respiration 5 Flashcards

(31 cards)

1
Q

lung compliance and elastance

A
  • compliance is how easily the lungs stretch during inhalation
  • elastance is ease of returning to shape on exhalation
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2
Q

surfactants

A
  • surface tension in alveolar fluid lowers compliance

- reduces surface tension by disrupting cohesive forces between water molecules

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3
Q

resistance increases/decreases with…

A

increases with length and viscosity

descreases with radius

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4
Q

airway resistance and diameter

A

as diameter increases, resistance decreases, and vice versa

  • higher resistance requires more work/energy
  • diameter is affect by nervous system , hormones, and paracrine messengers
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5
Q

bronchoconstriction

A

caused by parasympathetic nerve stimulation and histamine

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6
Q

bronchodilation

A

caused by sympathetic nerve stim, epinephrine, high CO2, and corticosteroids

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7
Q

dead space

A

air that does not participate in gas exchange

anatomical: volume of trachea and bronchi
alveolar: volume of alveoli that is not perfused

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8
Q

tidal volume

A

volume of air moved in one normal ventilatory cycle

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9
Q

alveolar ventilation

A

volume of air that enters alveoli with each resp cycle

aka VA=VT-VD

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10
Q

inspired reserve volume (IRV)

A

max inspiration beyond normal tidal volume

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11
Q

inspiratory capacity (IC)

A

VT plus IRV

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12
Q

expired reserve volume (ERV)

A

max expiration beyond normal tidal volume

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13
Q

vital capacity VC

A

VT+IRV+ERV

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14
Q

residual volume RV

A

never expired or measured

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15
Q

total lung capacity TLC

A

Vt+IRV+ERV+RV or VC+RV

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16
Q

ventilation-perfusion matching

A

efficient gas exchange at resp surface requires match of vent and blood flow, at a ratio of Va/Q; alveolar ventilation vs rate of flow
-arterioles dilate or constrict to distribute blood to well ventilated alveoli

17
Q

O2 transport, Metalloproteins

A
  • respiratory pigments used to increase oxygen carrying capacity by up to 50x
  • proteins contain metal ions which reversibly bind to oxygen
  • at tissue surface low PO2 in blood causes release of O2 down its gradient
18
Q

metalloproteins

A

3 types: hemoglobins, hemocyanins, and hemerythrins

19
Q

hemoglobins

A
  • globin protein bound to heme molecule that contains iron
  • usually within blood cells
  • appear red when oxygenated
  • myoglobin is type of hemoglobin found in muscles
  • found in vertebrates, nematodes, crustaceans, and insects
20
Q

hemocyanins

A
  • found in arthropods and molluscs
  • contain COPPER, not heme
  • dissolved in hemolymph and appears blue when oxygenated
21
Q

hemerythrins

A

found in brachiopods and some annelids

  • contains iron directly bound to protein, no heme involved
  • ususaly inside coleomic cells or muscle cells
  • appears violet-pink when oxygented
22
Q

oxygen loading

A

amount of oxygen stored on hemoglobin determind via:

  1. amount of pressure oxygen can bring to bear on the system/how much O2 is being loaded=PO22 of the plasma
  2. the affinity/ability of the carrier (hemoglobin) to carry O2=Hb=oxygen affinity of hemoglobin
23
Q

oxygen loading and PO2 of envrionment/plasma

A

high PO2 favours loading, low favours unloading

24
Q

oxygen loading and Hb affinity

A

high affinity favours loading, low affinity favours unloading

25
hyperbolic oxygen equilibrium graphs
found in myoglobin because each oxygen binds independently
26
sigmoidal oxygen equil graphs
sigmoidal because of cooperativity; hemoglobin has a higher affinity for oxygen since more oxygen bind to its heme
27
factors that affect hb affinity
pH, pCO2, aka the bohr and root effects | -temperature effect and organic modulators
28
bohr effect
higher pH, fewer H+, minimal CO2, and O2 its taken up more easily at resp surface - low pH lots of H+ and CO2 allows O2 more easily released at tissues - bohr effect is a decreased affinity due to increased CO2
29
root effect
increased H+/decreased pH decreases affinity
30
temperature shift
higher temp indicates more active tissues, thus O2 affinity must decrease to move more O2 to tissues
31
organic modulators
act as allosteric regulators, they affect the function of a protein by binding to the non-active sties -can be activators or inhibitors -important in control loops ie 2,3-DPG in mammals and reptiles lowers Hb affinity