Normal Erythrocytes Flashcards

1
Q

Life span of mature RBCs

A

~120 days

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2
Q

Which organ removes fragile old RBCs from circulation

A

Spleen

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3
Q

Globular haemoglobin is broken down to what?

A

Amino acids (these then enter bloodstream)

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4
Q

The haem group is converted to what?

A

Haem group (minus iron) is converted to bilirubin

-bilirubin is transported to liver and secreted into bile

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5
Q

What happens to the iron?

A

Binds to transferrin and is recycled

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6
Q

What is a proerythroblast derived from?

A

Myeloid stem cell

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7
Q

What is special about the shape of red blood cells?

A
  • diffusion distance minimised
  • surface to volume ration maximised
  • flexible membrane allows cells to squeeze in single file through capillaries
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8
Q

RBC ion balance and cell volume are actively regulated by which ENERGY-DEPENDENT PUMP?

A

Na+/K+ ATPase (the sodium pump)

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9
Q

RBC’s have no mitochondria so how do they make ATP?

A

Anaerobic glycolysis

-glucose is key fuel

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10
Q

_____ from glycolysis helps keep iron in Fe2+ state?

A

NADH from glycolysis helps keep iron in Fe2+ state (HbFe3+ cannot bind oxygen!!)

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11
Q

What is required for maintaining adequate levels of reduced glutathione? and how is it produced?

A

NADPH

-some glucose is metabolised through the hexose monophosphate shunt and this produces NADPH

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12
Q

What releases O2 from Hb?

A

2,3, BPG (2,3 bisphosphoglycerate)

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13
Q

Describe the structure of glutathione

A

Tripeptide consisting of glutamate, cysteine and glycine

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14
Q

What does reduced glutathione do?

A

Combats oxidative stress

-helps protect against he toxic effects of free radicals

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15
Q

What are free radicals?

A

Highly reactive molecules with unpaired electrons

-can lead to damage of cellular structures and enzymes

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16
Q

What is the primary intermediate in oxidative damage and what protects against its effects?

A

Primary intermediate is hydrogen peroxide (glutathione detoxifies it)

17
Q

What is needed from the pentose phosphate pathway to produce reduced glutathione?

A

NADPH

18
Q

How is carbon dioxide transported? and how is this facilitated?

A
  • dissolved in solution (10%)
  • bound to Hb: carbamino-haemoglobin (30%)
  • as bicarbonate ion (60%)

Facilitated by CARBONIC ANHYDRASE

19
Q

When fully saturated, 1g Hb will bind how many mls of oxygen?

A

1.34mls

20
Q

Normal haemoglobin concentrations in adults?

A

Males: 130-180 g/l
Females: 115-165 g/l

21
Q

Structure of adult haemoglobin

A
  • 4 globin sub-units, each containing a single haem

- each haem contains a single Fe2+ ion and can bind one O2 molecule

22
Q

What is co-operativity?

A

The influence that the binding of a ligand to one site on the molecule has on the binding of ligand to a different functional site

23
Q

What facilitates the transfer of O2 from the mother to foetus?

A
  • Foetal Hb has a higher affinity for O2 than adult

- HbF has a lower affinity for 2,3 BPG than does HbA