Plasma proteins and hemoglobin Flashcards

1
Q

Describe the 6 features of serum albumin

A
  • Synthesized in liver
  • High negative charge prevents excretion in the urine
  • Maintains oncotic pressure (burn treatment)
  • 11 pockets acts as carrier protein
  • Antioxidant
  • Transports NO
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2
Q

Alpha-1 antitrypsin (serpine, also Alpha-1 antichymotrypsin)

A
  • Serine protease inhibitor that has protective role in inflammation.
  • Inactivation by cigarette smoke leads to increased elastase activity that contributes to emphysema and COPD
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3
Q

Alpha-1 acid glycoprotein

A
  • Alpha-1 globin

- Carries basic or lipophilic compounds

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4
Q

Serum amyloid A

A
  • Alpha-1 globin

- Part of HDL secreted by liver in response to inflammatory cytokines–> recruits immune cells

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5
Q

Lipoprotein

A
  • Alpha-1 globin

- Part of HDL and LDL

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6
Q

Name the alpa-2 globins

A
  • Haptoglobin- Transports iron to spleen
  • Major urinary protein
  • Alpa-2 macroglobin- Protease inactivator
  • Alpha-2 antiplasmin
  • Ceruloplasmin- Transports copper
  • Thyroxine binding protein
  • Protein C- inactivates coagulation
  • Angiotensin- When proteolysed by ACE causes vasoconstriction
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7
Q

Proteins associated with endothelial disfunction

A
  • I-CAM-1, V-CAM-1, vWF
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8
Q

Proteins associated with Inflammation

A
  • CRP, IL-6 and 1B, TNF
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9
Q

Proteins associated with pro-coagulation

A
  • PAI-1, Fibrinogen, P selectin
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10
Q

How do O2 and CO2 bind to hemoglobin?

A
  • O2 binds to iron

- CO2 bind to amino terminus of globin

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11
Q

Describe cooperative O2 binding

A
  • Electrostatic repulsion between His and porphyrin results in non-planar structure
  • First O2 binding results in relaxation of the porphyrin structure and a planar structure allowing further binding
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12
Q

How does protonation effect hemoglobin?

A
  • Protonation induces deoxyhemoglobin
  • CO2 from tissues along with anaerobic conditions (LDH) induces deoxy hemoglobin and O2 release to the tissues.
  • BPG synthesis from shunt of glycolytic intermediates induces deoxy hemoglobin and O2 release in hypoxic conditions.
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13
Q

Describe EPO function and regulation

A
  • Cytokine that binds to receptor on RBC progenitor cells to prevent apoptosis
  • Produced in renal capillaries, production increased under hypoxic conditions.
  • Cleaved by constitutively produced hypoxia inducing factor (HIF)
  • HIF is hydroxylated and degraded in the presence of O2.
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14
Q

Where does heme biosynthesis occur?

A
  • Occurs both in the mitochondria and in the cytoplasm
  • ALAS and ferrochelatase in the mitochondria
  • ALAD in the cytoplasm
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15
Q

How does sickle cell affect RBC?

A
  • Mutation in the 6th position glutamic acid to valine
  • Val6 is exposed in deoxy hemoglobin form
  • Exposure promotes association with alpha chain and induces hemoglobin polymerization which causes sickling.
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16
Q

How is iron store within cells?

A
  • Ferritin - 24 SU multimer binds 4500 Fe3+
17
Q

What is the function of hepcidin?

A
  • Peptide generated in the liver

- BInds ferreportin in enterocytes preventing iron uptake and mobilization.

18
Q

What form of iron does transferritin bind?

A
  • Fe3+