of H2O2

A

oxidant drugs
infection

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Hexose monophosphate shunt

H2O2 oxidizes ——- to ——- via ——-

——- is oxidized to ——-, giving GSH, via ——-

——- combines with ——- to form NADPH, via ——-

A

H2O2 oxidizes GSH to GSSG via glutathione peroxidase

NADPH is oxidized to NADP, giving GSH, via glutathione reductase

NADP combines with G6P to form NADPH, via G6PD

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

if the HMS is deficient, the amount of reduced ——– will be insufficient, and oxidants within the cell will…

A

glutathione
oxidize hgb sulfhydryl groups, leading to globin denaturation (Heinz bodies)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Methemoglobin reductase pathway

——- and methemoglobin give ——- and hemoglobin, via ——-

A

NADH and methemoglobin give NAD and hemoglobin, via methemoglobin reductase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

——% mHgb gives hypoxia and cyanosis

A

20-40%

19
Q

LR pathway gives accumulation of ———-

A

2,3-DPG

20
Q

O2 + Hgb =

A

oxyhemoglobin

21
Q

OH released from deoxyhemoglobin…

A

combines with CO2 to form carbonic acid, which then dissociates to form bicarbonate

5% of CO2 carried in solution

22
Q

3 ways of transporting CO2

A
  1. in solution (5%)
  2. direct, carbamate molecule (20%)
  3. indirect, forming carbonic acid and then bicarb in RBC, after which chloride shift occurs (70%)
23
Q

chloride shift

A

HCO3 moves out of RBC, Cl moves in

24
Q

factors that affect affinity of O2 and Hgb

A
  • pO2
  • pCO2
  • temperature
  • pH
  • 2,3-DPG
25
Q

shift from deoxyhgb to oxyhgb when…

A

3rd heme is oxygenated

26
Q

responsible for sigmoid shape

A

heme-heme interaction

27
Q

tense state
relaxed state

A

2,3-DPG present, deoxygenated

2,3-DPG expelled, increased O2 affinity

28
Q

factors that decrease Hgb affinity for O2 (right shift), allowing O2 to be released into tissues

A

↑ temperature
↑ 2,3-DPG
↓ pH (Bohr effect)
↓ pO2
↑ pCO2

29
Q

concentration of intra-erythrocytic 2,3-DPG affected mostly by…

A

pH and pO2

30
Q

during deoxygenation, —— chains pull apart, allowing 2,3-DPG to bind

A

beta

31
Q

——- and O2 are competitive

A

2,3-DPG

32
Q

p50 value

A

pO2 at which Hgb is 50% saturated with O2, under standard temp/pH conditions

33
Q

O2-Hgb affinity will be (greater/less) in rapidly metabolizing tissues

A

less

34
Q

3 abnormal hemoglobin pigments

A
  • carboxyhemoglobin (HbCO)
  • methemoglobin (Hi)
  • sulfhemoglobin (SHb)
35
Q

HbCO results in…

A

death from anoxia
cherry red blood

36
Q

toxic level of CO

A

5.0g%

37
Q

affinity for CO is ——x greater than that for O2

A

218

38
Q

2 types of methemoglobinemia

A
  • hereditary
  • acquired (most common; drug effects)
39
Q

2 types of hereditary methemoglobinemia and tx

A
  • MR enzyme deficiency—tx with ascorbic acid, methylene blue
  • HgbM, abnormal structure with enhanced tendency toward oxidation—no response to reducing agents
40
Q

SHb

A

Hgb binds sulfur rather than O2
very stable compound, lasts until RBCs die
normal RBC lifespan

41
Q

causes of SHb

A

sulfur-containing drugs
TNT explosives

42
Q

SHb (does/does not) respond to reducing agents

A

does not

43
Q

toxic SHb level

A

0.5 g%

44
Q
A

heinz bodies